메뉴 건너뛰기




Volumn 186, Issue 17, 2004, Pages 5741-5752

Sequence diversity and molecular evolution of the heat-modifiable outer membrane protein gene (ompA) of Mannheimia (Pasteurella) haemolytica, Mannheimia glucosida, and Pasteurella trehalosi

Author keywords

[No Author keywords available]

Indexed keywords

OUTER MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN A; UNCLASSIFIED DRUG;

EID: 4344580280     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.17.5741-5752.2004     Document Type: Article
Times cited : (42)

References (60)
  • 1
    • 0032938873 scopus 로고    scopus 로고
    • Taxonomic relationships of the [Pasteurella] haemolytica complex as evaluated by DNA-DNA hybridizations and 16S rRNA sequencing with proposal of Mannheimia haemolytica gen. nov., comb. nov., Mannheimia granulomatis comb. nov., Mannheimia glucosida sp. nov., Mannheimia ruminalis sp. nov. and Mannheimia varigena sp. nov.
    • Angen, O., R. Mutters, D. A. Caugant, J. E. Olsen, and M. Bisgaard. 1999. Taxonomic relationships of the [Pasteurella] haemolytica complex as evaluated by DNA-DNA hybridizations and 16S rRNA sequencing with proposal of Mannheimia haemolytica gen. nov., comb. nov., Mannheimia granulomatis comb. nov., Mannheimia glucosida sp. nov., Mannheimia ruminalis sp. nov. and Mannheimia varigena sp. nov. Int. J. Syst. Bacteriol. 49:67-86.
    • (1999) Int. J. Syst. Bacteriol. , vol.49 , pp. 67-86
    • Angen, O.1    Mutters, R.2    Caugant, D.A.3    Olsen, J.E.4    Bisgaard, M.5
  • 2
    • 0035066331 scopus 로고    scopus 로고
    • Structure of outer membrane protein A transmembrane domain by NMR spectroscopy
    • Arora, A., F. Abildgaard, J. H. Bushweller, and L. K. Tamm. 2001. Structure of outer membrane protein A transmembrane domain by NMR spectroscopy. Nat. Struct. Biol. 8:334-338.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 334-338
    • Arora, A.1    Abildgaard, F.2    Bushweller, J.H.3    Tamm, L.K.4
  • 3
    • 0019312556 scopus 로고
    • Major heat-modifiable outer membrane protein in gram-negative bacteria: Comparison with the OmpA protein of Escherichia coli
    • Beher, M. G., C. A. Schnaitman, and A. P. Pugsley. 1980. Major heat-modifiable outer membrane protein in gram-negative bacteria: comparison with the OmpA protein of Escherichia coli. J. Bacteriol. 143:906-913.
    • (1980) J. Bacteriol. , vol.143 , pp. 906-913
    • Beher, M.G.1    Schnaitman, C.A.2    Pugsley, A.P.3
  • 5
    • 0033517134 scopus 로고    scopus 로고
    • Homologue scanning mutagenesis reveals CD66 receptor residues required for neisserial Opa protein binding
    • Bos, M. P., D. Hogan, and R. J. Belland. 1999. Homologue scanning mutagenesis reveals CD66 receptor residues required for neisserial Opa protein binding. J. Exp. Med. 190:331-340.
    • (1999) J. Exp. Med. , vol.190 , pp. 331-340
    • Bos, M.P.1    Hogan, D.2    Belland, R.J.3
  • 6
    • 0033979627 scopus 로고    scopus 로고
    • Bovine respiratory disease: Commercial vaccines currently available in Canada
    • Bowland, S. L., and P. E. Shewen. 2000. Bovine respiratory disease: commercial vaccines currently available in Canada. Can. Vet. J. 41:33-48.
    • (2000) Can. Vet. J. , vol.41 , pp. 33-48
    • Bowland, S.L.1    Shewen, P.E.2
  • 7
    • 0024616062 scopus 로고
    • Effects of Pasteurella haemolytica leukotoxin on cultured bovine lymphoma cells
    • Clinkenbeard, K. D., D. A. Mosier, A. L. Timko, and A. W. Confer. 1989. Effects of Pasteurella haemolytica leukotoxin on cultured bovine lymphoma cells. Am. J. Vet. Res. 50:271-275.
    • (1989) Am. J. Vet. Res. , vol.50 , pp. 271-275
    • Clinkenbeard, K.D.1    Mosier, D.A.2    Timko, A.L.3    Confer, A.W.4
  • 8
    • 0029919614 scopus 로고    scopus 로고
    • Aeromonas salmonicida possesses two genes encoding homologs of the major outer membrane protein, OmpA
    • Costello, G. M., R. Vipond, and S. MacIntyre. 1996. Aeromonas salmonicida possesses two genes encoding homologs of the major outer membrane protein, OmpA. J. Bacteriol. 178:1623-1630.
    • (1996) J. Bacteriol. , vol.178 , pp. 1623-1630
    • Costello, G.M.1    Vipond, R.2    MacIntyre, S.3
  • 9
    • 0041976985 scopus 로고    scopus 로고
    • Molecular and immunological characterization of Pasteurella multocida serotype A:3 OmpA: Evidence of its role in P. multocida interaction with extracellular matrix molecules
    • Dabo, S. M., A. W. Confer, and R. A. Quijano-Blas. 2003. Molecular and immunological characterization of Pasteurella multocida serotype A:3 OmpA: evidence of its role in P. multocida interaction with extracellular matrix molecules. Microb. Pathog. 35:147-157.
    • (2003) Microb. Pathog. , vol.35 , pp. 147-157
    • Dabo, S.M.1    Confer, A.W.2    Quijano-Blas, R.A.3
  • 10
    • 0017672731 scopus 로고
    • Major proteins of the Escherichia coli outer cell envelope membrane as bacteriophage receptors
    • Datta, D. B., B. Arden, and U. Henning. 1977. Major proteins of the Escherichia coli outer cell envelope membrane as bacteriophage receptors. J. Bacteriol. 131:821-829.
    • (1977) J. Bacteriol. , vol.131 , pp. 821-829
    • Datta, D.B.1    Arden, B.2    Henning, U.3
  • 11
    • 0030930694 scopus 로고    scopus 로고
    • Evolutionary genetics of Pasteurella haemolytica isolates recovered from cattle and sheep
    • Davies, R. L., S. Arkinsaw, and R. K. Selander. 1997. Evolutionary genetics of Pasteurella haemolytica isolates recovered from cattle and sheep. Infect. Immun. 65:3585-3593.
    • (1997) Infect. Immun. , vol.65 , pp. 3585-3593
    • Davies, R.L.1    Arkinsaw, S.2    Selander, R.K.3
  • 12
    • 0030840531 scopus 로고    scopus 로고
    • Genetic relationships among Pasteurella trehalosi isolates based on multilocus enzyme electrophoresis
    • Davies, R. L., S. Arkinsaw, and R. K. Selander. 1997. Genetic relationships among Pasteurella trehalosi isolates based on multilocus enzyme electrophoresis. Microbiology 143:2841-2849.
    • (1997) Microbiology , vol.143 , pp. 2841-2849
    • Davies, R.L.1    Arkinsaw, S.2    Selander, R.K.3
  • 13
    • 0036135496 scopus 로고    scopus 로고
    • Mosaic structure and molecular evolution of the leukotoxin operon (lktCABD) in Mannheimia (Pasteurella) haemolytica, Mannheimia glucosida, and Pasteurella trehalosi
    • Davies, R. L., S. Campbell, and T. S. Whittam. 2002. Mosaic structure and molecular evolution of the leukotoxin operon (lktCABD) in Mannheimia (Pasteurella) haemolytica, Mannheimia glucosida, and Pasteurella trehalosi. J. Bacteriol. 184:266-277.
    • (2002) J. Bacteriol. , vol.184 , pp. 266-277
    • Davies, R.L.1    Campbell, S.2    Whittam, T.S.3
  • 14
    • 0029973240 scopus 로고    scopus 로고
    • Intraspecific diversity and host specificity within Pasteurella haemolytica based on variation of capsular polysaccharide, lipopolysaccharide and outer-membrane proteins
    • Davies, R. L., and W. Donachie. 1996. Intraspecific diversity and host specificity within Pasteurella haemolytica based on variation of capsular polysaccharide, lipopolysaccharide and outer-membrane proteins. Microbiology 142:1895-1907.
    • (1996) Microbiology , vol.142 , pp. 1895-1907
    • Davies, R.L.1    Donachie, W.2
  • 15
    • 0029681362 scopus 로고    scopus 로고
    • Phylogenetic relationships and diversity within the Pasteurella haemolytica complex based on 16S rRNA sequence comparison and outer membrane protein and lipopolysaccharide analysis
    • Davies, R. L., B. J. Paster, and F. E. Dewhirst. 1996. Phylogenetic relationships and diversity within the Pasteurella haemolytica complex based on 16S rRNA sequence comparison and outer membrane protein and lipopolysaccharide analysis. Int. J. Syst. Bacteriol. 46:736-744.
    • (1996) Int. J. Syst. Bacteriol. , vol.46 , pp. 736-744
    • Davies, R.L.1    Paster, B.J.2    Dewhirst, F.E.3
  • 16
    • 0029863332 scopus 로고    scopus 로고
    • Intra-specific diversity within Pasteurella trehalosi based on variation of capsular polysaccharide, lipopolysaccharide and outer-membrane proteins
    • Davies, R. L., and M. Quirie. 1996. Intra-specific diversity within Pasteurella trehalosi based on variation of capsular polysaccharide, lipopolysaccharide and outer-membrane proteins. Microbiology 142:551-560.
    • (1996) Microbiology , vol.142 , pp. 551-560
    • Davies, R.L.1    Quirie, M.2
  • 17
    • 0035140046 scopus 로고    scopus 로고
    • Sequence diversity and molecular evolution of the leukotoxin (lktA) gene in bovine and ovine strains of Mannheimia (Pasteurella) haemolytica
    • Davies, R. L., T. S. Whittam, and R. K. Selander. 2001. Sequence diversity and molecular evolution of the leukotoxin (lktA) gene in bovine and ovine strains of Mannheimia (Pasteurella) haemolytica. J. Bacteriol. 183:1394-1404.
    • (2001) J. Bacteriol. , vol.183 , pp. 1394-1404
    • Davies, R.L.1    Whittam, T.S.2    Selander, R.K.3
  • 18
    • 0028263998 scopus 로고
    • The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both gram-positive and gram-negative bacteria, possibly in the interaction of these proteins with peptidoglycan
    • De Mot, R., and J. Vanderleyden. 1994. The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both gram-positive and gram-negative bacteria, possibly in the interaction of these proteins with peptidoglycan. Mol. Microbiol. 12:333-334.
    • (1994) Mol. Microbiol. , vol.12 , pp. 333-334
    • De Mot, R.1    Vanderleyden, J.2
  • 19
    • 0030949539 scopus 로고    scopus 로고
    • Molecular variation in the major outer membrane protein P5 gene of nonencapsulated Haemophilus influenzae during chronic infections
    • Duim, B., L. D. Bowler, P. P. Eijk, H. M. Jansen, J. Dankert, and L. Van Alphen. 1997. Molecular variation in the major outer membrane protein P5 gene of nonencapsulated Haemophilus influenzae during chronic infections. Infect. Immun. 65:1351-1356.
    • (1997) Infect. Immun. , vol.65 , pp. 1351-1356
    • Duim, B.1    Bowler, L.D.2    Eijk, P.P.3    Jansen, H.M.4    Dankert, J.5    Van Alphen, L.6
  • 20
    • 0000154938 scopus 로고
    • Pasteurellosis of cattle
    • C. F. Adlam and J. M. Rutter (ed.). Academic Press, London, United Kingdom
    • Frank, G. H. 1989. Pasteurellosis of cattle, p. 197-222. In C. F. Adlam and J. M. Rutter (ed.), Pasteurella and pasteurellosis. Academic Press, London, United Kingdom.
    • (1989) Pasteurella and Pasteurellosis , pp. 197-222
    • Frank, G.H.1
  • 21
    • 0002699212 scopus 로고
    • Pasteurellosis of sheep
    • C. F. Adlam and J. M. Rutter (ed.). Academic Press, London, United Kingdom
    • Gilmour, N. J. L., and J. S. Gilmour. 1989. Pasteurellosis of sheep, p. 223-261. In C. F. Adlam and J. M. Rutter (ed.), Pasteurella and pasteurellosis. Academic Press, London, United Kingdom.
    • (1989) Pasteurella and Pasteurellosis , pp. 223-261
    • Gilmour, N.J.L.1    Gilmour, J.S.2
  • 22
    • 0000417627 scopus 로고
    • Bacterial outer membranes: Evolving concepts
    • Hancock, R. E. W. 1991. Bacterial outer membranes: evolving concepts. ASM News 57:175-182.
    • (1991) ASM News , vol.57 , pp. 175-182
    • Hancock, R.E.W.1
  • 23
    • 0035464781 scopus 로고    scopus 로고
    • Molecular genetic analysis of virulence in Mannheimia (Pasteurella) haemolytica
    • Highlander, S. K. 2001. Molecular genetic analysis of virulence in Mannheimia (Pasteurella) haemolytica. Front. Biosci. 6:1128-1150.
    • (2001) Front. Biosci. , vol.6 , pp. 1128-1150
    • Highlander, S.K.1
  • 24
    • 0035110567 scopus 로고    scopus 로고
    • The variable P5 proteins of typeable and non-typeable Haemophilus influenzae target human CEACAM1
    • Hill, D. J., M. A. Toleman, D. J. Evans, S. Villullas, L. Van Alphen, and M. Virji. 2001. The variable P5 proteins of typeable and non-typeable Haemophilus influenzae target human CEACAM1. Mol. Microbiol. 39:850-862.
    • (2001) Mol. Microbiol. , vol.39 , pp. 850-862
    • Hill, D.J.1    Toleman, M.A.2    Evans, D.J.3    Villullas, S.4    Van Alphen, L.5    Virji, M.6
  • 25
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones, D. T. 1999. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292:195-202.
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 26
    • 0019076822 scopus 로고
    • Evidence of cytocidal effects of Pasteurella haemolytica on bovine peripheral blood mononuclear leukocytes
    • Kaehler, K. L., R. J. Markam, C. C. Muscoplat, and D. W. Johnson. 1980. Evidence of cytocidal effects of Pasteurella haemolytica on bovine peripheral blood mononuclear leukocytes. Am. J. Vet. Res. 41:1690-1693.
    • (1980) Am. J. Vet. Res. , vol.41 , pp. 1690-1693
    • Kaehler, K.L.1    Markam, R.J.2    Muscoplat, C.C.3    Johnson, D.W.4
  • 27
    • 0018951304 scopus 로고
    • Evidence of species specificity in the cytocidal effects of Pasteurella haemolytica
    • Kaehler, K. L., R. J. F. Markham, C. C. Muscoplat, and D. W. Johnson. 1980. Evidence of species specificity in the cytocidal effects of Pasteurella haemolytica. Infect. Immun. 30:615-616.
    • (1980) Infect. Immun. , vol.30 , pp. 615-616
    • Kaehler, K.L.1    Markham, R.J.F.2    Muscoplat, C.C.3    Johnson, D.W.4
  • 28
    • 0032438987 scopus 로고    scopus 로고
    • Hidden Markov models for detecting remote protein homologies
    • Karplus, K., C. Barrett, and R. Hughey. 1998. Hidden Markov models for detecting remote protein homologies. Bioinformatics 14:846-856.
    • (1998) Bioinformatics , vol.14 , pp. 846-856
    • Karplus, K.1    Barrett, C.2    Hughey, R.3
  • 30
    • 0036139211 scopus 로고    scopus 로고
    • MEGA2: Molecular evolutionary genetics analysis software
    • Kumar, S., K. Tamura, I. B. Jakobsen, and M. Nei. 2001. MEGA2: molecular evolutionary genetics analysis software. Bioinformatics 17:1244-1245.
    • (2001) Bioinformatics , vol.17 , pp. 1244-1245
    • Kumar, S.1    Tamura, K.2    Jakobsen, I.B.3    Nei, M.4
  • 31
  • 32
    • 0032902128 scopus 로고    scopus 로고
    • Molecular evolution and mosaic structure of alpha, beta, and gamma intimins of pathogenic Escherichia coli
    • McGraw, E. A., J. Li, R. K. Selander, and T. S. Whittam. 1999. Molecular evolution and mosaic structure of alpha, beta, and gamma intimins of pathogenic Escherichia coli. Mol. Biol. Evol. 16:12-22.
    • (1999) Mol. Biol. Evol. , vol.16 , pp. 12-22
    • McGraw, E.A.1    Li, J.2    Selander, R.K.3    Whittam, T.S.4
  • 33
    • 0034814950 scopus 로고    scopus 로고
    • Recombination in the ompA gene but not the omcB gene of Chlamydia contributes to serovar-specific differences in tissue tropism, immune surveillance, and persistence of the organism
    • Millman, K. L., S. Tararé, and D. Dean. 2001. Recombination in the ompA gene but not the omcB gene of Chlamydia contributes to serovar-specific differences in tissue tropism, immune surveillance, and persistence of the organism. J. Bacteriol. 183:5997-6008.
    • (2001) J. Bacteriol. , vol.183 , pp. 5997-6008
    • Millman, K.L.1    Tararé, S.2    Dean, D.3
  • 34
    • 0021213980 scopus 로고
    • Escherichia coli K12 outer membrane protein as a bacteriophage receptor: Analysis of mutant genes expressing altered proteins
    • Morona, R., M. Klose, and U. Henning. 1984. Escherichia coli K12 outer membrane protein as a bacteriophage receptor: analysis of mutant genes expressing altered proteins. J. Bacteriol. 159:570-578.
    • (1984) J. Bacteriol. , vol.159 , pp. 570-578
    • Morona, R.1    Klose, M.2    Henning, U.3
  • 35
    • 0022358531 scopus 로고
    • Bacteriophage receptor area of outer membrane protein OmpA of Escherichia coli K12
    • Morona, R., C. Kramer, and U. Henning. 1985. Bacteriophage receptor area of outer membrane protein OmpA of Escherichia coli K12. J. Bacteriol. 164:539-543.
    • (1985) J. Bacteriol. , vol.164 , pp. 539-543
    • Morona, R.1    Kramer, C.2    Henning, U.3
  • 36
    • 0025979037 scopus 로고
    • Interaction of chlamydiae and host cells in vitro
    • Moulder, J. W. 1991. Interaction of chlamydiae and host cells in vitro. Microbiol. Rev. 55:143-190.
    • (1991) Microbiol. Rev. , vol.55 , pp. 143-190
    • Moulder, J.W.1
  • 37
    • 0022507362 scopus 로고
    • Simple methods for estimating the numbers of synonymous and nonsynonymous nucleotide substitutions
    • Nei, M., and T. Gojobori. 1986. Simple methods for estimating the numbers of synonymous and nonsynonymous nucleotide substitutions. Mol. Biol. Evol. 3:418-426.
    • (1986) Mol. Biol. Evol. , vol.3 , pp. 418-426
    • Nei, M.1    Gojobori, T.2
  • 38
    • 0025303119 scopus 로고
    • Iron acquisition in Pasteurella haemolytica: Expression and identification of a bovine-specific transferrin receptor
    • Ogunnariwo, J. A., and A. B. Schryvers. 1990. Iron acquisition in Pasteurella haemolytica: expression and identification of a bovine-specific transferrin receptor. Infect. Immun. 58:2091-2097.
    • (1990) Infect. Immun. , vol.58 , pp. 2091-2097
    • Ogunnariwo, J.A.1    Schryvers, A.B.2
  • 39
    • 0034724567 scopus 로고    scopus 로고
    • High-resolution structure of the OmpA membrane domain
    • Pautsch, A., and G. E. Schulz. 2000. High-resolution structure of the OmpA membrane domain. J. Mol. Biol. 298:273-282.
    • (2000) J. Mol. Biol. , vol.298 , pp. 273-282
    • Pautsch, A.1    Schulz, G.E.2
  • 40
    • 0031733336 scopus 로고    scopus 로고
    • Structure of the outer membrane protein A transmembrane domain
    • Pautsch, A., and G. E. Schulz. 1998. Structure of the outer membrane protein A transmembrane domain. Nat. Struct. Biol. 5:1013-1017.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1013-1017
    • Pautsch, A.1    Schulz, G.E.2
  • 41
    • 0033188169 scopus 로고    scopus 로고
    • Molecular analysis of neisserial Opa protein interactions with the CEA family of receptors: Identification of determinants contributing to the differential specificities of binding
    • Popp, A., C. Dehio, F. Grunert, T. F. Meyer, and S. D. Gray-Owen. 1999. Molecular analysis of neisserial Opa protein interactions with the CEA family of receptors: identification of determinants contributing to the differential specificities of binding. Cell. Microbiol. 1:169-181.
    • (1999) Cell. Microbiol. , vol.1 , pp. 169-181
    • Popp, A.1    Dehio, C.2    Grunert, F.3    Meyer, T.F.4    Gray-Owen, S.D.5
  • 42
    • 0036070655 scopus 로고    scopus 로고
    • Identification of Escherichia coli outer membrane protein A receptor on human brain microvascular endothelial cells
    • Prasadarao, N. V. 2002. Identification of Escherichia coli outer membrane protein A receptor on human brain microvascular endothelial cells. Infect. Immun. 70:4556-4563.
    • (2002) Infect. Immun. , vol.70 , pp. 4556-4563
    • Prasadarao, N.V.1
  • 43
    • 0029671023 scopus 로고    scopus 로고
    • Endothelial cell GlcNAcβ1-4GlcNAc epitopes for outer membrane protein A enhance traversal of Escherichia coli across the blood-brain barrier
    • Prasadarao, N. V., C. A. Wass, and K. S. Kim. 1996. Endothelial cell GlcNAcβ1-4GlcNAc epitopes for outer membrane protein A enhance traversal of Escherichia coli across the blood-brain barrier, Infect. Immun. 64:154-160.
    • (1996) Infect. Immun. , vol.64 , pp. 154-160
    • Prasadarao, N.V.1    Wass, C.A.2    Kim, K.S.3
  • 44
    • 0030068232 scopus 로고    scopus 로고
    • Outer membrane protein A of Escherichia coli contributes to invasion of brain microvascular endothelial cells
    • Prasadarao, N. V., C. A. Wass, J. N. Weiser, M. F. Stins, S. Huang, and K. S. Kim. 1996. Outer membrane protein A of Escherichia coli contributes to invasion of brain microvascular endothelial cells, Infect. Immun. 64:146-153.
    • (1996) Infect. Immun. , vol.64 , pp. 146-153
    • Prasadarao, N.V.1    Wass, C.A.2    Weiser, J.N.3    Stins, M.F.4    Huang, S.5    Kim, K.S.6
  • 45
    • 0025283269 scopus 로고
    • A strong antibody response to the periplasmic C-terminal domain of the OmpA protein of Escherichia coli is produced by immunization with purified OmpA or with whole E. coli or Salmonella enterica serovar Typhimurium bacteria
    • Puohiniemi, R., M. Karvonen, J. Vuopio-Varkila, A. Muotiala, I. M. Helander, and M. Sarvas. 1990. A strong antibody response to the periplasmic C-terminal domain of the OmpA protein of Escherichia coli is produced by immunization with purified OmpA or with whole E. coli or Salmonella enterica serovar Typhimurium bacteria. Infect. Immun. 58:1691-1696.
    • (1990) Infect. Immun. , vol.58 , pp. 1691-1696
    • Puohiniemi, R.1    Karvonen, M.2    Vuopio-Varkila, J.3    Muotiala, A.4    Helander, I.M.5    Sarvas, M.6
  • 46
    • 0029897942 scopus 로고    scopus 로고
    • Binding between outer membrane proteins of nontypeable Haemophilus influenzae and human nasopharyngeal mucin
    • Reddy, M. S., J. M. Bernstein, T. F. Murphy, and H. S. Faden. 1996. Binding between outer membrane proteins of nontypeable Haemophilus influenzae and human nasopharyngeal mucin. Infect. Immun. 64:1477-1479.
    • (1996) Infect. Immun. , vol.64 , pp. 1477-1479
    • Reddy, M.S.1    Bernstein, J.M.2    Murphy, T.F.3    Faden, H.S.4
  • 47
    • 0032930778 scopus 로고    scopus 로고
    • Sequence diversity of flagellin (fliC) alleles in pathogenic Escherichia coli
    • Reid, S. D., R. K. Selander, and T. S. Whittam. 1999. Sequence diversity of flagellin (fliC) alleles in pathogenic Escherichia coli. J. Bacteriol. 181:153-160.
    • (1999) J. Bacteriol. , vol.181 , pp. 153-160
    • Reid, S.D.1    Selander, R.K.2    Whittam, T.S.3
  • 48
    • 0017330062 scopus 로고
    • Action of a major outer cell envelope membrane protein in conjugation of Escherichia coli K-12
    • Schweizer, M., and U. Henning. 1977. Action of a major outer cell envelope membrane protein in conjugation of Escherichia coli K-12. J. Bacteriol. 129:1651-1652.
    • (1977) J. Bacteriol. , vol.129 , pp. 1651-1652
    • Schweizer, M.1    Henning, U.2
  • 49
    • 0020040850 scopus 로고
    • Cytotoxin of Pasteurella haemolytica acting on bovine leukocytes
    • Shewen, P. E., and B. N. Wilkie. 1982. Cytotoxin of Pasteurella haemolytica acting on bovine leukocytes. Infect. Immun. 35:91-94.
    • (1982) Infect. Immun. , vol.35 , pp. 91-94
    • Shewen, P.E.1    Wilkie, B.N.2
  • 50
    • 0032819207 scopus 로고    scopus 로고
    • The detection and measurement of recombination from sequence data
    • Smith, J. M. 1999. The detection and measurement of recombination from sequence data. Genetics 153:1021-1027.
    • (1999) Genetics , vol.153 , pp. 1021-1027
    • Smith, J.M.1
  • 51
    • 0025359737 scopus 로고
    • Actinobacillus rossii sp. nov., Actinobacillus seminis sp. nov., nom. rev., Pasteurella bettii sp. nov., Pasteurella lymphangitidis sp. nov., Pasteurella mairi sp, nov., and Pasteurella trehalosi sp. nov.
    • Sneath, P. H. A., and M. Stevens. 1990. Actinobacillus rossii sp. nov., Actinobacillus seminis sp. nov., nom. rev., Pasteurella bettii sp. nov., Pasteurella lymphangitidis sp. nov., Pasteurella mairi sp, nov., and Pasteurella trehalosi sp. nov. Int. J. Syst. Bacteriol. 40:148-153.
    • (1990) Int. J. Syst. Bacteriol. , vol.40 , pp. 148-153
    • Sneath, P.H.A.1    Stevens, M.2
  • 52
    • 0018150270 scopus 로고
    • Cell envelope and shape of Escherichia coli: Multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins
    • Sonntag, I., H. Schwartz, Y. Hirota, and U. Henning. 1978. Cell envelope and shape of Escherichia coli: multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins. J. Bacteriol. 136:280-285.
    • (1978) J. Bacteriol. , vol.136 , pp. 280-285
    • Sonntag, I.1    Schwartz, H.2    Hirota, Y.3    Henning, U.4
  • 53
    • 0027210975 scopus 로고
    • Characterization of a heat-modifiable outer membrane protein of Haemophilus somnus
    • Tagawa, Y., M. Haritani, H. Ishikawa, and N. Yuasa. 1993. Characterization of a heat-modifiable outer membrane protein of Haemophilus somnus. Infect. Immun. 61:1750-1755.
    • (1993) Infect. Immun. , vol.61 , pp. 1750-1755
    • Tagawa, Y.1    Haritani, M.2    Ishikawa, H.3    Yuasa, N.4
  • 54
    • 0034058060 scopus 로고    scopus 로고
    • Evaluation of an isogenic major outer membrane protein-deficient mutant in the human model of Haemophilus ducreyi infection
    • Throm, R. E., J. A. Al-Tawfiq, K. R. Fortney, B. P. Katz, A. F. Hood, C. A. Slaughter, E. J. Hansen, and S. M. Spfnola. 2000. Evaluation of an isogenic major outer membrane protein-deficient mutant in the human model of Haemophilus ducreyi infection. Infect. Immun. 68:2602-2607.
    • (2000) Infect. Immun. , vol.68 , pp. 2602-2607
    • Throm, R.E.1    Al-Tawfiq, J.A.2    Fortney, K.R.3    Katz, B.P.4    Hood, A.F.5    Slaughter, C.A.6    Hansen, E.J.7    Spfnola, S.M.8
  • 55
    • 0041322752 scopus 로고    scopus 로고
    • Multiple elements controlling adherence of enterohemorrhagic Escherichia coli O157:H7 to HeLa cells
    • Torres, A. G., and J. B. Kaper. 2003. Multiple elements controlling adherence of enterohemorrhagic Escherichia coli O157:H7 to HeLa cells. Infect. Immun. 71:4985-4995.
    • (2003) Infect. Immun. , vol.71 , pp. 4985-4995
    • Torres, A.G.1    Kaper, J.B.2
  • 56
    • 0032752835 scopus 로고    scopus 로고
    • Critical determinants of host receptor targeting by Neisseria meningitidis and Neisseria gonorrhoeae: Identification of opa adhesiotopes on the N-domain of CD66 molecules
    • Virji, M., D. Evans, A. Hadfield, F. Grunert, A. M. Teixefra, and S. M. Watt. 1999. Critical determinants of host receptor targeting by Neisseria meningitidis and Neisseria gonorrhoeae: identification of opa adhesiotopes on the N-domain of CD66 molecules. Mol. Microbiol. 34:538-551.
    • (1999) Mol. Microbiol. , vol.34 , pp. 538-551
    • Virji, M.1    Evans, D.2    Hadfield, A.3    Grunert, F.4    Teixefra, A.M.5    Watt, S.M.6
  • 57
    • 0031759092 scopus 로고    scopus 로고
    • Secondary structure and molecular analysis of interstrain variability in the P5 outer-membrane protein of nontypable Haemophilus influenzae isolated from diverse anatomical sites
    • Webb, D. C., and A. W. Cripps. 1998. Secondary structure and molecular analysis of interstrain variability in the P5 outer-membrane protein of nontypable Haemophilus influenzae isolated from diverse anatomical sites. J. Med. Microbiol. 47:1059-1067.
    • (1998) J. Med. Microbiol. , vol.47 , pp. 1059-1067
    • Webb, D.C.1    Cripps, A.W.2
  • 58
    • 0025788466 scopus 로고
    • Outer membrane protein A (OmpA) contributes to serum resistance and pathogenicity of Escherichia coli K-1
    • Weiser, J. N., and E. C. Gotschlich. 1991. Outer membrane protein A (OmpA) contributes to serum resistance and pathogenicity of Escherichia coli K-1. Infect. Immun. 59:2252-2258.
    • (1991) Infect. Immun. , vol.59 , pp. 2252-2258
    • Weiser, J.N.1    Gotschlich, E.C.2
  • 59
    • 0026777742 scopus 로고
    • Interaction of ruminant transferrins with transferrin receptors in bovine isolates of Pasteurella haemolytica and Haemophilus somnus
    • Yu, R. H., S. D. Gray-Owen, J. Ogunnariwo, and A. B. Schryvers. 1992. Interaction of ruminant transferrins with transferrin receptors in bovine isolates of Pasteurella haemolytica and Haemophilus somnus. Infect. Immun. 60:2992-2994.
    • (1992) Infect. Immun. , vol.60 , pp. 2992-2994
    • Yu, R.H.1    Gray-Owen, S.D.2    Ogunnariwo, J.3    Schryvers, A.B.4
  • 60
    • 0032794169 scopus 로고    scopus 로고
    • Molecular cloning of the Pasteurella haemolytica pomA gene and identification of bovine antibodies against PomA surface domains
    • Zeng, H., K. Pandher, and G. L. Murphy. 1999. Molecular cloning of the Pasteurella haemolytica pomA gene and identification of bovine antibodies against PomA surface domains. Infect. Immun. 67:4968-4973.
    • (1999) Infect. Immun. , vol.67 , pp. 4968-4973
    • Zeng, H.1    Pandher, K.2    Murphy, G.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.