메뉴 건너뛰기




Volumn 36, Issue 13-14, 1999, Pages 915-928

The contrasting mechanisms of serum resistance of Neisseria gonorrhoeae and group B Neisseria meningitidis

Author keywords

C4b binding protein; Capsular polysaccharide; Complement; Factor H; Neisseria gonorrhoeae; Neisseria meningitidis; Porin

Indexed keywords

COMPLEMENT MEMBRANE ATTACK COMPLEX;

EID: 18344406352     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0161-5890(99)00114-5     Document Type: Conference Paper
Times cited : (134)

References (159)
  • 1
    • 0031558247 scopus 로고    scopus 로고
    • Annual report of the Australian Meningococcal Surveillance Programme 1996
    • Anon.
    • Anon., 1997. Annual report of the Australian Meningococcal Surveillance Programme 1996. Commun. Dis. Intell. 21, 217-221.
    • (1997) Commun. Dis. Intell. , vol.21 , pp. 217-221
  • 2
    • 0032500453 scopus 로고    scopus 로고
    • Outbreaks of group B meningococcal disease - Florida, 1995 and 1997
    • Anon.
    • Anon., 1998. Outbreaks of group B meningococcal disease - Florida, 1995 and 1997. MMWR Morb. Mortal Wkly Rep. 47, 833-837.
    • (1998) MMWR Morb. Mortal Wkly Rep. , vol.47 , pp. 833-837
  • 3
    • 0014942142 scopus 로고
    • Increased susceptibility to infection associated with abnormalities of complement-mediated functions and of the third component of complement (C3)
    • Alper C.A., Abramson N., Johnston R.B. Jr, Jandl J.H., Rosen F.S. Increased susceptibility to infection associated with abnormalities of complement-mediated functions and of the third component of complement (C3). N. Engl. J. Med. 282:1970;350-354.
    • (1970) N. Engl. J. Med. , vol.282 , pp. 350-354
    • Alper, C.A.1    Abramson, N.2    Johnston R.B., Jr.3    Jandl, J.H.4    Rosen, F.S.5
  • 4
    • 0025354034 scopus 로고
    • Modification by sialic acid of Neisseria gonorrhoeae lipooligosaccharide epitope expression in human urethral exudates: An immunoelectron microscopic analysis
    • Apicella M.A., Mandrell R.E., Shero M., Wilson M.E., Griffiss J.M., Brooks G.F., Lammel C., Breen J.F., Rice P.A. Modification by sialic acid of Neisseria gonorrhoeae lipooligosaccharide epitope expression in human urethral exudates: an immunoelectron microscopic analysis. J. Infect. Dis. 162:1990;506-512.
    • (1990) J. Infect. Dis. , vol.162 , pp. 506-512
    • Apicella, M.A.1    Mandrell, R.E.2    Shero, M.3    Wilson, M.E.4    Griffiss, J.M.5    Brooks, G.F.6    Lammel, C.7    Breen, J.F.8    Rice, P.A.9
  • 7
    • 0028364359 scopus 로고
    • Polymorphism of the complement C8A and -B genes in two families with C8 beta deficiency and neisserial infections
    • Barba G.M., Kaufmann T.J., Schneider P.M., Rittner C., Brai M. Polymorphism of the complement C8A and -B genes in two families with C8 beta deficiency and neisserial infections. Clin. Immunol. Immunopathol. 72:1994;83-89.
    • (1994) Clin. Immunol. Immunopathol. , vol.72 , pp. 83-89
    • Barba, G.M.1    Kaufmann, T.J.2    Schneider, P.M.3    Rittner, C.4    Brai, M.5
  • 8
    • 0023628634 scopus 로고
    • Molecular cloning and expression of Neisseria meningitidis class 1 outer membrane protein in Escherichia coli K-12
    • Barlow A.K., Heckels J.E., Clarke I.N. Molecular cloning and expression of Neisseria meningitidis class 1 outer membrane protein in Escherichia coli K-12. Infect. Immun. 55:1987;2734-2740.
    • (1987) Infect. Immun. , vol.55 , pp. 2734-2740
    • Barlow, A.K.1    Heckels, J.E.2    Clarke, I.N.3
  • 9
    • 0024453090 scopus 로고
    • The class 1 outer membrane protein of Neisseria meningitidis: Gene sequence and structural and immunological similarities to gonococcal porins
    • Barlow A.K., Heckels J.E., Clarke I.N. The class 1 outer membrane protein of Neisseria meningitidis: gene sequence and structural and immunological similarities to gonococcal porins. Mol. Microbiol. 3:1989;131-139.
    • (1989) Mol. Microbiol. , vol.3 , pp. 131-139
    • Barlow, A.K.1    Heckels, J.E.2    Clarke, I.N.3
  • 10
    • 0242646437 scopus 로고    scopus 로고
    • Bordetella pertussis binds the human complement regulator C4BP: Role of filamentous hemagglutinin
    • Berggard K., Johnsson E., Mooi F.R., Lindahl G. Bordetella pertussis binds the human complement regulator C4BP: role of filamentous hemagglutinin. Infect. Immun. 65:1997;3638-3643.
    • (1997) Infect. Immun. , vol.65 , pp. 3638-3643
    • Berggard, K.1    Johnsson, E.2    Mooi, F.R.3    Lindahl, G.4
  • 12
    • 0000913183 scopus 로고
    • Functional and immunological properties of pathogenic neisserial surface proteins
    • M. Inouye. New York: John Wiley
    • Blake M.S., Gotschlich E.C. Functional and immunological properties of pathogenic neisserial surface proteins. Inouye M. Bacterial Outer Membranes as Model Systems. 1986;377-400 John Wiley, New York.
    • (1986) Bacterial Outer Membranes As Model Systems , pp. 377-400
    • Blake, M.S.1    Gotschlich, E.C.2
  • 13
    • 77049141169 scopus 로고
    • Serological relationship among meningococci
    • Branham S. Serological relationship among meningococci. Bacteriol. Rev. 17:1953;175-188.
    • (1953) Bacteriol. Rev. , vol.17 , pp. 175-188
    • Branham, S.1
  • 14
    • 0012618585 scopus 로고
    • Reference strains for the serologic groups of meningococcus (Neisseria meningitidis)
    • Branham S. Reference strains for the serologic groups of meningococcus (Neisseria meningitidis). Int. Bull. Bacteriol. Nomenclature Taxonomy. 8:1958;1-15.
    • (1958) Int. Bull. Bacteriol. Nomenclature Taxonomy , vol.8 , pp. 1-15
    • Branham, S.1
  • 15
    • 0021853858 scopus 로고
    • Correlation of auxotype and protein I type with expression of disease due to Neisseria gonorrhoeae
    • Brunham R.C., Plummer F., Slaney L., Rand F., DeWitt W. Correlation of auxotype and protein I type with expression of disease due to Neisseria gonorrhoeae. J. Infect. Dis. 152:1985;339-343.
    • (1985) J. Infect. Dis. , vol.152 , pp. 339-343
    • Brunham, R.C.1    Plummer, F.2    Slaney, L.3    Rand, F.4    Dewitt, W.5
  • 16
    • 0026043799 scopus 로고
    • Class-3 porin protein of Neisseria meningitidis: Cloning and structure of the gene
    • Butcher S., Sarvas M., Runeberg-Nyman K. Class-3 porin protein of Neisseria meningitidis: cloning and structure of the gene. Gene. 105:1991;125-128.
    • (1991) Gene , vol.105 , pp. 125-128
    • Butcher, S.1    Sarvas, M.2    Runeberg-Nyman, K.3
  • 17
    • 0020581162 scopus 로고
    • Confirmation of association of protein I serotype of Neisseria gonorrhoeae with ability to cause disseminated infection
    • Cannon J.G., Buchanan T.M., Sparling P.F. Confirmation of association of protein I serotype of Neisseria gonorrhoeae with ability to cause disseminated infection. Infect. Immun. 40:1983;816-819.
    • (1983) Infect. Immun. , vol.40 , pp. 816-819
    • Cannon, J.G.1    Buchanan, T.M.2    Sparling, P.F.3
  • 18
    • 0025324683 scopus 로고
    • Construction of isogenic gonococci with variable porin structure: Effects on susceptibility to human serum and antibiotics
    • Carbonetti N., Simnad V., Elkins C., Sparling P.F. Construction of isogenic gonococci with variable porin structure: effects on susceptibility to human serum and antibiotics. Mol. Microbiol. 4:1990;1009-1018.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1009-1018
    • Carbonetti, N.1    Simnad, V.2    Elkins, C.3    Sparling, P.F.4
  • 19
    • 0343313105 scopus 로고
    • Genetics of protein I of Neisseria gonorrhoeae: Construction of hybrid porins [published erratum appears in Proc. Natl. Acad. Sci. USA 1989 Feb;86(4):1317]
    • Carbonetti N.H., Simnad V.I., Seifert H.S., So M., Sparling P.F. Genetics of protein I of Neisseria gonorrhoeae: construction of hybrid porins [published erratum appears in Proc. Natl. Acad. Sci. USA 1989 Feb;86(4):1317]. Proc. Natl. Acad. Sci. USA. 85:1988;6841-6845.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6841-6845
    • Carbonetti, N.H.1    Simnad, V.I.2    Seifert, H.S.3    So, M.4    Sparling, P.F.5
  • 21
    • 0027181091 scopus 로고
    • Role of the YadA protein in prevention of opsonization of Yersinia enterocolitica by C3b molecules
    • China B., Sory M.P., N'Guyen B.T., De Bruyere M., Cornelis G.R. Role of the YadA protein in prevention of opsonization of Yersinia enterocolitica by C3b molecules. Infect. Immun. 61:1993;3129-3136.
    • (1993) Infect. Immun. , vol.61 , pp. 3129-3136
    • China, B.1    Sory, M.P.2    N'Guyen, B.T.3    De Bruyere, M.4    Cornelis, G.R.5
  • 22
    • 0033000992 scopus 로고    scopus 로고
    • Is group C meningococcal disease increasing in Europe? A report of surveillance of meningococcal infection in Europe 1993-6 European Meningitis Surveillance Group
    • Connolly M., Noah N. Is group C meningococcal disease increasing in Europe? A report of surveillance of meningococcal infection in Europe 1993-6 European Meningitis Surveillance Group. Epidemiol. Infect. 122:1999;41-49.
    • (1999) Epidemiol. Infect. , vol.122 , pp. 41-49
    • Connolly, M.1    Noah, N.2
  • 23
    • 0017639894 scopus 로고
    • Asymptomatic gonorrhea in men: Caused by gonococci with unique nutritional requirements
    • Crawford C., Knapp J.S., Hale J., Holmes K.K. Asymptomatic gonorrhea in men: caused by gonococci with unique nutritional requirements. Science. 196:1977;1352-1353.
    • (1977) Science , vol.196 , pp. 1352-1353
    • Crawford, C.1    Knapp, J.S.2    Hale, J.3    Holmes, K.K.4
  • 24
    • 0018935005 scopus 로고
    • Relative resistance of the F-42-stabilized classical pathway C3 convertase to inactivation by C4-binding protein
    • Daha M.R., van Es L.A. Relative resistance of the F-42-stabilized classical pathway C3 convertase to inactivation by C4-binding protein. J. Immunol. 125:1980;2051-2054.
    • (1980) J. Immunol. , vol.125 , pp. 2051-2054
    • Daha, M.R.1    Van Es, L.A.2
  • 25
    • 0023095705 scopus 로고
    • Familial properdin deficiency and fatal meningococcemia: Correction of the bactericidal defect by vaccination
    • Densen P., Weiler J.M., Griffiss J.M., Hoffmann L.G. Familial properdin deficiency and fatal meningococcemia: Correction of the bactericidal defect by vaccination. N. Engl. J. Med. 316:1987;922-926.
    • (1987) N. Engl. J. Med. , vol.316 , pp. 922-926
    • Densen, P.1    Weiler, J.M.2    Griffiss, J.M.3    Hoffmann, L.G.4
  • 26
    • 0032954440 scopus 로고    scopus 로고
    • Structural and evolutionary inference from molecular variation in Neisseria porins
    • Derrick J.P., Urwin R., Suker J., Feavers I.M., Maiden M.C. Structural and evolutionary inference from molecular variation in Neisseria porins. Infect. Immun. 67:1999;2406-2413.
    • (1999) Infect. Immun. , vol.67 , pp. 2406-2413
    • Derrick, J.P.1    Urwin, R.2    Suker, J.3    Feavers, I.M.4    Maiden, M.C.5
  • 27
    • 0019919737 scopus 로고
    • The meningococcus and mechanisms of pathogenicity
    • DeVoe I.W. The meningococcus and mechanisms of pathogenicity. Microbiol. Rev. 46:1982;162-190.
    • (1982) Microbiol. Rev. , vol.46 , pp. 162-190
    • Devoe, I.W.1
  • 28
    • 0033611934 scopus 로고    scopus 로고
    • Epidemic serogroup B meningococcal disease in Oregon: The evolving epidemiology of the ET-5 strain [see comments]
    • Diermayer M., Hedberg K., Hoesly F., Fischer M., Perkins B., Reeves M., Fleming D. Epidemic serogroup B meningococcal disease in Oregon: the evolving epidemiology of the ET-5 strain [see comments]. JAMA. 281:1999;1493-1497.
    • (1999) JAMA , vol.281 , pp. 1493-1497
    • Diermayer, M.1    Hedberg, K.2    Hoesly, F.3    Fischer, M.4    Perkins, B.5    Reeves, M.6    Fleming, D.7
  • 29
    • 0019795651 scopus 로고
    • Three new serogroups of Neisseria meningitidis
    • Ding S.Q., Ye R.B., Zhang H.C. Three new serogroups of Neisseria meningitidis. J. Biol. Stand. 9:1981;307-315.
    • (1981) J. Biol. Stand. , vol.9 , pp. 307-315
    • Ding, S.Q.1    Ye, R.B.2    Zhang, H.C.3
  • 30
    • 0019787613 scopus 로고
    • Protein I of Neisseria gonorrhoeae outer membrane is a porin
    • Douglas J.T., Lee M.D., Nikaido H. Protein I of Neisseria gonorrhoeae outer membrane is a porin. FEMS Microbiol. Lett. 12:1981;305-309.
    • (1981) FEMS Microbiol. Lett. , vol.12 , pp. 305-309
    • Douglas, J.T.1    Lee, M.D.2    Nikaido, H.3
  • 32
    • 0020086091 scopus 로고
    • Capsular sialic acid prevents activation of the alternative complement pathway by type III, group B streptococci
    • Edwards M.S., Kasper D.L., Jennings H.J., Baker C.J., Nicholson-Weller A. Capsular sialic acid prevents activation of the alternative complement pathway by type III, group B streptococci. J. Immunol. 128:1982;1278-1283.
    • (1982) J. Immunol. , vol.128 , pp. 1278-1283
    • Edwards, M.S.1    Kasper, D.L.2    Jennings, H.J.3    Baker, C.J.4    Nicholson-Weller, A.5
  • 33
    • 0020611492 scopus 로고
    • Prevalence of congenital or acquired complement deficiency in patients with sporadic meningocococcal disease
    • Ellison R.T.D., Kohler P.F., Curd J.G., Judson F.N., Reller L.B. Prevalence of congenital or acquired complement deficiency in patients with sporadic meningocococcal disease. N. Engl. J. Med. 308:1983;913-916.
    • (1983) N. Engl. J. Med. , vol.308 , pp. 913-916
    • Ellison, R.T.D.1    Kohler, P.F.2    Curd, J.G.3    Judson, F.N.4    Reller, L.B.5
  • 34
    • 1842299263 scopus 로고    scopus 로고
    • Sialylation of Neisseria meningitidis lipooligosaccharide inhibits serum bactericidal activity by masking lacto-N-neotetraose
    • Estabrook M.M., Griffiss J.M., Jarvis G.A. Sialylation of Neisseria meningitidis lipooligosaccharide inhibits serum bactericidal activity by masking lacto-N-neotetraose. Infect. Immun. 65:1997;4436-4444.
    • (1997) Infect. Immun. , vol.65 , pp. 4436-4444
    • Estabrook, M.M.1    Griffiss, J.M.2    Jarvis, G.A.3
  • 35
    • 0014289492 scopus 로고
    • Prevalence of meningococcal serogroups and description of three new groups
    • Evans J.R., Artenstein M.S., Hunter D.H. Prevalence of meningococcal serogroups and description of three new groups. Am. J. Epidemiol. 87:1968;643-646.
    • (1968) Am. J. Epidemiol. , vol.87 , pp. 643-646
    • Evans, J.R.1    Artenstein, M.S.2    Hunter, D.H.3
  • 36
    • 0011647956 scopus 로고
    • Regulation by membrane sialic acid of beta1H-dependent decay-dissociation of amplification C3 convertase of the alternative complement pathway
    • Fearon D.T. Regulation by membrane sialic acid of beta1H-dependent decay-dissociation of amplification C3 convertase of the alternative complement pathway. Proc. Natl. Acad. Sci. USA. 75:1978;1971-1975.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 1971-1975
    • Fearon, D.T.1
  • 37
    • 0011188401 scopus 로고
    • Activation of the alternative complement pathway due to resistance of zymosan-bound amplification convertase to endogenous regulatory mechanisms
    • Fearon D.T., Austen K.F. Activation of the alternative complement pathway due to resistance of zymosan-bound amplification convertase to endogenous regulatory mechanisms. Proc. Natl. Acad. Sci. USA. 74:1977;1683-1687.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 1683-1687
    • Fearon, D.T.1    Austen, K.F.2
  • 38
    • 0027379446 scopus 로고
    • Complement deficiency states and meningococcal disease
    • Figueroa J., Andreoni J., Densen P. Complement deficiency states and meningococcal disease. Immunol. Res. 12:1993;295-311.
    • (1993) Immunol. Res. , vol.12 , pp. 295-311
    • Figueroa, J.1    Andreoni, J.2    Densen, P.3
  • 39
    • 0024446314 scopus 로고
    • Complement deficiencies in patients over ten years old with meningococcal disease due to uncommon serogroups [see comments]
    • Fijen C.A., Kuijper E.J., Hannema A.J., Sjoholm A.G., van Putten J.P. Complement deficiencies in patients over ten years old with meningococcal disease due to uncommon serogroups [see comments]. Lancet. 2:1989;585-588.
    • (1989) Lancet , vol.2 , pp. 585-588
    • Fijen, C.A.1    Kuijper, E.J.2    Hannema, A.J.3    Sjoholm, A.G.4    Van Putten, J.P.5
  • 40
    • 0028804370 scopus 로고
    • Location of the complement factor H binding site on streptococcal M6 protein
    • Fischetti V.A., Horstmann R.D., Pancholi V. Location of the complement factor H binding site on streptococcal M6 protein. Infect. Immun. 63:1995;149-153.
    • (1995) Infect. Immun. , vol.63 , pp. 149-153
    • Fischetti, V.A.1    Horstmann, R.D.2    Pancholi, V.3
  • 41
    • 0026218329 scopus 로고
    • The surface structure seen on gonococci after treatment with CMP-NANA is due to sialylation of surface lipopolysaccharide previously described as a 'capsule'
    • Fox A.J., Curry A., Jones D.M., Demarco de Hormaeche R., Parsons N.J., Cole J.A., Smith H. The surface structure seen on gonococci after treatment with CMP-NANA is due to sialylation of surface lipopolysaccharide previously described as a 'capsule'. Microb. Pathog. 11:1991;199-210.
    • (1991) Microb. Pathog. , vol.11 , pp. 199-210
    • Fox, A.J.1    Curry, A.2    Jones, D.M.3    Demarco De Hormaeche, R.4    Parsons, N.J.5    Cole, J.A.6    Smith, H.7
  • 42
    • 0025793736 scopus 로고
    • An epidemiologically valuable typing method for Neisseria meningitidis by analysis of restriction fragment length polymorphisms
    • Fox A.J., Jones D.M., Gray S.J., Caugant D.A., Saunders N.A. An epidemiologically valuable typing method for Neisseria meningitidis by analysis of restriction fragment length polymorphisms. J. Med. Microbiol. 34:1991;265-270.
    • (1991) J. Med. Microbiol. , vol.34 , pp. 265-270
    • Fox, A.J.1    Jones, D.M.2    Gray, S.J.3    Caugant, D.A.4    Saunders, N.A.5
  • 43
    • 0024831397 scopus 로고
    • Serum killing of meningococci and several other gram-negative bacterial species is not decreased by incubating them with cytidine 5'- monophospho-N-acetyl neuraminic acid [letter]
    • Fox A.J., Jones D.M., Scotland S.M., Rowe B., Smith A., Brown M.R., Fitzgeorge R.G., Baskerville A., Parsons N.J., Cole J.A., et al. Serum killing of meningococci and several other gram-negative bacterial species is not decreased by incubating them with cytidine 5'- monophospho-N-acetyl neuraminic acid [letter]. Microb. Pathog. 7:1989;317-318.
    • (1989) Microb. Pathog. , vol.7 , pp. 317-318
    • Fox, A.J.1    Jones, D.M.2    Scotland, S.M.3    Rowe, B.4    Smith, A.5    Brown, M.R.6    Fitzgeorge, R.G.7    Baskerville, A.8    Parsons, N.J.9    Cole, J.A.10
  • 44
    • 0010606499 scopus 로고
    • Noncapsular surface antigens of Neisseria meningitidis
    • L. Weinstein, & B. Fields. New York: Stratton International Medical Book Corporation
    • Frasch C., Gotschlich E. Noncapsular surface antigens of Neisseria meningitidis. Weinstein L., Fields B. Seminars in Infectious Diseases. 1979;304-337 Stratton International Medical Book Corporation, New York.
    • (1979) Seminars in Infectious Diseases , pp. 304-337
    • Frasch, C.1    Gotschlich, E.2
  • 45
    • 0342827809 scopus 로고
    • Proposed schema for identification of serotypes of Neisseria meningitidis
    • G. Schoolnik. Washington, DC: American Society for Microbiology
    • Frasch C., Zollinger W., Poolman J. Proposed schema for identification of serotypes of Neisseria meningitidis. Schoolnik G. The Pathogenic Neisseria. 1985;519-524 American Society for Microbiology, Washington, DC.
    • (1985) The Pathogenic Neisseria , pp. 519-524
    • Frasch, C.1    Zollinger, W.2    Poolman, J.3
  • 46
    • 0039313678 scopus 로고
    • Molecular characterization and expression in Escherichia coli of the gene complex encoding the polysaccharide capsule of Neisseria meningitidis group B
    • Frosch M., Weisgerber C., Meyer T.F. Molecular characterization and expression in Escherichia coli of the gene complex encoding the polysaccharide capsule of Neisseria meningitidis group B. Proc. Natl. Acad. Sci. USA. 86:1989;1669-1673.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1669-1673
    • Frosch, M.1    Weisgerber, C.2    Meyer, T.F.3
  • 47
    • 0018073707 scopus 로고
    • Human C4-binding protein. II. Role in proteolysis of C4b by C3b- inactivator
    • Fujita T., Gigli I., Nussenzweig V. Human C4-binding protein. II. Role in proteolysis of C4b by C3b- inactivator. J. Exp. Med. 148:1978;1044-1051.
    • (1978) J. Exp. Med. , vol.148 , pp. 1044-1051
    • Fujita, T.1    Gigli, I.2    Nussenzweig, V.3
  • 48
    • 0018418530 scopus 로고
    • The role of C4-binding protein and beta 1H in proteolysis of C4b and C3b
    • Fujita T., Nussenzweig V. The role of C4-binding protein and beta 1H in proteolysis of C4b and C3b. J. Exp. Med. 150:1979;267-276.
    • (1979) J. Exp. Med. , vol.150 , pp. 267-276
    • Fujita, T.1    Nussenzweig, V.2
  • 49
    • 0020645909 scopus 로고
    • Interaction of C4-binding protein with cell-bound C4b. A quantitative analysis of binding and the role of C4-binding protein in proteolysis of cell-bound C4b
    • Fujita T., Tamura N. Interaction of C4-binding protein with cell-bound C4b. A quantitative analysis of binding and the role of C4-binding protein in proteolysis of cell-bound C4b. J. Exp. Med. 157:1983;1239-1251.
    • (1983) J. Exp. Med. , vol.157 , pp. 1239-1251
    • Fujita, T.1    Tamura, N.2
  • 50
    • 0011369135 scopus 로고
    • Modulation of the classical pathway C3 convertase by plasma proteins C4 binding protein and C3b inactivator
    • Gigli I., Fujita T., Nussenzweig V. Modulation of the classical pathway C3 convertase by plasma proteins C4 binding protein and C3b inactivator. Proc. Natl. Acad. Sci. USA. 76:1979;6596-6600.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 6596-6600
    • Gigli, I.1    Fujita, T.2    Nussenzweig, V.3
  • 51
    • 0029961489 scopus 로고    scopus 로고
    • Cloning of the lipooligosaccharide alpha-2,3-sialyltransferase from the bacterial pathogens Neisseria meningitidis and Neisseria gonorrhoeae
    • Gilbert M., Watson D.C., Cunningham A.M., Jennings M.P., Young N.M., Wakarchuk W.W. Cloning of the lipooligosaccharide alpha-2,3-sialyltransferase from the bacterial pathogens Neisseria meningitidis and Neisseria gonorrhoeae. J. Biol. Chem. 271:1996;28271-28276.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28271-28276
    • Gilbert, M.1    Watson, D.C.2    Cunningham, A.M.3    Jennings, M.P.4    Young, N.M.5    Wakarchuk, W.W.6
  • 53
    • 0018294072 scopus 로고
    • Phenotypically determined resistance of Neisseria gonorrhoeae to normal human serum: Environmental factors in subcutaneous chambers in guinea pigs
    • Goldner M., Penn C.W., Sanyal S.C., Veale D.R., Smith H. Phenotypically determined resistance of Neisseria gonorrhoeae to normal human serum: environmental factors in subcutaneous chambers in guinea pigs. J. Gen. Microbiol. 114:1979;169-177.
    • (1979) J. Gen. Microbiol. , vol.114 , pp. 169-177
    • Goldner, M.1    Penn, C.W.2    Sanyal, S.C.3    Veale, D.R.4    Smith, H.5
  • 54
    • 0023394345 scopus 로고
    • Physical heterogeneity of Neisserial lipooligosaccharides reflects oligosaccharides that differ in apparent molecular weight, chemical composition, and antigenic expression
    • Griffiss J.M., O'Brien J.P., Yamasaki R., Williams G.D., Rice P.A., Schneider H. Physical heterogeneity of Neisserial lipooligosaccharides reflects oligosaccharides that differ in apparent molecular weight, chemical composition, and antigenic expression. Infect. Immun. 55:1987;1792-1800.
    • (1987) Infect. Immun. , vol.55 , pp. 1792-1800
    • Griffiss, J.M.1    O'Brien, J.P.2    Yamasaki, R.3    Williams, G.D.4    Rice, P.A.5    Schneider, H.6
  • 56
    • 0029806568 scopus 로고    scopus 로고
    • Immunogenicity of Neisseria gonorrhoeae lipooligosaccharide epitope 2C7, widely expressed in vivo with no immunochemical similarity to human glycosphingolipids [published erratum appears in J. Infect. Dis. 1997 Apr;175(4):1027]
    • Gulati S., McQuillen D.P., Mandrell R.E., Jani D.B., Rice P.A. Immunogenicity of Neisseria gonorrhoeae lipooligosaccharide epitope 2C7, widely expressed in vivo with no immunochemical similarity to human glycosphingolipids [published erratum appears in J. Infect. Dis. 1997 Apr;175(4):1027]. J. Infect. Dis. 174:1996;1223-1237.
    • (1996) J. Infect. Dis. , vol.174 , pp. 1223-1237
    • Gulati, S.1    McQuillen, D.P.2    Mandrell, R.E.3    Jani, D.B.4    Rice, P.A.5
  • 57
    • 0343698324 scopus 로고    scopus 로고
    • Factor H interactions with sialylated gonococcal lipooligosaccharide
    • (abstract)
    • Gulati S., Ram S., McQuillen D.P., Pangburn M.K., Rice P.A. Factor H interactions with sialylated gonococcal lipooligosaccharide. Mol. Immunol. 35:1998;398. (abstract).
    • (1998) Mol. Immunol. , vol.35 , pp. 398
    • Gulati, S.1    Ram, S.2    McQuillen, D.P.3    Pangburn, M.K.4    Rice, P.A.5
  • 58
    • 0028972229 scopus 로고
    • Anti-Gal binds to pili of Neisseria meningitidis: The immunoglobulin A isotype blocks complement-mediated killing
    • Hamadeh R.M., Estabrook M.M., Zhou P., Jarvis G.A., Griffiss J.M. Anti-Gal binds to pili of Neisseria meningitidis: the immunoglobulin A isotype blocks complement-mediated killing. Infect. Immun. 63:1995;4900-4906.
    • (1995) Infect. Immun. , vol.63 , pp. 4900-4906
    • Hamadeh, R.M.1    Estabrook, M.M.2    Zhou, P.3    Jarvis, G.A.4    Griffiss, J.M.5
  • 59
    • 0028364942 scopus 로고
    • Contribution of genes from the capsule gene complex (cps) to lipooligosaccharide biosynthesis and serum resistance in Neisseria meningitidis
    • Hammerschmidt S., Birkholz C., Zahringer U., Robertson B.D., van Putten J., Ebeling O., Frosch M. Contribution of genes from the capsule gene complex (cps) to lipooligosaccharide biosynthesis and serum resistance in Neisseria meningitidis. Mol. Microbiol. 11:1994;885-896.
    • (1994) Mol. Microbiol. , vol.11 , pp. 885-896
    • Hammerschmidt, S.1    Birkholz, C.2    Zahringer, U.3    Robertson, B.D.4    Van Putten, J.5    Ebeling, O.6    Frosch, M.7
  • 61
    • 0019448014 scopus 로고
    • Host modification of Sindbis virus sialic acid content influences alternative complement pathway activation and virus clearance
    • Hirsch R.L., Griffin D.E., Winkelstein J.A. Host modification of Sindbis virus sialic acid content influences alternative complement pathway activation and virus clearance. J. Immunol. 127:1981;1740-1743.
    • (1981) J. Immunol. , vol.127 , pp. 1740-1743
    • Hirsch, R.L.1    Griffin, D.E.2    Winkelstein, J.A.3
  • 62
    • 0020651387 scopus 로고
    • Natural immunity to Sindbis virus is influenced by host tissue sialic acid content
    • Hirsch R.L., Griffin D.E., Winkelstein J.A. Natural immunity to Sindbis virus is influenced by host tissue sialic acid content. Proc. Natl. Acad. Sci. USA. 80:1983;548-550.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 548-550
    • Hirsch, R.L.1    Griffin, D.E.2    Winkelstein, J.A.3
  • 63
    • 0001809806 scopus 로고    scopus 로고
    • Gonococcal infections in the adult
    • K.K. Holmes, P.F. Sparling, P.A. Mardh, P.J. Wiesner, J.W. Cates, S.M. Lemon, & W.E. Stamm. New York: McGraw-Hill
    • Hook J.E.W., Handsfield H.H. Gonococcal infections in the adult. Holmes K.K., Sparling P.F., Mardh P.A., Wiesner P.J., Cates J.W., Lemon S.M., Stamm W.E. Sexually Transmitted Diseases. 1999;451-466 McGraw-Hill, New York.
    • (1999) Sexually Transmitted Diseases , pp. 451-466
    • Hook, J.E.W.1    Handsfield, H.H.2
  • 64
    • 0343017792 scopus 로고
    • Antiphagocytic activity of streptococcal M protein: Selective binding of complement control protein factor H
    • Horstmann R.D., Sievertsen H.J., Knobloch J., Fischetti V.A. Antiphagocytic activity of streptococcal M protein: selective binding of complement control protein factor H. Proc. Natl. Acad. Sci. USA. 85:1988;1657-1661.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1657-1661
    • Horstmann, R.D.1    Sievertsen, H.J.2    Knobloch, J.3    Fischetti, V.A.4
  • 65
    • 0018150104 scopus 로고
    • Serum bactericidal action and activation of the classic and alternate complement pathways by Neisseria gonorrhoeae
    • Ingwer I., Petersen B.H., Brooks G. Serum bactericidal action and activation of the classic and alternate complement pathways by Neisseria gonorrhoeae. J. Lab. Clin. Med. 92:1978;211-220.
    • (1978) J. Lab. Clin. Med. , vol.92 , pp. 211-220
    • Ingwer, I.1    Petersen, B.H.2    Brooks, G.3
  • 66
    • 0030740792 scopus 로고    scopus 로고
    • Community immunization programme in response to an outbreak of invasive Neisseria meningitidis serogroup C infection in the Trent region of England 1995-1996 [see comments]
    • Irwin D.J., Miller J.M., Milner P.C., Patterson T., Richards R.G., Williams D.A., Insley C.A., Stuart J.M. Community immunization programme in response to an outbreak of invasive Neisseria meningitidis serogroup C infection in the Trent region of England 1995-1996 [see comments]. J. Public Health Med. 19:1997;162-170.
    • (1997) J. Public Health Med. , vol.19 , pp. 162-170
    • Irwin, D.J.1    Miller, J.M.2    Milner, P.C.3    Patterson, T.4    Richards, R.G.5    Williams, D.A.6    Insley, C.A.7    Stuart, J.M.8
  • 67
    • 0031914961 scopus 로고    scopus 로고
    • Activation of complement by mannose-binding lectin on isogenic mutants of Neisseria meningitidis serogroup
    • Jack D.L., Dodds A.W., Anwar N., Ison C.A., Law A., Frosch M., Turner M.W., Klein N.J. Activation of complement by mannose-binding lectin on isogenic mutants of Neisseria meningitidis serogroup. Br. J. Immunol. 160:1998;1346-1353.
    • (1998) Br. J. Immunol. , vol.160 , pp. 1346-1353
    • Jack, D.L.1    Dodds, A.W.2    Anwar, N.3    Ison, C.A.4    Law, A.5    Frosch, M.6    Turner, M.W.7    Klein, N.J.8
  • 68
    • 0028230242 scopus 로고
    • Analysis of C3 deposition and degradation on Neisseria meningitidis and Neisseria gonorrhoeae
    • Jarvis G.A. Analysis of C3 deposition and degradation on Neisseria meningitidis and Neisseria gonorrhoeae. Infect. Immun. 62:1994;1755-1760.
    • (1994) Infect. Immun. , vol.62 , pp. 1755-1760
    • Jarvis, G.A.1
  • 69
    • 0029042369 scopus 로고
    • Recognition and control of neisserial infection by antibody and complement
    • Jarvis G.A. Recognition and control of neisserial infection by antibody and complement. Trends Microbiol. 3:1995;198-201.
    • (1995) Trends Microbiol. , vol.3 , pp. 198-201
    • Jarvis, G.A.1
  • 70
    • 0024448296 scopus 로고
    • Human IgA1 initiates complement-mediated killing of Neisseria meningitidis
    • Jarvis G.A., Griffiss J.M. Human IgA1 initiates complement-mediated killing of Neisseria meningitidis. J. Immunol. 143:1989;1703-1709.
    • (1989) J. Immunol. , vol.143 , pp. 1703-1709
    • Jarvis, G.A.1    Griffiss, J.M.2
  • 71
    • 0023085007 scopus 로고
    • Sialic acid of group B Neisseria meningitidis regulates alternative complement pathway activation
    • Jarvis G.A., Vedros N.A. Sialic acid of group B Neisseria meningitidis regulates alternative complement pathway activation. Infect. Immun. 55:1987;174-180.
    • (1987) Infect. Immun. , vol.55 , pp. 174-180
    • Jarvis, G.A.1    Vedros, N.A.2
  • 72
    • 0025914739 scopus 로고
    • The bacterial porin superfamily: Sequence alignment and structure prediction
    • Jeanteur D., Lakey J.H., Pattus F. The bacterial porin superfamily: sequence alignment and structure prediction. Mol. Microbiol. 5:1991;2153-2164.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2153-2164
    • Jeanteur, D.1    Lakey, J.H.2    Pattus, F.3
  • 73
    • 0030267784 scopus 로고    scopus 로고
    • A highly variable region in members of the streptococcal M protein family binds the human complement regulator C4BP
    • Johnsson E., Thern A., Dahlback B., Heden L.O., Wikstrom M., Lindahl G. A highly variable region in members of the streptococcal M protein family binds the human complement regulator C4BP. J. Immunol. 157:1996;3021-3029.
    • (1996) J. Immunol. , vol.157 , pp. 3021-3029
    • Johnsson, E.1    Thern, A.2    Dahlback, B.3    Heden, L.O.4    Wikstrom, M.5    Lindahl, G.6
  • 74
    • 0020061925 scopus 로고
    • Studies on the mechanism of bacterial resistance to complement-mediated killing. I. Terminal complement components are deposited and released from Salmonella minnesota S218 without causing bacterial death
    • Joiner K.A., Hammer C.H., Brown E.J., Cole R.J., Frank M.M. Studies on the mechanism of bacterial resistance to complement-mediated killing. I. Terminal complement components are deposited and released from Salmonella minnesota S218 without causing bacterial death. J. Exp. Med. 155:1982;797-808.
    • (1982) J. Exp. Med. , vol.155 , pp. 797-808
    • Joiner, K.A.1    Hammer, C.H.2    Brown, E.J.3    Cole, R.J.4    Frank, M.M.5
  • 75
    • 0020058726 scopus 로고
    • Studies on the mechanism of bacterial resistance to complement-mediated killing. II. C8 and C9 release C5b67 from the surface of Salmonella minnesota S218 because the terminal complex does not insert into the bacterial outer membrane
    • Joiner K.A., Hammer C.H., Brown E.J., Frank M.M. Studies on the mechanism of bacterial resistance to complement-mediated killing. II. C8 and C9 release C5b67 from the surface of Salmonella minnesota S218 because the terminal complex does not insert into the bacterial outer membrane. J. Exp. Med. 155:1982;809-819.
    • (1982) J. Exp. Med. , vol.155 , pp. 809-819
    • Joiner, K.A.1    Hammer, C.H.2    Brown, E.J.3    Frank, M.M.4
  • 76
    • 0001556106 scopus 로고    scopus 로고
    • Each of the three binding sites on factor H interacts with a distinct site on C3b
    • (abstract)
    • Jokiranta T.S., Hellwage J., Koistinen V., Zipfel P.F., Meri S. Each of the three binding sites on factor H interacts with a distinct site on C3b. Mol. Immunol. 35:1998;360. (abstract).
    • (1998) Mol. Immunol. , vol.35 , pp. 360
    • Jokiranta, T.S.1    Hellwage, J.2    Koistinen, V.3    Zipfel, P.F.4    Meri, S.5
  • 77
    • 0030590494 scopus 로고    scopus 로고
    • Analysis of the recognition mechanism of the alternative pathway of complement by monoclonal anti-factor H antibodies: Evidence for multiple interactions between H and surface bound C3b
    • Jokiranta T.S., Zipfel P.F., Hakulinen J., Kuhn S., Pangburn M.K., Tamerius J.D., Meri S. Analysis of the recognition mechanism of the alternative pathway of complement by monoclonal anti-factor H antibodies: evidence for multiple interactions between H and surface bound C3b. FEBS Lett. 393:1996;297-302.
    • (1996) FEBS Lett. , vol.393 , pp. 297-302
    • Jokiranta, T.S.1    Zipfel, P.F.2    Hakulinen, J.3    Kuhn, S.4    Pangburn, M.K.5    Tamerius, J.D.6    Meri, S.7
  • 78
  • 79
    • 0031597437 scopus 로고    scopus 로고
    • The (α2→8)-linked polysialic acid capsule and lipooligosaccharide structure both contribute to the ability of serogroup B Neisseria meningitidis to resist the bactericidal activity of normal human serum
    • Kahler C.M., Martin L.E., Shih G.C., Rahman M.M., Carlson R.W., Stephens D.S. The (α2→8)-linked polysialic acid capsule and lipooligosaccharide structure both contribute to the ability of serogroup B Neisseria meningitidis to resist the bactericidal activity of normal human serum. Infect. Immun. 66:1998;5939-5947.
    • (1998) Infect. Immun. , vol.66 , pp. 5939-5947
    • Kahler, C.M.1    Martin, L.E.2    Shih, G.C.3    Rahman, M.M.4    Carlson, R.W.5    Stephens, D.S.6
  • 80
    • 0018317786 scopus 로고
    • Human alternative complement pathway: Membrane-associated sialic acid regulates the competition between B and β1H for cell-bound C3b
    • Kazatchkine M.D., Fearon D.T., Austen K.F. Human alternative complement pathway: membrane-associated sialic acid regulates the competition between B and β1H for cell-bound C3b. J. Immunol. 122:1979;75-81.
    • (1979) J. Immunol. , vol.122 , pp. 75-81
    • Kazatchkine, M.D.1    Fearon, D.T.2    Austen, K.F.3
  • 82
    • 0033063964 scopus 로고    scopus 로고
    • Protein H, an antiphagocytic surface protein in Streptococcus pyogenes
    • Kihlberg B.M., Collin M., Olsen A., Bjorck L. Protein H, an antiphagocytic surface protein in Streptococcus pyogenes. Infect. Immun. 67:1999;1708-1714.
    • (1999) Infect. Immun. , vol.67 , pp. 1708-1714
    • Kihlberg, B.M.1    Collin, M.2    Olsen, A.3    Bjorck, L.4
  • 83
    • 0009694416 scopus 로고
    • Overview of epidemiological and clinical applications of auxotype/serovar classification of Neisseria gonorrhoeae
    • G.K. Schoolnik. Washington, DC: American Society for Microbiology
    • Knapp J.S., Sandstrom E.G., Holmes K.K. Overview of epidemiological and clinical applications of auxotype/serovar classification of Neisseria gonorrhoeae. Schoolnik G.K. The Pathogenic Neisseriae. 1985;6-12 American Society for Microbiology, Washington, DC.
    • (1985) The Pathogenic Neisseriae , pp. 6-12
    • Knapp, J.S.1    Sandstrom, E.G.2    Holmes, K.K.3
  • 84
    • 0021235884 scopus 로고
    • Serological classification of Neisseria gonorrhoeae with use of monoclonal antibodies to gonococcal outer membrane protein I
    • Knapp J.S., Tam M.R., Nowinski R.C., Holmes K.K., Sandstrom E.G. Serological classification of Neisseria gonorrhoeae with use of monoclonal antibodies to gonococcal outer membrane protein I. J. Infect. Dis. 150:1984;44-48.
    • (1984) J. Infect. Dis. , vol.150 , pp. 44-48
    • Knapp, J.S.1    Tam, M.R.2    Nowinski, R.C.3    Holmes, K.K.4    Sandstrom, E.G.5
  • 85
    • 0026470620 scopus 로고
    • Meningococcal septicaemia in a C6-deficient patient and effects of plasma transfusion on lipopolysaccharide release
    • Lehner P.J., Davies K.A., Walport M.J., Cope A.P., Wurzner R., Orren A., Morgan B.P., Cohen J. Meningococcal septicaemia in a C6-deficient patient and effects of plasma transfusion on lipopolysaccharide release. Lancet. 340:1992;1379-1381.
    • (1992) Lancet , vol.340 , pp. 1379-1381
    • Lehner, P.J.1    Davies, K.A.2    Walport, M.J.3    Cope, A.P.4    Wurzner, R.5    Orren, A.6    Morgan, B.P.7    Cohen, J.8
  • 86
    • 0022979311 scopus 로고
    • Reactogenicity and immunogenicity of a quadrivalent combined meningococcal polysaccharide vaccine in children
    • Lepow M.L., Beeler J., Randolph M., Samuelson J.S., Hankins W.A. Reactogenicity and immunogenicity of a quadrivalent combined meningococcal polysaccharide vaccine in children. J. Infect. Dis. 154:1986;1033-1036.
    • (1986) J. Infect. Dis. , vol.154 , pp. 1033-1036
    • Lepow, M.L.1    Beeler, J.2    Randolph, M.3    Samuelson, J.S.4    Hankins, W.A.5
  • 87
    • 84886624669 scopus 로고
    • Absence of the sixth component of complement in a patient with repeated episodes of meningococcal meningitis
    • Lim D., Gewurz A., Lint T.F., Ghaze M., Sepheri B., Gewurz H. Absence of the sixth component of complement in a patient with repeated episodes of meningococcal meningitis. J. Pediatr. 89:1976;42-47.
    • (1976) J. Pediatr. , vol.89 , pp. 42-47
    • Lim, D.1    Gewurz, A.2    Lint, T.F.3    Ghaze, M.4    Sepheri, B.5    Gewurz, H.6
  • 88
    • 0032194160 scopus 로고    scopus 로고
    • Membrane cofactor protein: Importance of N- And O-glycosylation for complement regulatory function
    • Liszewski M.K., Leung M.K., Atkinson J.P. Membrane cofactor protein: importance of N- and O-glycosylation for complement regulatory function. J. Immunol. 161:1998;3711-3718.
    • (1998) J. Immunol. , vol.161 , pp. 3711-3718
    • Liszewski, M.K.1    Leung, M.K.2    Atkinson, J.P.3
  • 89
    • 0000097235 scopus 로고    scopus 로고
    • Spread of Neisseria meningitidis group A clone III-I meningitis epidemic into Zambia
    • Luo N., Perera C., Holton J., Ayles H., Zumla A. Spread of Neisseria meningitidis group A clone III-I meningitis epidemic into Zambia. J. Infect. 36:1998;141-143.
    • (1998) J. Infect. , vol.36 , pp. 141-143
    • Luo, N.1    Perera, C.2    Holton, J.3    Ayles, H.4    Zumla, A.5
  • 90
    • 0027818696 scopus 로고
    • Demonstration of lipooligosaccharide immunotype and capsule as virulence factors for Neisseria meningitidis using an infant mouse intranasal infection model
    • Mackinnon F.G., Borrow R., Gorringe A.R., Fox A.J., Jones D.M., Robinson A. Demonstration of lipooligosaccharide immunotype and capsule as virulence factors for Neisseria meningitidis using an infant mouse intranasal infection model. Microb. Pathog. 15:1993;359-366.
    • (1993) Microb. Pathog. , vol.15 , pp. 359-366
    • Mackinnon, F.G.1    Borrow, R.2    Gorringe, A.R.3    Fox, A.J.4    Jones, D.M.5    Robinson, A.6
  • 91
    • 0342393009 scopus 로고    scopus 로고
    • The molecular basis of serum resistance in group B meningococci: Inhibition of membrane attack complex insertion by capsular polysaccharide
    • (abstract)
    • Mackinnon F.G., Gulati S., Gorringe A., Oppermann M., Rice P.A., Ram S. The molecular basis of serum resistance in group B meningococci: inhibition of membrane attack complex insertion by capsular polysaccharide. Mol. Immunol. 36:1999;295. (abstract).
    • (1999) Mol. Immunol. , vol.36 , pp. 295
    • Mackinnon, F.G.1    Gulati, S.2    Gorringe, A.3    Oppermann, M.4    Rice, P.A.5    Ram, S.6
  • 94
    • 0019838281 scopus 로고
    • Induction of phenotypically determined resistance of Neisseria gonorrhoeae to human serum by factors in human serum
    • Martin P.M., Patel P.V., Parsons N.J., Smith H. Induction of phenotypically determined resistance of Neisseria gonorrhoeae to human serum by factors in human serum. J. Gen. Microbiol. 127:1981;213-217.
    • (1981) J. Gen. Microbiol. , vol.127 , pp. 213-217
    • Martin, P.M.1    Patel, P.V.2    Parsons, N.J.3    Smith, H.4
  • 95
    • 0021961279 scopus 로고
    • Influence of nutrient limitation and low pH on serogroup B Neisseria meningitidis capsular polysaccharide levels: Correlation with virulence for mice
    • Masson L., Holbein B.E. Influence of nutrient limitation and low pH on serogroup B Neisseria meningitidis capsular polysaccharide levels: correlation with virulence for mice. Infect. Immun. 47:1985;465-471.
    • (1985) Infect. Immun. , vol.47 , pp. 465-471
    • Masson, L.1    Holbein, B.E.2
  • 96
    • 0020064405 scopus 로고
    • Virulence linked to polysaccharide production in serogroup B Neisseria meningitidis
    • Masson L., Holbein B.E., Ashton F.E. Virulence linked to polysaccharide production in serogroup B Neisseria meningitidis. FEMS Microbiol. Lett. 13:1982;187-190.
    • (1982) FEMS Microbiol. Lett. , vol.13 , pp. 187-190
    • Masson, L.1    Holbein, B.E.2    Ashton, F.E.3
  • 97
    • 0032952645 scopus 로고    scopus 로고
    • Complement processing and immunoglobulin binding to Neisseria gonorrhoeae determined in vitro simulates in vivo effects
    • McQuillen D.P., Gulati S., Ram S., Turner A.K., Jani D.B., Heeren T.C., Rice P.A. Complement processing and immunoglobulin binding to Neisseria gonorrhoeae determined in vitro simulates in vivo effects. J. Infect. Dis. 179:1999;124-135.
    • (1999) J. Infect. Dis. , vol.179 , pp. 124-135
    • McQuillen, D.P.1    Gulati, S.2    Ram, S.3    Turner, A.K.4    Jani, D.B.5    Heeren, T.C.6    Rice, P.A.7
  • 98
    • 0028260801 scopus 로고
    • Regulation of alternative pathway complement activation by glycosaminoglycans: Specificity of the polyanion binding site on factor H
    • Meri S., Pangburn M.K. Regulation of alternative pathway complement activation by glycosaminoglycans: specificity of the polyanion binding site on factor H. Biochem. Biophys. Res. Commun. 198:1994;52-59.
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 52-59
    • Meri, S.1    Pangburn, M.K.2
  • 99
    • 0028097419 scopus 로고
    • Expression of the L8 lipopolysaccharide determinant increases the sensitivity of Neisseria meningitidis to serum bactericidal activity
    • Moran E.E., Brandt B.L., Zollinger W.D. Expression of the L8 lipopolysaccharide determinant increases the sensitivity of Neisseria meningitidis to serum bactericidal activity. Infect. Immun. 62:1994;5290-5295.
    • (1994) Infect. Immun. , vol.62 , pp. 5290-5295
    • Moran, E.E.1    Brandt, B.L.2    Zollinger, W.D.3
  • 100
    • 0026757312 scopus 로고
    • Recurrence of neisserial meningococcemia due to deficiency of terminal complement component
    • Morris J.T., Kelly W.J. Recurrence of neisserial meningococcemia due to deficiency of terminal complement component. South. Med. J. 85:1992;1030-1031.
    • (1992) South. Med. J. , vol.85 , pp. 1030-1031
    • Morris, J.T.1    Kelly, W.J.2
  • 101
    • 0024239495 scopus 로고
    • Cytidine 5′-monophospho-N-acetylneuraminic acid or a related compound is the low Mr factor from human red blood cells which induces gonococcal resistance to killing by human serum
    • Nairn C.A., Cole J.A., Patel P.V., Parsons N.J., Fox J.E., Smith H. Cytidine 5′-monophospho-N-acetylneuraminic acid or a related compound is the low Mr factor from human red blood cells which induces gonococcal resistance to killing by human serum. J. Gen. Microbiol. 134:1988;3295-3306.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 3295-3306
    • Nairn, C.A.1    Cole, J.A.2    Patel, P.V.3    Parsons, N.J.4    Fox, J.E.5    Smith, H.6
  • 102
    • 0009761898 scopus 로고
    • [Study of ninety strains of serogroup A Neisseria meningitidis isolated from cerebrospinal fluid (25) and rhinopharynx (65) in Morocco (December 1989-April 1990)]
    • Nejmi S., Belhaj A., Guibourdenche M., Riou J.Y. [Study of ninety strains of serogroup A Neisseria meningitidis isolated from cerebrospinal fluid (25) and rhinopharynx (65) in Morocco (December 1989-April 1990)]. Pathol. Biol. (Paris). 40:1992;993-998.
    • (1992) Pathol. Biol. (Paris) , vol.40 , pp. 993-998
    • Nejmi, S.1    Belhaj, A.2    Guibourdenche, M.3    Riou, J.Y.4
  • 103
    • 0024459070 scopus 로고
    • Complement deficiencies in selected groups of patients with meningococcal disease
    • Nielsen H.E., Koch C., Magnussen P., Lind I. Complement deficiencies in selected groups of patients with meningococcal disease. Scand. J. Infect. Dis. 21:1989;389-396.
    • (1989) Scand. J. Infect. Dis. , vol.21 , pp. 389-396
    • Nielsen, H.E.1    Koch, C.2    Magnussen, P.3    Lind, I.4
  • 104
    • 0021089302 scopus 로고
    • Disseminated gonococcal infection: A prospective analysis of 49 patients and a review of pathophysiology and immune mechanisms
    • O'Brien J.P., Goldenberg D.L., Rice P.A. Disseminated gonococcal infection: a prospective analysis of 49 patients and a review of pathophysiology and immune mechanisms. Medicine. 62:1983;395-406.
    • (1983) Medicine , vol.62 , pp. 395-406
    • O'Brien, J.P.1    Goldenberg, D.L.2    Rice, P.A.3
  • 105
    • 0028884489 scopus 로고
    • Classical complement pathway activation on nucleated cells. Role of factor H in the control of deposited C3b
    • Ollert M.W., David K., Bredehorst R., Vogel C.W. Classical complement pathway activation on nucleated cells. Role of factor H in the control of deposited C3b. J. Immunol. 155:1995;4955-4962.
    • (1995) J. Immunol. , vol.155 , pp. 4955-4962
    • Ollert, M.W.1    David, K.2    Bredehorst, R.3    Vogel, C.W.4
  • 106
    • 0026101134 scopus 로고
    • A sensitive enzyme immunoassay for the quantitation of human C5a/C5a(desArganaphylatoxin using a monoclonal antibody with specificity for a neoepitope
    • Oppermann M., Schulze M., Gotze O. A sensitive enzyme immunoassay for the quantitation of human C5a/C5a(desArganaphylatoxin using a monoclonal antibody with specificity for a neoepitope. Complement Inflamm. 8:1991;13-24.
    • (1991) Complement Inflamm. , vol.8 , pp. 13-24
    • Oppermann, M.1    Schulze, M.2    Gotze, O.3
  • 107
    • 0027966121 scopus 로고
    • Characterization of strains of Neisseria meningitidis recovered from complement-sufficient and complement-deficient patients in the Western Cape Province, South Africa
    • Orren A., Caugant D.A., Fijen C.A., Dankert J., van Schalkwyk E.J., Poolman J.T., Coetzee G.J. Characterization of strains of Neisseria meningitidis recovered from complement-sufficient and complement-deficient patients in the Western Cape Province, South Africa. J. Clin. Microbiol. 32:1994;2185-2191.
    • (1994) J. Clin. Microbiol. , vol.32 , pp. 2185-2191
    • Orren, A.1    Caugant, D.A.2    Fijen, C.A.3    Dankert, J.4    Van Schalkwyk, E.J.5    Poolman, J.T.6    Coetzee, G.J.7
  • 108
    • 0017704496 scopus 로고
    • Human complement C3b inactivator: Isolation, characterization, and demonstration of an absolute requirement for the serum protein beta1H for cleavage of C3b and C4b in solution
    • Pangburn M.K., Schreiber R.D., Muller-Eberhard H.J. Human complement C3b inactivator: isolation, characterization, and demonstration of an absolute requirement for the serum protein beta1H for cleavage of C3b and C4b in solution. J. Exp. Med. 146:1977;257-270.
    • (1977) J. Exp. Med. , vol.146 , pp. 257-270
    • Pangburn, M.K.1    Schreiber, R.D.2    Muller-Eberhard, H.J.3
  • 109
    • 0027119577 scopus 로고
    • The serum resistance of gonococci in the majority of urethral exudates is due to sialylated lipopolysaccharide seen as a surface coat
    • Parsons N.J., Curry A., Fox A.J., Jones D.M., Cole J.A., Smith H. The serum resistance of gonococci in the majority of urethral exudates is due to sialylated lipopolysaccharide seen as a surface coat. FEMS Microbiol. Lett. 69:1992;295-299.
    • (1992) FEMS Microbiol. Lett. , vol.69 , pp. 295-299
    • Parsons, N.J.1    Curry, A.2    Fox, A.J.3    Jones, D.M.4    Cole, J.A.5    Smith, H.6
  • 110
    • 0024246109 scopus 로고
    • Cytidine 5′-monophospho-N-acetyl neuraminic acid and a low molecular weight factor from human blood cells induce lipopolysaccharide alteration in gonococci when conferring resistance to killing by human serum
    • Parsons N.J., Patel P.V., Tan E.L., Andrade J.R., Nairn C.A., Goldner M., Cole J.A., Smith H. Cytidine 5′-monophospho-N-acetyl neuraminic acid and a low molecular weight factor from human blood cells induce lipopolysaccharide alteration in gonococci when conferring resistance to killing by human serum. Microb. Pathog. 5:1988;303-309.
    • (1988) Microb. Pathog. , vol.5 , pp. 303-309
    • Parsons, N.J.1    Patel, P.V.2    Tan, E.L.3    Andrade, J.R.4    Nairn, C.A.5    Goldner, M.6    Cole, J.A.7    Smith, H.8
  • 112
    • 0021690463 scopus 로고
    • Red blood cells, a source of factors which induce Neisseria gonorrhoeae to resistance to complement-mediated killing by human serum
    • Patel P.V., Martin P.M., Goldner M., Parsons N.J., Smith H. Red blood cells, a source of factors which induce Neisseria gonorrhoeae to resistance to complement-mediated killing by human serum. J. Gen. Microbiol. 130:1984;2767-2770.
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 2767-2770
    • Patel, P.V.1    Martin, P.M.2    Goldner, M.3    Parsons, N.J.4    Smith, H.5
  • 113
    • 0021719821 scopus 로고
    • Fractionation of guinea pig serum for an inducer of gonococcal resistance to killing by human serum: Active fractions containing glucopeptides similar to those from human red blood cells
    • Patel P.V., Veale D.R., Fox J.E., Martin P.M., Parsons N.J., Smith H. Fractionation of guinea pig serum for an inducer of gonococcal resistance to killing by human serum: active fractions containing glucopeptides similar to those from human red blood cells. J. Gen. Microbiol. 130:1984;2757-2766.
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 2757-2766
    • Patel, P.V.1    Veale, D.R.2    Fox, J.E.3    Martin, P.M.4    Parsons, N.J.5    Smith, H.6
  • 114
    • 0023866809 scopus 로고
    • Protein changes associated with induced resistance of Neisseria gonorrhoeae to killing by human serum are relatively minor
    • Patel P.V., Martin P.M., Tan E.L., Nairn C.A., Parsons N.J., Goldner M., Smith H. Protein changes associated with induced resistance of Neisseria gonorrhoeae to killing by human serum are relatively minor. J. Gen. Microbiol. 134:1988;499-507.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 499-507
    • Patel, P.V.1    Martin, P.M.2    Tan, E.L.3    Nairn, C.A.4    Parsons, N.J.5    Goldner, M.6    Smith, H.7
  • 115
    • 0017239786 scopus 로고
    • Human deficiency of the eighth component of complement. The requirement of C8 for serum Neisseria gonorrhoeae bactericidal activity
    • Petersen B.H., Graham J.A., Brooks G.F. Human deficiency of the eighth component of complement. The requirement of C8 for serum Neisseria gonorrhoeae bactericidal activity. J. Clin. Invest. 57:1976;283-290.
    • (1976) J. Clin. Invest. , vol.57 , pp. 283-290
    • Petersen, B.H.1    Graham, J.A.2    Brooks, G.F.3
  • 116
    • 0028979185 scopus 로고
    • Direct interaction of complement factor H with the C1 domain of HIV type 1 glycoprotein 120
    • Pinter C., Siccardi A.G., Longhi R., Clivio A. Direct interaction of complement factor H with the C1 domain of HIV type 1 glycoprotein 120. AIDS Res. Hum. Retroviruses. 11:1995;577-588.
    • (1995) AIDS Res. Hum. Retroviruses , vol.11 , pp. 577-588
    • Pinter, C.1    Siccardi, A.G.2    Longhi, R.3    Clivio, A.4
  • 117
    • 0029082458 scopus 로고
    • HIV glycoprotein 41 and complement factor H interact with each other and share functional as well as antigenic homology
    • Pinter C., Siccardi A.G., Lopalco L., Longhi R., Clivio A. HIV glycoprotein 41 and complement factor H interact with each other and share functional as well as antigenic homology. AIDS Res. Hum. Retroviruses. 11:1995;971-980.
    • (1995) AIDS Res. Hum. Retroviruses , vol.11 , pp. 971-980
    • Pinter, C.1    Siccardi, A.G.2    Lopalco, L.3    Longhi, R.4    Clivio, A.5
  • 118
    • 0032055135 scopus 로고    scopus 로고
    • The C-terminus of factor H: Monoclonal antibodies inhibit heparin binding and identify epitopes common to factor H and factor H-related proteins
    • Prodinger W.M., Hellwage J., Spruth M., Dierich M.P., Zipfel P.F. The C-terminus of factor H: monoclonal antibodies inhibit heparin binding and identify epitopes common to factor H and factor H-related proteins. Biochem. J. 331:1998;41-47.
    • (1998) Biochem. J. , vol.331 , pp. 41-47
    • Prodinger, W.M.1    Hellwage, J.2    Spruth, M.3    Dierich, M.P.4    Zipfel, P.F.5
  • 119
    • 0006809878 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae regulate the classical pathway by directly binding C4-binding protein
    • (abstract)
    • Ram S., McQuillen D.P., Boden R., Gulati S., Pangburn M.K., Rice P.A. Neisseria gonorrhoeae regulate the classical pathway by directly binding C4-binding protein. Mol. Immunol. 35:1998;398. (abstract).
    • (1998) Mol. Immunol. , vol.35 , pp. 398
    • Ram, S.1    McQuillen, D.P.2    Boden, R.3    Gulati, S.4    Pangburn, M.K.5    Rice, P.A.6
  • 120
    • 0032541390 scopus 로고    scopus 로고
    • Binding of complement factor H to loop 5 of porin protein 1A: A molecular mechanism of serum resistance of non-sialylated Neisseria gonorrhoeae
    • Ram S., McQuillen D.P., Gulati S., Elkins C., Pangburn M.K., Rice P.A. Binding of complement factor H to loop 5 of porin protein 1A: a molecular mechanism of serum resistance of non-sialylated Neisseria gonorrhoeae. J. Exp. Med. 188:1998;671-680.
    • (1998) J. Exp. Med. , vol.188 , pp. 671-680
    • Ram, S.1    McQuillen, D.P.2    Gulati, S.3    Elkins, C.4    Pangburn, M.K.5    Rice, P.A.6
  • 121
    • 0032473556 scopus 로고    scopus 로고
    • A novel sialic acid binding site on factor H mediates serum resistance of sialylated Neisseria gonorrhoeae
    • Ram S., Sharma A.K., Simpson S.D., Gulati S., McQuillen D.P., Pangburn M.K., Rice P.A. A novel sialic acid binding site on factor H mediates serum resistance of sialylated Neisseria gonorrhoeae. J. Exp. Med. 187:1998;743-752.
    • (1998) J. Exp. Med. , vol.187 , pp. 743-752
    • Ram, S.1    Sharma, A.K.2    Simpson, S.D.3    Gulati, S.4    McQuillen, D.P.5    Pangburn, M.K.6    Rice, P.A.7
  • 122
    • 0343698316 scopus 로고    scopus 로고
    • Interactions between Neisseria gonorrhoeae and C4b-binding protein: A molecular basis for gonococcal serum resistance
    • (abstract)
    • Ram S., Gulati S., McQuillen D.P., Boden R., Elkins C., Pangburn M.K., Rice P.A. Interactions between Neisseria gonorrhoeae and C4b-binding protein: a molecular basis for gonococcal serum resistance. Mol. Immunol. 36:1999;297. (abstract).
    • (1999) Mol. Immunol. , vol.36 , pp. 297
    • Ram, S.1    Gulati, S.2    McQuillen, D.P.3    Boden, R.4    Elkins, C.5    Pangburn, M.K.6    Rice, P.A.7
  • 124
    • 0024521898 scopus 로고
    • Molecular basis for serum resistance in Neisseria gonorrhoeae
    • Rice P.A. Molecular basis for serum resistance in Neisseria gonorrhoeae. Clin. Microbiol. Rev. 2S:1989;S112-S117.
    • (1989) Clin. Microbiol. Rev. , vol.2
    • Rice, P.A.1
  • 125
    • 0019449551 scopus 로고
    • Clinical manifestations of disseminated infection caused by Neisseria gonorrhoeae are linked to differences in bactericidal reactivity of infecting strains
    • Rice P.A., Goldenberg D.L. Clinical manifestations of disseminated infection caused by Neisseria gonorrhoeae are linked to differences in bactericidal reactivity of infecting strains. Ann. Intern. Med. 95:1981;175-178.
    • (1981) Ann. Intern. Med. , vol.95 , pp. 175-178
    • Rice, P.A.1    Goldenberg, D.L.2
  • 126
    • 0031561575 scopus 로고    scopus 로고
    • A college outbreak of group C meningococcal infection: How widely should investigation and prophylaxis extend?
    • Riordan T. A college outbreak of group C meningococcal infection: how widely should investigation and prophylaxis extend? Commun. Dis. Rep. CDR Rev. 7:1997;R5-R9.
    • (1997) Commun. Dis. Rep. CDR Rev. , vol.7
    • Riordan, T.1
  • 127
    • 0023875503 scopus 로고
    • The complete amino acid sequence of human complement factor H
    • Ripoche J., Day A.J., Harris T.J., Sim R.B. The complete amino acid sequence of human complement factor H. Biochem. J. 249:1988;593-602.
    • (1988) Biochem. J. , vol.249 , pp. 593-602
    • Ripoche, J.1    Day, A.J.2    Harris, T.J.3    Sim, R.B.4
  • 128
    • 0023877213 scopus 로고
    • Chronic meningococcal meningitis. An association with C5 deficiency
    • Rosen M.S., Lorber B., Myers A.R. Chronic meningococcal meningitis. An association with C5 deficiency. Arch. Intern. Med. 148:1988;1441-1442.
    • (1988) Arch. Intern. Med. , vol.148 , pp. 1441-1442
    • Rosen, M.S.1    Lorber, B.2    Myers, A.R.3
  • 129
    • 0028559266 scopus 로고
    • Regulation of C3 deposition on gp120 coated CD4 positive cells by decay accelerating factor and factor H
    • Sadlon T.A., Parker S.J., Gordon D.L. Regulation of C3 deposition on gp120 coated CD4 positive cells by decay accelerating factor and factor H. Immunol. Cell Biol. 72:1994;461-470.
    • (1994) Immunol. Cell Biol. , vol.72 , pp. 461-470
    • Sadlon, T.A.1    Parker, S.J.2    Gordon, D.L.3
  • 130
    • 0019915784 scopus 로고
    • Serology of Neisseria gonorrhoeae: Coagglutination serogroups WI and WII/III correspond to different outer membrane protein I molecules
    • Sandstrom E.G., Chen K.C., Buchanan T.M. Serology of Neisseria gonorrhoeae: coagglutination serogroups WI and WII/III correspond to different outer membrane protein I molecules. Infect. Immun. 38:1982;462-470.
    • (1982) Infect. Immun. , vol.38 , pp. 462-470
    • Sandstrom, E.G.1    Chen, K.C.2    Buchanan, T.M.3
  • 132
    • 0023883116 scopus 로고
    • Instability of expression of lipooligosaccharides and their epitopes in Neisseria gonorrhoeae
    • Schneider H., Hammack C.A., Apicella M.A., Griffiss J.M. Instability of expression of lipooligosaccharides and their epitopes in Neisseria gonorrhoeae. Infect. Immun. 56:1988;942-946.
    • (1988) Infect. Immun. , vol.56 , pp. 942-946
    • Schneider, H.1    Hammack, C.A.2    Apicella, M.A.3    Griffiss, J.M.4
  • 133
    • 0027447582 scopus 로고
    • Meningococcal disease in The Netherlands 1958-1990: A steady increase in the incidence since 1982 partially caused by new serotypes and subtypes of Neisseria meningitidis
    • Scholten R.J., Bijlmer H.A., Poolman J.T., Kuipers B., Caugant D.A., Van Alphen L., Dankert J., Valkenburg H.A. Meningococcal disease in The Netherlands 1958-1990: a steady increase in the incidence since 1982 partially caused by new serotypes and subtypes of Neisseria meningitidis. Clin. Infect. Dis. 16:1993;237-246.
    • (1993) Clin. Infect. Dis. , vol.16 , pp. 237-246
    • Scholten, R.J.1    Bijlmer, H.A.2    Poolman, J.T.3    Kuipers, B.4    Caugant, D.A.5    Van Alphen, L.6    Dankert, J.7    Valkenburg, H.A.8
  • 134
    • 0028284219 scopus 로고
    • Biologically active recombinant human complement factor H: Synthesis and secretion by the baculovirus system
    • Sharma A.K., Pangburn M.K. Biologically active recombinant human complement factor H: synthesis and secretion by the baculovirus system. Gene. 143:1994;301-302.
    • (1994) Gene , vol.143 , pp. 301-302
    • Sharma, A.K.1    Pangburn, M.K.2
  • 135
    • 0029763437 scopus 로고    scopus 로고
    • Identification of three physically and functionally distinct binding sites for C3b in human complement factor H by deletion mutagenesis
    • Sharma A.K., Pangburn M.K. Identification of three physically and functionally distinct binding sites for C3b in human complement factor H by deletion mutagenesis. Proc. Natl. Acad. Sci. USA. 93:1996;10996-11001.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10996-11001
    • Sharma, A.K.1    Pangburn, M.K.2
  • 136
    • 0019776981 scopus 로고
    • Pattern of degradation of human complement fragment, C3b
    • Sim E., Wood A.B., Hsiung L.M., Sim R.B. Pattern of degradation of human complement fragment, C3b. FEBS Lett. 132:1981;55-60.
    • (1981) FEBS Lett. , vol.132 , pp. 55-60
    • Sim, E.1    Wood, A.B.2    Hsiung, L.M.3    Sim, R.B.4
  • 137
    • 51249194327 scopus 로고
    • Serological typing of meningococci by means of microprecipitation
    • Slaterus K. Serological typing of meningococci by means of microprecipitation. Antonie Van Leeuwenhoek. 27:1961;304-315.
    • (1961) Antonie Van Leeuwenhoek , vol.27 , pp. 304-315
    • Slaterus, K.1
  • 138
    • 0028906959 scopus 로고
    • Sequence evolution of the porB gene of Neisseria gonorrhoeae and Neisseria meningitidis: Evidence of positive Darwinian selection
    • Smith N.H., Maynard Smith J., Spratt B.G. Sequence evolution of the porB gene of Neisseria gonorrhoeae and Neisseria meningitidis: evidence of positive Darwinian selection. Mol. Biol. Evol. 12:1995;363-370.
    • (1995) Mol. Biol. Evol. , vol.12 , pp. 363-370
    • Smith, N.H.1    Maynard, S.J.2    Spratt, B.G.3
  • 139
    • 0024385632 scopus 로고
    • Another Swedish family with complete properdin deficiency: Association with fulminant meningococcal disease in one male family member
    • Soderstrom C., Sjoholm A.G., Svensson R., Ostenson S. Another Swedish family with complete properdin deficiency: association with fulminant meningococcal disease in one male family member. Scand. J. Infect. Dis. 21:1989;259-265.
    • (1989) Scand. J. Infect. Dis. , vol.21 , pp. 259-265
    • Soderstrom, C.1    Sjoholm, A.G.2    Svensson, R.3    Ostenson, S.4
  • 141
    • 0000517003 scopus 로고
    • Biology of Neisseria gonorrhoeae
    • K.K. Holmes, P.A. Mardh, P.F. Sparling, P.J. Wiesner, J.W. Cates, S.M. Lemon, & W.E. Stamm. New York: McGraw-Hill
    • Sparling P.F. Biology of Neisseria gonorrhoeae. Holmes K.K., Mardh P.A., Sparling P.F., Wiesner P.J., Cates J.W., Lemon S.M., Stamm W.E. Sexually Transmitted Diseases. 1990;McGraw-Hill, New York.
    • (1990) Sexually Transmitted Diseases
    • Sparling, P.F.1
  • 142
    • 0028833387 scopus 로고
    • Interaction of several complement proteins with gp120 and gp41, the two envelope glycoproteins of HIV-1
    • Stoiber H., Ebenbichler C., Schneider R., Janatova J., Dierich M.P. Interaction of several complement proteins with gp120 and gp41, the two envelope glycoproteins of HIV-1. Aids. 9:1995;19-26.
    • (1995) Aids , vol.9 , pp. 19-26
    • Stoiber, H.1    Ebenbichler, C.2    Schneider, R.3    Janatova, J.4    Dierich, M.P.5
  • 143
    • 0029059046 scopus 로고
    • Human complement proteins C3b, C4b, factor H and properdin react with specific sites in gp120 and gp41, the envelope proteins of HIV-1
    • Stoiber H., Schneider R., Janatova J., Dierich M.P. Human complement proteins C3b, C4b, factor H and properdin react with specific sites in gp120 and gp41, the envelope proteins of HIV-1. Immunobiology. 193:1995;98-113.
    • (1995) Immunobiology , vol.193 , pp. 98-113
    • Stoiber, H.1    Schneider, R.2    Janatova, J.3    Dierich, M.P.4
  • 144
    • 0022639918 scopus 로고
    • Lipopolysaccharide alteration is associated with induced resistance of Neisseria gonorrhoeae to killing by human serum
    • Tan E.L., Patel P.V., Parsons N.J., Martin P.M., Smith H. Lipopolysaccharide alteration is associated with induced resistance of Neisseria gonorrhoeae to killing by human serum. J. Gen. Microbiol. 132:1986;1407-1413.
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 1407-1413
    • Tan, E.L.1    Patel, P.V.2    Parsons, N.J.3    Martin, P.M.4    Smith, H.5
  • 145
    • 0027930729 scopus 로고
    • Role of sialic acid in the resistance of Trypanosoma cruzi trypomastigotes to complement
    • Tomlinson S., Pontes de Carvalho L.C., Vandekerckhove F., Nussenzweig V. Role of sialic acid in the resistance of Trypanosoma cruzi trypomastigotes to complement. J. Immunol. 153:1994;3141-3147.
    • (1994) J. Immunol. , vol.153 , pp. 3141-3147
    • Tomlinson, S.1    Pontes De Carvalho, L.C.2    Vandekerckhove, F.3    Nussenzweig, V.4
  • 146
    • 0025951590 scopus 로고
    • Eight lipooligosaccharides of Neisseria meningitidis react with a monoclonal antibody which binds lacto-N-neotetraose (Gal β 1-4GlcNAc β 1-3Gal β 1-4Glc)
    • Tsai C.M., Civin C.I. Eight lipooligosaccharides of Neisseria meningitidis react with a monoclonal antibody which binds lacto-N-neotetraose (Gal β 1-4GlcNAc β 1-3Gal β 1-4Glc). Infect. Immun. 59:1991;3604-3609.
    • (1991) Infect. Immun. , vol.59 , pp. 3604-3609
    • Tsai, C.M.1    Civin, C.I.2
  • 147
    • 0019506074 scopus 로고
    • Factors affecting the induction of phenotypically determined serum resistance of Neisseria gonorrhoeae grown in media containing serum or its diffusible components
    • Veale D.R., Penn C.W., Smith H. Factors affecting the induction of phenotypically determined serum resistance of Neisseria gonorrhoeae grown in media containing serum or its diffusible components. J. Gen. Microbiol. 122:1981;235-245.
    • (1981) J. Gen. Microbiol. , vol.122 , pp. 235-245
    • Veale, D.R.1    Penn, C.W.2    Smith, H.3
  • 148
    • 0030668781 scopus 로고    scopus 로고
    • Functional characterization of an isogenic meningococcal alpha-2,3- sialyltransferase mutant: The role of lipooligosaccharide sialylation for serum resistance in serogroup B meningococci
    • Vogel U., Claus H., Heinze G., Frosch M. Functional characterization of an isogenic meningococcal alpha-2,3- sialyltransferase mutant: the role of lipooligosaccharide sialylation for serum resistance in serogroup B meningococci. Med. Microbiol. Immunol. (Berl.). 186:1997;159-166.
    • (1997) Med. Microbiol. Immunol. (Berl.) , vol.186 , pp. 159-166
    • Vogel, U.1    Claus, H.2    Heinze, G.3    Frosch, M.4
  • 149
    • 0030748949 scopus 로고    scopus 로고
    • Complement factor C3 deposition and serum resistance in isogenic capsule and lipooligosaccharide sialic acid mutants of serogroup B Neisseria meningitidis
    • Vogel U., Weinberger A., Frank R.A.M., Kohl J., Atkinson J.P., Frosch M. Complement factor C3 deposition and serum resistance in isogenic capsule and lipooligosaccharide sialic acid mutants of serogroup B Neisseria meningitidis. Infect. Immun. 65:1997;4022-4029.
    • (1997) Infect. Immun. , vol.65 , pp. 4022-4029
    • Vogel, U.1    Weinberger, A.2    Frank, R.A.M.3    Kohl, J.4    Atkinson, J.P.5    Frosch, M.6
  • 150
    • 0030748949 scopus 로고    scopus 로고
    • Complement factor C3 deposition and serum resistance in isogenic capsule and lipooligosaccharide sialic acid mutants of serogroup B Neisseria meningitidis
    • Vogel U., Weinberger A., Frank R., Muller A., Kohl J., Atkinson J.P., Frosch M. Complement factor C3 deposition and serum resistance in isogenic capsule and lipooligosaccharide sialic acid mutants of serogroup B Neisseria meningitidis. Infect. Immun. 65:1997;4022-4029.
    • (1997) Infect. Immun. , vol.65 , pp. 4022-4029
    • Vogel, U.1    Weinberger, A.2    Frank, R.3    Muller, A.4    Kohl, J.5    Atkinson, J.P.6    Frosch, M.7
  • 151
    • 0032957239 scopus 로고    scopus 로고
    • Role of lipopolysaccharide sialylation in serum resistance of serogroup B and C meningococcal disease isolates
    • Vogel U., Claus H., Heinze G., Frosch M. Role of lipopolysaccharide sialylation in serum resistance of serogroup B and C meningococcal disease isolates. Infect. Immun. 67:1999;954-957.
    • (1999) Infect. Immun. , vol.67 , pp. 954-957
    • Vogel, U.1    Claus, H.2    Heinze, G.3    Frosch, M.4
  • 152
    • 0029742453 scopus 로고    scopus 로고
    • Sialic acids of both the capsule and the sialylated lipooligosaccharide of Neisseria meningitis serogroup B are prerequisites for virulence of meningococci in the infant rat
    • Vogel U., Hammerschmidt S., Frosch M. Sialic acids of both the capsule and the sialylated lipooligosaccharide of Neisseria meningitis serogroup B are prerequisites for virulence of meningococci in the infant rat. Med. Microbiol. Immunol. (Berl.). 185:1996;81-87.
    • (1996) Med. Microbiol. Immunol. (Berl.) , vol.185 , pp. 81-87
    • Vogel, U.1    Hammerschmidt, S.2    Frosch, M.3
  • 153
    • 0014962331 scopus 로고
    • Gonococci in urethral exudates possess a virulence factor lost on subculture
    • Ward M.E., Watt P.J., Glynn A.A. Gonococci in urethral exudates possess a virulence factor lost on subculture. Nature. 227:1970;382-384.
    • (1970) Nature , vol.227 , pp. 382-384
    • Ward, M.E.1    Watt, P.J.2    Glynn, A.A.3
  • 154
    • 0027120718 scopus 로고
    • Sequence analysis and relationships between meningococcal class 3 serotype proteins and other porins from pathogenic and non-pathogenic Neisseria species
    • Ward M.J., Lambden P.R., Heckels J.E. Sequence analysis and relationships between meningococcal class 3 serotype proteins and other porins from pathogenic and non-pathogenic Neisseria species. FEMS Microbiol Lett. 73:1992;283-289.
    • (1992) FEMS Microbiol Lett. , vol.73 , pp. 283-289
    • Ward, M.J.1    Lambden, P.R.2    Heckels, J.E.3
  • 155
    • 0012042656 scopus 로고
    • Control of the amplification convertase of complement by the plasma protein beta1H
    • Weiler J.M., Daha M.R., Austen K.F., Fearon D.T. Control of the amplification convertase of complement by the plasma protein beta1H. Proc. Natl. Acad. Sci. USA. 73:1976;3268-3272.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 3268-3272
    • Weiler, J.M.1    Daha, M.R.2    Austen, K.F.3    Fearon, D.T.4
  • 156
    • 0017139872 scopus 로고
    • Modulation of the alternative complement pathways by beta 1 H globulin
    • Whaley K., Ruddy S. Modulation of the alternative complement pathways by beta 1 H globulin. J. Exp. Med. 144:1976;1147-1163.
    • (1976) J. Exp. Med. , vol.144 , pp. 1147-1163
    • Whaley, K.1    Ruddy, S.2
  • 157
    • 0013488655 scopus 로고    scopus 로고
    • Sialylation of LOS inhibits gonococcal killing primarily through an effect on classical pathway activation
    • W.D. Zollinger, C.E. Frasch, & C.D. Deal. Baltimore, MD: National Institutes of Health
    • Zaleski A., Densen P. Sialylation of LOS inhibits gonococcal killing primarily through an effect on classical pathway activation. Zollinger W.D., Frasch C.E., Deal C.D. Abstracts of the Tenth International Pathogenic Neisseria Conference. 1996;114 National Institutes of Health, Baltimore, MD.
    • (1996) Abstracts of the Tenth International Pathogenic Neisseria Conference , pp. 114
    • Zaleski, A.1    Densen, P.2
  • 158
    • 0032974746 scopus 로고    scopus 로고
    • Factor H and disease: A complement regulator affects vital body functions [In Process Citation]
    • Zipfel P.F., Hellwage J., Friese M.A., Hegasy G., Jokiranta S.T., Meri S. Factor H and disease: a complement regulator affects vital body functions [In Process Citation]. Mol. Immunol. 36:1999;241-248.
    • (1999) Mol. Immunol. , vol.36 , pp. 241-248
    • Zipfel, P.F.1    Hellwage, J.2    Friese, M.A.3    Hegasy, G.4    Jokiranta, S.T.5    Meri, S.6
  • 159
    • 0020665394 scopus 로고
    • Importance of complement source in bactericidal activity of human antibody and murine monoclonal antibody to meningococcal group B polysaccharide
    • Zollinger W.D., Mandrell R.E. Importance of complement source in bactericidal activity of human antibody and murine monoclonal antibody to meningococcal group B polysaccharide. Infect. Immun. 40:1983;257-264.
    • (1983) Infect. Immun. , vol.40 , pp. 257-264
    • Zollinger, W.D.1    Mandrell, R.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.