메뉴 건너뛰기




Volumn 44, Issue 3, 2014, Pages 742-751

Yersinia pestis Ail recruitment of C4b-binding protein leads to factor I-mediated inactivation of covalently and noncovalently bound C4b

Author keywords

Ail; C4b binding protein; Complement; Yersinia

Indexed keywords

COMPLEMENT COMPONENT C4; COMPLEMENT COMPONENT C4B; COMPLEMENT COMPONENT C4B BINDING PROTEIN; FIBRINOGEN; MONOCLONAL ANTIBODY; MUTANT PROTEIN; OUTER MEMBRANE PROTEIN; PROTEIN AIL; SERINE PROTEINASE; UNCLASSIFIED DRUG; AIL PROTEIN, YERSINIA PESTIS; BLOCKING ANTIBODY; C4BPA PROTEIN, HUMAN; PROTEIN BINDING; RECOMBINANT PROTEIN; VIRULENCE FACTOR;

EID: 84896050071     PISSN: 00142980     EISSN: 15214141     Source Type: Journal    
DOI: 10.1002/eji.201343552     Document Type: Article
Times cited : (25)

References (32)
  • 1
    • 84886025351 scopus 로고    scopus 로고
    • Plague gives surprises in the first decade of the 21st century in the United States and worldwide
    • Butler, T., Plague gives surprises in the first decade of the 21st century in the United States and worldwide. Am. J. Trop. Med. Hyg. 2013. 89: 788-793.
    • (2013) Am. J. Trop. Med. Hyg. , vol.89 , pp. 788-793
    • Butler, T.1
  • 3
    • 0034600229 scopus 로고    scopus 로고
    • Plague as a biological weapon: medical and public health management. Working Group on Civilian Biodefense
    • Inglesby, T. V., Dennis, D. T., Henderson, D. A., Bartlett, J. G., Ascher, M. S., Eitzen, E., Fine, A. D. et al., Plague as a biological weapon: medical and public health management. Working Group on Civilian Biodefense. JAMA 2000. 283: 2281-2290.
    • (2000) JAMA , vol.283 , pp. 2281-2290
    • Inglesby, T.V.1    Dennis, D.T.2    Henderson, D.A.3    Bartlett, J.G.4    Ascher, M.S.5    Eitzen, E.6    Fine, A.D.7
  • 4
    • 33748875900 scopus 로고    scopus 로고
    • Virulence factors of Yersinia pestis are overcome by a strong lipopolysaccharide response
    • Montminy, S. W., Khan, N., McGrath, S., Walkowicz, M. J., Sharp, F., Conlon, J. E., Fukase, K. et al., Virulence factors of Yersinia pestis are overcome by a strong lipopolysaccharide response. Nat. Immunol. 2006. 7: 1066-1073.
    • (2006) Nat. Immunol. , vol.7 , pp. 1066-1073
    • Montminy, S.W.1    Khan, N.2    McGrath, S.3    Walkowicz, M.J.4    Sharp, F.5    Conlon, J.E.6    Fukase, K.7
  • 6
    • 0036182734 scopus 로고    scopus 로고
    • Role of fraction 1 antigen of Yersinia pestis in inhibition of phagocytosis
    • Du, Y., Rosqvist, R. and Forsberg, A., Role of fraction 1 antigen of Yersinia pestis in inhibition of phagocytosis. Infect. Immun. 2002. 70: 1453-1460.
    • (2002) Infect. Immun. , vol.70 , pp. 1453-1460
    • Du, Y.1    Rosqvist, R.2    Forsberg, A.3
  • 7
    • 39149084406 scopus 로고    scopus 로고
    • Resistance of Yersinia pestis to complement-dependent killing is mediated by the Ail outer membrane protein
    • Bartra, S. S., Styer, K. L., O'Bryant, D. M., Nilles, M. L., Hinnebusch, B. J., Aballay, A. and Plano, G. V., Resistance of Yersinia pestis to complement-dependent killing is mediated by the Ail outer membrane protein. Infect. Immun. 2008. 76: 612-622.
    • (2008) Infect. Immun. , vol.76 , pp. 612-622
    • Bartra, S.S.1    Styer, K.L.2    O'Bryant, D.M.3    Nilles, M.L.4    Hinnebusch, B.J.5    Aballay, A.6    Plano, G.V.7
  • 8
    • 0026537238 scopus 로고
    • The Salmonella typhimurium virulence plasmid complement resistance gene rck is homologous to a family of virulence-related outer membrane protein genes, including pagC and ail
    • Heffernan, E. J., Harwood, J., Fierer, J. and Guiney, D., The Salmonella typhimurium virulence plasmid complement resistance gene rck is homologous to a family of virulence-related outer membrane protein genes, including pagC and ail. J. Bacteriol. 1992. 174: 84-91.
    • (1992) J. Bacteriol. , vol.174 , pp. 84-91
    • Heffernan, E.J.1    Harwood, J.2    Fierer, J.3    Guiney, D.4
  • 9
    • 50249151385 scopus 로고    scopus 로고
    • Genomic O island 122, locus for enterocyte effacement, and the evolution of virulent verocytotoxin-producing Escherichia coli
    • Konczy, P., Ziebell, K., Mascarenhas, M., Choi, A., Michaud, C., Kropinski, A. M., Whittam, T. S. et al., Genomic O island 122, locus for enterocyte effacement, and the evolution of virulent verocytotoxin-producing Escherichia coli. J. Bacteriol. 2008. 190: 5832-5840.
    • (2008) J. Bacteriol. , vol.190 , pp. 5832-5840
    • Konczy, P.1    Ziebell, K.2    Mascarenhas, M.3    Choi, A.4    Michaud, C.5    Kropinski, A.M.6    Whittam, T.S.7
  • 10
    • 0033570111 scopus 로고    scopus 로고
    • The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence
    • Vogt, J. and Schulz, G. E., The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence. Structure 1999. 7: 1301-1309.
    • (1999) Structure , vol.7 , pp. 1301-1309
    • Vogt, J.1    Schulz, G.E.2
  • 12
    • 78751584742 scopus 로고    scopus 로고
    • In silico comparison of Yersinia pestis and Yersinia pseudotuberculosis transcriptomes reveals a higher expression level of crucial virulence determinants in the plague bacillus
    • Chauvaux, S., Dillies, M. A., Marceau, M., Rosso, M. L., Rousseau, S., Moszer, I., Simonet, M. and Carniel, E., In silico comparison of Yersinia pestis and Yersinia pseudotuberculosis transcriptomes reveals a higher expression level of crucial virulence determinants in the plague bacillus. Int. J. Med. Microbiol. 2011. 301: 105-116.
    • (2011) Int. J. Med. Microbiol. , vol.301 , pp. 105-116
    • Chauvaux, S.1    Dillies, M.A.2    Marceau, M.3    Rosso, M.L.4    Rousseau, S.5    Moszer, I.6    Simonet, M.7    Carniel, E.8
  • 13
    • 62249186821 scopus 로고    scopus 로고
    • Temperature and growth phase influence the outer-membrane proteome and the expression of a type VI secretion system in Yersinia pestis
    • Pieper, R., Huang, S. T., Robinson, J. M., Clark, D. J., Alami, H., Parmar, P. P., Perry, R. D. et al., Temperature and growth phase influence the outer-membrane proteome and the expression of a type VI secretion system in Yersinia pestis. Microbiology 2009. 155: 498-512.
    • (2009) Microbiology , vol.155 , pp. 498-512
    • Pieper, R.1    Huang, S.T.2    Robinson, J.M.3    Clark, D.J.4    Alami, H.5    Parmar, P.P.6    Perry, R.D.7
  • 14
    • 34648833684 scopus 로고    scopus 로고
    • A surface-focused biotinylation procedure identifies the Yersinia pestis catalase KatY as a membrane-associated but non-surface-located protein
    • Myers-Morales, T., Cowan, C., Gray, M. E., Wulff, C. R., Parker, C. E., Borchers, C. H. and Straley, S. C., A surface-focused biotinylation procedure identifies the Yersinia pestis catalase KatY as a membrane-associated but non-surface-located protein. Appl. Environ. Microbiol. 2007. 73: 5750-5759.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 5750-5759
    • Myers-Morales, T.1    Cowan, C.2    Gray, M.E.3    Wulff, C.R.4    Parker, C.E.5    Borchers, C.H.6    Straley, S.C.7
  • 16
    • 78649976494 scopus 로고    scopus 로고
    • Outer membrane protein X (Ail) contributes to Yersinia pestis virulence in pneumonic plague and its activity is dependent on the lipopolysaccharide core length
    • Kolodziejek, A. M., Schnider, D. R., Rohde, H. N., Wojtowicz, A. J., Bohach, G. A., Minnich, S. A. and Hovde, C. J., Outer membrane protein X (Ail) contributes to Yersinia pestis virulence in pneumonic plague and its activity is dependent on the lipopolysaccharide core length. Infect Immun. 2010. 78: 5233-5243.
    • (2010) Infect Immun. , vol.78 , pp. 5233-5243
    • Kolodziejek, A.M.1    Schnider, D.R.2    Rohde, H.N.3    Wojtowicz, A.J.4    Bohach, G.A.5    Minnich, S.A.6    Hovde, C.J.7
  • 17
    • 0030053692 scopus 로고    scopus 로고
    • The reaction mechanism of the internal thioester in the human complement component C4
    • Dodds, A. W., Ren, X. D., Willis, A. C. and Law, S. K., The reaction mechanism of the internal thioester in the human complement component C4. Nature 1996. 379: 177-179.
    • (1996) Nature , vol.379 , pp. 177-179
    • Dodds, A.W.1    Ren, X.D.2    Willis, A.C.3    Law, S.K.4
  • 18
    • 33646378643 scopus 로고    scopus 로고
    • Lectin complement system and pattern recognition
    • Endo, Y., Takahashi, M. and Fujita, T., Lectin complement system and pattern recognition. Immunobiology 2006. 211: 283-293.
    • (2006) Immunobiology , vol.211 , pp. 283-293
    • Endo, Y.1    Takahashi, M.2    Fujita, T.3
  • 19
    • 0035810399 scopus 로고    scopus 로고
    • Complement. First of two parts
    • Walport, M. J., Complement. First of two parts. N. Engl. J. Med. 2001. 344: 1058-1066.
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1058-1066
    • Walport, M.J.1
  • 20
    • 0037199490 scopus 로고    scopus 로고
    • Structural requirements for the intracellular subunit polymerization of the complement inhibitor C4b-binding protein
    • Kask, L., Hillarp, A., Ramesh, B., Dahlback, B. and Blom, A. M., Structural requirements for the intracellular subunit polymerization of the complement inhibitor C4b-binding protein. Biochemistry 2002. 41: 9349-9357.
    • (2002) Biochemistry , vol.41 , pp. 9349-9357
    • Kask, L.1    Hillarp, A.2    Ramesh, B.3    Dahlback, B.4    Blom, A.M.5
  • 21
    • 1842557722 scopus 로고    scopus 로고
    • Complement inhibitor C4b-binding protein-friend or foe in the innate immune system?
    • Blom, A. M., Villoutreix, B. O. and Dahlback, B., Complement inhibitor C4b-binding protein-friend or foe in the innate immune system? Mol. Immunol. 2004. 40: 1333-1346.
    • (2004) Mol. Immunol. , vol.40 , pp. 1333-1346
    • Blom, A.M.1    Villoutreix, B.O.2    Dahlback, B.3
  • 22
    • 68249086824 scopus 로고    scopus 로고
    • Complement evasion strategies of pathogens-acquisition of inhibitors and beyond
    • Blom, A. M., Hallstrom, T. and Riesbeck, K., Complement evasion strategies of pathogens-acquisition of inhibitors and beyond. Mol. Immunol. 2009. 46: 2808-2817.
    • (2009) Mol. Immunol. , vol.46 , pp. 2808-2817
    • Blom, A.M.1    Hallstrom, T.2    Riesbeck, K.3
  • 23
    • 50849105103 scopus 로고    scopus 로고
    • Yersinia enterocolitica serum resistance proteins YadA and ail bind the complement regulator C4b-binding protein
    • Kirjavainen, V., Jarva, H., Biedzka-Sarek, M., Blom, A. M., Skurnik, M. and Meri, S., Yersinia enterocolitica serum resistance proteins YadA and ail bind the complement regulator C4b-binding protein. PLoS Pathog. 2008. 4: e1000140.
    • (2008) PLoS Pathog. , vol.4
    • Kirjavainen, V.1    Jarva, H.2    Biedzka-Sarek, M.3    Blom, A.M.4    Skurnik, M.5    Meri, S.6
  • 24
    • 84860316450 scopus 로고    scopus 로고
    • Functional recruitment of the human complement inhibitor C4BP to Yersinia pseudotuberculosis outer membrane protein Ail
    • Ho, D. K., Riva, R., Kirjavainen, V., Jarva, H., Ginstrom, E., Blom, A. M., Skurnik, M. and Meri, S., Functional recruitment of the human complement inhibitor C4BP to Yersinia pseudotuberculosis outer membrane protein Ail. J. Immunol. 2012. 188: 4450-4459.
    • (2012) J. Immunol. , vol.188 , pp. 4450-4459
    • Ho, D.K.1    Riva, R.2    Kirjavainen, V.3    Jarva, H.4    Ginstrom, E.5    Blom, A.M.6    Skurnik, M.7    Meri, S.8
  • 25
    • 28044459813 scopus 로고    scopus 로고
    • Human C4b-binding protein selectively interacts with Neisseria gonorrhoeae and results in species-specific infection
    • Ngampasutadol, J., Ram, S., Blom, A. M., Jarva, H., Jerse, A. E., Lien, E., Goguen, J. et al., Human C4b-binding protein selectively interacts with Neisseria gonorrhoeae and results in species-specific infection. Proc. Natl. Acad. Sci. USA 2005. 102: 17142-17147.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17142-17147
    • Ngampasutadol, J.1    Ram, S.2    Blom, A.M.3    Jarva, H.4    Jerse, A.E.5    Lien, E.6    Goguen, J.7
  • 26
    • 0035920160 scopus 로고    scopus 로고
    • Structural requirements for the complement regulatory activities of C4BP
    • Blom, A. M., Kask, L. and Dahlback, B., Structural requirements for the complement regulatory activities of C4BP. J. Biol. Chem. 2001. 276: 27136-27144.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27136-27144
    • Blom, A.M.1    Kask, L.2    Dahlback, B.3
  • 27
    • 15844421217 scopus 로고    scopus 로고
    • Identification of the outer-membrane protein PagC required for the serum resistance phenotype in Salmonella enterica serovar Choleraesuis
    • Nishio, M., Okada, N., Miki, T., Haneda, T. and Danbara, H., Identification of the outer-membrane protein PagC required for the serum resistance phenotype in Salmonella enterica serovar Choleraesuis. Microbiology 2005. 151: 863-873.
    • (2005) Microbiology , vol.151 , pp. 863-873
    • Nishio, M.1    Okada, N.2    Miki, T.3    Haneda, T.4    Danbara, H.5
  • 28
    • 77956410186 scopus 로고    scopus 로고
    • Human complement factor h binds to outer membrane protein rck of salmonella
    • Ho, D. K., Jarva, H. and Meri, S., Human complement factor h binds to outer membrane protein rck of salmonella. J. Immunol. 2010. 185: 1763-1769.
    • (2010) J. Immunol. , vol.185 , pp. 1763-1769
    • Ho, D.K.1    Jarva, H.2    Meri, S.3
  • 29
    • 80755126035 scopus 로고    scopus 로고
    • Functional recruitment of human complement inhibitor c4b-binding protein to outer membrane protein rck of salmonella
    • Ho, D. K., Tissari, J., Jarvinen, H. M., Blom, A. M., Meri, S. and Jarva, H., Functional recruitment of human complement inhibitor c4b-binding protein to outer membrane protein rck of salmonella. PLoS One 2011. 6: e27546.
    • (2011) PLoS One , vol.6
    • Ho, D.K.1    Tissari, J.2    Jarvinen, H.M.3    Blom, A.M.4    Meri, S.5    Jarva, H.6
  • 30
    • 84866550119 scopus 로고    scopus 로고
    • The Yersinia pseudotuberculosis outer membrane protein Ail recruits the human complement regulatory protein factor H
    • Ho, D. K., Riva, R., Skurnik, M. and Meri, S., The Yersinia pseudotuberculosis outer membrane protein Ail recruits the human complement regulatory protein factor H. J. Immunol. 2012. 189: 3593-3599.
    • (2012) J. Immunol. , vol.189 , pp. 3593-3599
    • Ho, D.K.1    Riva, R.2    Skurnik, M.3    Meri, S.4
  • 31
    • 15244360991 scopus 로고    scopus 로고
    • Single-step purification of human C4b-binding protein (C4BP) by affinity chromatography on a peptide derived from a streptococcal surface protein
    • Persson, J. and Lindahl, G., Single-step purification of human C4b-binding protein (C4BP) by affinity chromatography on a peptide derived from a streptococcal surface protein. J. Immunol. Methods 2005. 297:] 83-95.
    • (2005) J. Immunol. Methods , vol.297 , pp. 83-95
    • Persson, J.1    Lindahl, G.2
  • 32
    • 0023046349 scopus 로고
    • Evidence that a nicked C4b, C4b', is a functionally active C4b derivative
    • Yamazaki, M., Ichihara, C. and Nagasawa, S., Evidence that a nicked C4b, C4b', is a functionally active C4b derivative. FEBS Lett. 1986. 208: 147-150.
    • (1986) FEBS Lett. , vol.208 , pp. 147-150
    • Yamazaki, M.1    Ichihara, C.2    Nagasawa, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.