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Volumn 8, Issue 12, 2013, Pages 1575-1585

Bacterial receptors for host transferrin and lactoferrin: Molecular mechanisms and role in host-microbe interactions

Author keywords

bacterial receptors; iron acquisition; iron homeostasis; lactoferrin; transferrin

Indexed keywords

CARCINOEMBRYONIC ANTIGEN RELATED CELL ADHESION MOLECULE 1; CERULOPLASMIN; FERRIC ION; FERROPORTIN; FERROUS ION; IRON BINDING PROTEIN; LACTOFERRIN; TRANSFERRIN; TRANSFERRIN BINDING PROTEIN A; TRANSFERRIN BINDING PROTEIN B;

EID: 84889573712     PISSN: 17460913     EISSN: 17460921     Source Type: Journal    
DOI: 10.2217/fmb.13.125     Document Type: Review
Times cited : (56)

References (51)
  • 1
    • 37549059612 scopus 로고    scopus 로고
    • Regulation of iron acquisition and storage: Consequences for iron-linked disorders
    • De Domenico I, McVey Ward D, Kaplan J. Regulation of iron acquisition and storage: Consequences for iron-linked disorders. Nat. Rev. Mol. Cell. Biol. 9(1), 72-81 (2008).
    • (2008) Nat. Rev. Mol. Cell. Biol. , vol.9 , Issue.1 , pp. 72-81
    • De Domenico, I.1    McVey Ward, D.2    Kaplan, J.3
  • 2
    • 59449109182 scopus 로고    scopus 로고
    • Iron homeostasis: Recently identified proteins provide insight into novel control mechanisms
    • Zhang AS, Enns CA. Iron homeostasis: Recently identified proteins provide insight into novel control mechanisms. J. Biol. Chem. 284(2), 711-715 (2009).
    • (2009) J. Biol. Chem. , vol.284 , Issue.2 , pp. 711-715
    • Zhang, A.S.1    Enns, C.A.2
  • 3
    • 80051966207 scopus 로고    scopus 로고
    • How the binding of human transferrin primes the transferrin receptor potentiating iron release at endosomal pH
    • Eckenroth BE, Steere AN, Chasteen ND, Everse SJ, Mason AB. How the binding of human transferrin primes the transferrin receptor potentiating iron release at endosomal pH. Proc. Natl Acad. Sci. USA 108(32), 13089-13094 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , Issue.32 , pp. 13089-13094
    • Eckenroth, B.E.1    Steere, A.N.2    Chasteen, N.D.3    Everse, S.J.4    Mason, A.B.5
  • 4
    • 67349234858 scopus 로고    scopus 로고
    • Iron availability and infection
    • Weinberg ED. Iron availability and infection. Biochim. Biophys. Acta 1790(7), 600-605 (2009).
    • (2009) Biochim. Biophys. Acta , vol.1790 , Issue.7 , pp. 600-605
    • Weinberg, E.D.1
  • 5
    • 84861414827 scopus 로고    scopus 로고
    • Lactoferrin, a key molecule in immune and inflammatory processes
    • Legrand D. Lactoferrin, a key molecule in immune and inflammatory processes. Biochem. Cell Biol. 90(3), 252-268 (2012).
    • (2012) Biochem. Cell Biol. , vol.90 , Issue.3 , pp. 252-268
    • Legrand, D.1
  • 6
    • 77953286718 scopus 로고    scopus 로고
    • A critical review of the roles of host lactoferrin in immunity
    • Legrand D, Mazurier J. A critical review of the roles of host lactoferrin in immunity. Biometals 23(3), 365-376 (2010).
    • (2010) Biometals , vol.23 , Issue.3 , pp. 365-376
    • Legrand, D.1    Mazurier, J.2
  • 7
    • 68649102264 scopus 로고    scopus 로고
    • Invasive Haemophilus influenzae disease: Changing epidemiology and host-parasite interactions in the 21st century
    • Ulanova M, Tsang RS. Invasive Haemophilus influenzae disease: Changing epidemiology and host-parasite interactions in the 21st century. Infect. Genet. Evol. 9(4), 594-605 (2009).
    • (2009) Infect. Genet. Evol. , vol.9 , Issue.4 , pp. 594-605
    • Ulanova, M.1    Tsang, R.S.2
  • 9
    • 63049088278 scopus 로고    scopus 로고
    • Pathogenic Neisseriae: Surface modulation, pathogenesis and infection control
    • Virji M. Pathogenic Neisseriae: Surface modulation, pathogenesis and infection control. Nat. Rev. Microbiol. 7(4), 274-286 (2009).
    • (2009) Nat. Rev. Microbiol. , vol.7 , Issue.4 , pp. 274-286
    • Virji, M.1
  • 10
    • 84857387277 scopus 로고    scopus 로고
    • Evidence-based effectiveness of vaccination against Mannheimia haemolytica Pasteurella multocida, and Histophilus somni in feedlot cattle for mitigating the incidence and effect of bovine respiratory disease complex
    • 106e1-106e7 ix
    • Larson RL, Step DL. Evidence-based effectiveness of vaccination against Mannheimia haemolytica, Pasteurella multocida, and Histophilus somni in feedlot cattle for mitigating the incidence and effect of bovine respiratory disease complex. Vet. Clin. North Am. Food Anim. Pract. 28(1), 97-106, 106e1-106e7, ix (2012).
    • (2012) Vet. Clin. North Am. Food Anim. Pract. , vol.28 , Issue.1 , pp. 97-106
    • Larson, R.L.1    Step, D.L.2
  • 12
    • 0029894182 scopus 로고    scopus 로고
    • Bacterial transferrin and lactoferrin receptors
    • DOI 10.1016/0966-842X(96)10025-1
    • Gray-Owen SD, Schryvers AB. Bacterial transferrin and lactoferrin receptors. Trends Microbiol. 4(5), 185-191 (1996). (Pubitemid 26162132)
    • (1996) Trends in Microbiology , vol.4 , Issue.5 , pp. 185-191
    • Gray-Owen, S.D.1    Schryvers, A.B.2
  • 13
    • 0025212523 scopus 로고
    • Receptors for transferrin in pathogenic bacteria are specific for the host's protein
    • Schryvers AB, Gonzalez GC. Receptors for transferrin in pathogenic bacteria are specific for the host's protein. Can. J. Microbiol. 36, 145-147 (1990). (Pubitemid 20144330)
    • (1990) Canadian Journal of Microbiology , vol.36 , Issue.2 , pp. 145-147
    • Schryvers, A.B.1    Gonzalez, G.C.2
  • 14
    • 0037783267 scopus 로고    scopus 로고
    • Opposing selective forces for expression of the gonococcal lactoferrin receptor
    • DOI 10.1046/j.1365-2958.2003.03496.x
    • Anderson JE, Hobbs MM, Biswas GD, Sparling PF. Opposing selective forces for expression of the gonococcal lactoferrin receptor. Mol. Microbiol. 48(5), 1325-1337 (2003). (Pubitemid 36718226)
    • (2003) Molecular Microbiology , vol.48 , Issue.5 , pp. 1325-1337
    • Anderson, J.E.1    Hobbs, M.M.2    Biswas, G.D.3    Sparling, P.F.4
  • 15
    • 0037046282 scopus 로고    scopus 로고
    • Both transferrin binding proteins are virulence factors in Actinobacillus pleuropneumoniae serotype 7 infection
    • DOI 10.1016/S0378-1097(02)00570-0, PII S0378109702005700
    • Baltes N, Hennig-Pauka I, Gerlach GF. Both transferrin binding proteins are virulence factors in Actinobacillus pleuropneumoniae serotype 7 infection. FEMS Microbiol. Lett. 209(2), 283-287 (2002). (Pubitemid 34465605)
    • (2002) FEMS Microbiology Letters , vol.209 , Issue.2 , pp. 283-287
    • Baltes, N.1    Hennig-Pauka, I.2    Gerlach, G.-F.3
  • 17
    • 79958056347 scopus 로고    scopus 로고
    • Helicobacter pylori perturbs iron trafficking in the epithelium to grow on the cell surface
    • Tan S, Noto JM, Romero-Gallo J, Peek RM Jr, Amieva MR. Helicobacter pylori perturbs iron trafficking in the epithelium to grow on the cell surface. PLoS Pathog. 7(5), e1002050 (2011).
    • (2011) PLoS Pathog , vol.7 , Issue.5
    • Tan, S.1    Noto, J.M.2    Romero-Gallo, J.3    Peek Jr., R.M.4    Amieva, M.R.5
  • 18
    • 79953302384 scopus 로고    scopus 로고
    • Opa proteins and CEACAMs: Pathways of immune engagement for pathogenic Neisseria
    • Sadarangani M, Pollard AJ, Gray-Owen SD. Opa proteins and CEACAMs: Pathways of immune engagement for pathogenic Neisseria. FEMS Microbiol. Rev. 35, 498-514 (2011).
    • (2011) FEMS Microbiol. Rev. , vol.35 , pp. 498-514
    • Sadarangani, M.1    Pollard, A.J.2    Gray-Owen, S.D.3
  • 19
    • 77955644270 scopus 로고    scopus 로고
    • Genome sequencing reveals widespread virulence gene exchange among human Neisseria species
    • Marri PR, Paniscus M, Weyand NJ et al. Genome sequencing reveals widespread virulence gene exchange among human Neisseria species. PLoS ONE 5(7), e11835 (2010).
    • (2010) PLoS ONE , vol.5 , Issue.7
    • Marri, P.R.1    Paniscus, M.2    Weyand, N.J.3
  • 20
    • 84861397686 scopus 로고    scopus 로고
    • The role of lactoferrin binding protein B in mediating protection against lactoferricin
    • Morgenthau A, Adamiak P, Livingstone MJ, Schryvers AB. The role of lactoferrin binding protein B in mediating protection against lactoferricin. Biochem. Cell Biol. 90(3), 417-423 (2012).
    • (2012) Biochem. Cell Biol. , vol.90 , Issue.3 , pp. 417-423
    • Morgenthau, A.1    Adamiak, P.2    Livingstone, M.J.3    Schryvers, A.B.4
  • 22
    • 42949150242 scopus 로고    scopus 로고
    • Identification of TbpA residues required for transferrin-iron utilization by Neisseria gonorrhoeae
    • DOI 10.1128/IAI.00020-08
    • Noto JM, Cornelissen CN. Identification of TbpA residues required for transferrin-iron utilization by Neisseria gonorrhoeae. Infect. Immun. 76(5), 1960-1969 (2008). (Pubitemid 351656128)
    • (2008) Infection and Immunity , vol.76 , Issue.5 , pp. 1960-1969
    • Noto, J.M.1    Cornelissen, C.N.2
  • 23
    • 68949221568 scopus 로고    scopus 로고
    • Insights into the bacterial transferrin receptor: The structure of transferrin binding protein B from Actinobacillus pleuropneumoniae
    • Moraes TF, Yu R-H, Strynadka NC, Schryvers AB. Insights into the bacterial transferrin receptor: The structure of transferrin binding protein B from Actinobacillus pleuropneumoniae. Mol. Cell 35(4), 523-533 (2009).
    • (2009) Mol. Cell , vol.35 , Issue.4 , pp. 523-533
    • Moraes, T.F.1    Yu, R.-H.2    Strynadka, N.C.3    Schryvers, A.B.4
  • 24
    • 84455173069 scopus 로고    scopus 로고
    • The anchor peptide of transferrin binding protein B is required for interaction with transferrin binding protein A
    • Yang X, Yu RH, Calmettes C, Moraes TF, Schryvers AB. The anchor peptide of transferrin binding protein B is required for interaction with transferrin binding protein A. J. Biol. Chem. 286(52), 45165-45173 (2011).
    • (2011) J. Biol. Chem. , vol.286 , Issue.52 , pp. 45165-45173
    • Yang, X.1    Yu, R.H.2    Calmettes, C.3    Moraes, T.F.4    Schryvers, A.B.5
  • 25
    • 79953323853 scopus 로고    scopus 로고
    • Structural variations within the transferrin binding site on transferrin binding protein
    • Calmettes C, Yu R-H, Silva LP et al. Structural variations within the transferrin binding site on transferrin binding protein, TbpB. J. Biol. Chem. 286, 12683-12692 (2011).
    • (2011) TbpB. J. Biol. Chem. , vol.286 , pp. 12683-12692
    • Calmettes, C.1    Yu, R.-H.2    Silva, L.P.3
  • 26
    • 79958752291 scopus 로고    scopus 로고
    • Conserved interaction between transferrin and transferrin-binding proteins from porcine pathogens
    • Silva LP, Yu R, Calmettes C et al. Conserved interaction between transferrin and transferrin-binding proteins from porcine pathogens. J. Biol. Chem. 286(24), 21353-21360 (2011).
    • (2011) J. Biol. Chem. , vol.286 , Issue.24 , pp. 21353-21360
    • Silva, L.P.1    Yu, R.2    Calmettes, C.3
  • 27
    • 84857999363 scopus 로고    scopus 로고
    • The structural basis of transferrin iron sequestration by transferrin binding protein B
    • Calmettes C, Alcantara J, Schryvers AB, Moraes TF. The structural basis of transferrin iron sequestration by transferrin binding protein B. Nat. Struct. Mol. Biol. 19(3), 358-360 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , Issue.3 , pp. 358-360
    • Calmettes, C.1    Alcantara, J.2    Schryvers, A.B.3    Moraes, T.F.4
  • 28
    • 84857783784 scopus 로고    scopus 로고
    • Structural basis for iron piracy by pathogenic Neisseria
    • Noinaj N, Easley NC, Oke M et al. Structural basis for iron piracy by pathogenic Neisseria. Nature 483, 53-58 (2012).
    • (2012) Nature , vol.483 , pp. 53-58
    • Noinaj, N.1    Easley, N.C.2    Oke, M.3
  • 29
    • 0033064808 scopus 로고    scopus 로고
    • Iron acquisition systems in the pathogenic Neisseria
    • DOI 10.1046/j.1365-2958.1999.01411.x
    • Schryvers AB, Stojiljkovic I. Iron acquisition systems in the pathogenic Neisseria. Mol. Microbiol. 32, 1117-1123 (1999). (Pubitemid 29286652)
    • (1999) Molecular Microbiology , vol.32 , Issue.6 , pp. 1117-1123
    • Schryvers, A.B.1    Stojiljkovic, I.2
  • 30
    • 77956164601 scopus 로고    scopus 로고
    • Hijacking transferrin bound iron: Protein-receptor interactions involved in iron transport in N. Gonorrhoeae
    • Silburt C, Roulhac P, Weaver K et al. Hijacking transferrin bound iron: Protein-receptor interactions involved in iron transport in N. gonorrhoeae. Metallomics 1(1), 249-255 (2009).
    • (2009) Metallomics , vol.1 , Issue.1 , pp. 249-255
    • Silburt, C.1    Roulhac, P.2    Weaver, K.3
  • 31
    • 34249776343 scopus 로고    scopus 로고
    • High-affinity binding by the periplasmic iron-binding protein from Haemophilus influenzae is required for acquiring iron from transferrin
    • DOI 10.1042/BJ20070110
    • Khan AG, Shouldice SR, Kirby SM, Yu R-H, Tari LW, Schryvers AB. High affinity binding by the periplasmic iron binding protein from Haemophilus influenzae is required for acquiring iron from transferrin. Biochem. J. 404(2), 217-225 (2007). (Pubitemid 46849593)
    • (2007) Biochemical Journal , vol.404 , Issue.2 , pp. 217-225
    • Khan, A.G.1    Shouldice, S.R.2    Kirby, S.D.3    Yu, R.-H.4    Tari, L.W.5    Schryvers, A.B.6
  • 32
    • 84860870450 scopus 로고    scopus 로고
    • Steric and allosteric factors prevent simultaneous binding of transferrin-binding proteins A and B to transferrin
    • Silva LP, Yu RH, Calmettes C et al. Steric and allosteric factors prevent simultaneous binding of transferrin-binding proteins A and B to transferrin. Biochem. J. 444, 189-197 (2012).
    • (2012) Biochem. J. , vol.444 , pp. 189-197
    • Silva, L.P.1    Yu, R.H.2    Calmettes, C.3
  • 33
    • 84884815303 scopus 로고    scopus 로고
    • Structural insight into the lactoferrin receptors from pathogenic Neisseria
    • Noinaj N, Cornelissen CN, Buchanan SK. Structural insight into the lactoferrin receptors from pathogenic Neisseria. J. Struct. Biol. 184(1), 83-92 (2013).
    • (2013) J. Struct. Biol. , vol.184 , Issue.1 , pp. 83-92
    • Noinaj, N.1    Cornelissen, C.N.2    Buchanan, S.K.3
  • 34
    • 0037810925 scopus 로고    scopus 로고
    • Bacterial lactoferrin-binding protein A binds to both domains of the human lactoferrin C-lobe
    • Wong H, Schryvers AB. Bacterial lactoferrin binding protein a binds to both domains of the human lactoferrin C-lobe. Microbiology 149, 1729-1737 (2003). (Pubitemid 36874319)
    • (2003) Microbiology , vol.149 , Issue.7 , pp. 1729-1737
    • Wong, H.1    Schryvers, A.B.2
  • 36
    • 0029587287 scopus 로고
    • Biochemical analysis of lactoferrin receptors in the Neisseriaceae: Identification of a second bacterial lactoferrin receptor protein
    • DOI 10.1016/S0882-4010(96)80002-7
    • Bonnah RA, Yu R-H, Schryvers AB. Biochemical analysis of lactoferrin receptors in the Neisseriaceae: Identification of a second bacterial lactoferrin receptor protein. Microb. Pathogen. 19(5), 285-297 (1995). (Pubitemid 26024244)
    • (1995) Microbial Pathogenesis , vol.19 , Issue.5 , pp. 285-297
    • Bonnah, R.A.1    Yu, R.-H.2    Schryvers, A.B.3
  • 37
    • 77953924496 scopus 로고    scopus 로고
    • NalP-mediated proteolytic release of lactoferrin-binding protein B from the meningococcal cell surface
    • Roussel-Jazede V, Jongerius I, Bos MP, Tommassen J, van Ulsen P. NalP-mediated proteolytic release of lactoferrin-binding protein B from the meningococcal cell surface. Infect. Immun. 78(7), 3083-3089 (2010).
    • (2010) Infect. Immun. , vol.78 , Issue.7 , pp. 3083-3089
    • Roussel-Jazede, V.1    Jongerius, I.2    Bos, M.P.3    Tommassen, J.4    Van Ulsen, P.5
  • 38
    • 79952230538 scopus 로고    scopus 로고
    • Genotypic and phenotypic modifications of Neisseria meningitidis after an accidental human passage
    • Omer H, Rose G, Jolley KA et al. Genotypic and phenotypic modifications of Neisseria meningitidis after an accidental human passage. PLoS ONE 6(2), e17145 (2011).
    • (2011) PLoS ONE , vol.6 , Issue.2
    • Omer, H.1    Rose, G.2    Jolley, K.A.3
  • 39
    • 79958032046 scopus 로고    scopus 로고
    • Transcriptome analysis of Neisseria meningitidis in human whole blood and mutagenesis studies identify virulence factors involved in blood survival
    • Echenique-Rivera H, Muzzi A, Del Tordello E et al. Transcriptome analysis of Neisseria meningitidis in human whole blood and mutagenesis studies identify virulence factors involved in blood survival. PLoS Pathog. 7(5), e1002027 (2011).
    • (2011) PLoS Pathog , vol.7 , Issue.5
    • Echenique-Rivera, H.1    Muzzi, A.2    Del Tordello, E.3
  • 40
    • 80455174939 scopus 로고    scopus 로고
    • Experimental gonococcal infection in male volunteers: Cumulative experience with Neisseria gonorrhoeae strains FA1090 and MS11mkC
    • Hobbs MM, Sparling PF, Cohen MS, Shafer WM, Deal CD, Jerse AE. Experimental gonococcal infection in male volunteers: Cumulative experience with Neisseria gonorrhoeae strains FA1090 and MS11mkC. Front. Microbiol. 2, 123 (2011).
    • (2011) Front. Microbiol. , vol.2 , Issue.123
    • Hobbs, M.M.1    Sparling, P.F.2    Cohen, M.S.3    Shafer, W.M.4    Deal, C.D.5    Jerse, A.E.6
  • 41
    • 44249127516 scopus 로고    scopus 로고
    • Distribution of transferrin binding protein B gene (tbpB) variants among Neisseria species
    • Harrison OB, Maiden MC, Rokbi B. Distribution of transferrin binding protein B gene (tbpB) variants among Neisseria species. BMC Microbiol. 8, 66 (2008).
    • (2008) BMC Microbiol , vol.8 , pp. 66
    • Harrison, O.B.1    Maiden, M.C.2    Rokbi, B.3
  • 42
    • 84878193178 scopus 로고    scopus 로고
    • Processing-independent CRISPR RNAs limit natural transformation in Neisseria meningitidis
    • Zhang Y, Heidrich N, Ampattu BJ et al. Processing-independent CRISPR RNAs limit natural transformation in Neisseria meningitidis. Mol. Cell 50(4), 488-503 (2013).
    • (2013) Mol. Cell , vol.50 , Issue.4 , pp. 488-503
    • Zhang, Y.1    Heidrich, N.2    Ampattu, B.J.3
  • 43
    • 84863610046 scopus 로고    scopus 로고
    • Restriction and sequence alterations affect DNA uptake sequence-dependent transformation in Neisseria meningitidis
    • Ambur OH, Frye SA, Nilsen M, Hovland E, Tonjum T. Restriction and sequence alterations affect DNA uptake sequence-dependent transformation in Neisseria meningitidis. PLoS ONE 7(7), e39742 (2012).
    • (2012) PLOS ONE , vol.7 , Issue.7
    • Ambur, O.H.1    Frye, S.A.2    Nilsen, M.3    Hovland, E.4    Tonjum, T.5
  • 44
    • 0035148818 scopus 로고    scopus 로고
    • Characterization of a novel transferrin receptor in bovine strains of Pasteurella multocida
    • DOI 10.1128/JB.183.3.890-896.2001
    • Ogunnariwo JA, Schryvers AB. Characterization of a novel transferrin receptor in bovine strains of Pasteurella multocida. J. Bacteriol. 183(3), 890-896 (2001). (Pubitemid 32095298)
    • (2001) Journal of Bacteriology , vol.183 , Issue.3 , pp. 890-896
    • Ogunnariwo, J.A.1    Schryvers, A.B.2
  • 45
    • 3042655159 scopus 로고    scopus 로고
    • Haemophilus somnus possesses two systems for acquisition of transferrin-bound iron
    • DOI 10.1128/JB.186.13.4407-4411.2004
    • Ekins A, Bahrami F, Sijercic A, Maret D, Niven DF. Haemophilus somnus possesses two systems for acquisition of transferrin-bound iron. J. Bacteriol. 186(13), 4407-4411 (2004). (Pubitemid 38802593)
    • (2004) Journal of Bacteriology , vol.186 , Issue.13 , pp. 4407-4411
    • Ekins, A.1    Bahrami, F.2    Sijercic, A.3    Maret, D.4    Niven, D.F.5
  • 46
    • 84861407451 scopus 로고    scopus 로고
    • Patterns of sequence variation with the Neisseria meningitidis lactoferrin-binding proteins
    • Adamiak P, Beddek A, Pajon R, Schryvers AB. Patterns of sequence variation with the Neisseria meningitidis lactoferrin-binding proteins. Biochem. Cell Biol. 90(3), 339-350 (2012).
    • (2012) Biochem. Cell Biol. , vol.90 , Issue.3 , pp. 339-350
    • Adamiak, P.1    Beddek, A.2    Pajon, R.3    Schryvers, A.B.4
  • 47
    • 84884743799 scopus 로고    scopus 로고
    • In vivo adaptation and persistence of Neisseria meningitidis within the nasopharyngeal mucosa
    • Johswich KO, McCaw SE, Islam E et al. In vivo adaptation and persistence of Neisseria meningitidis within the nasopharyngeal mucosa. PLoS Pathog. 9(7), e1003509 (2013).
    • (2013) PLoS Pathog. , vol.9 , Issue.7
    • Johswich, K.O.1    McCaw, S.E.2    Islam, E.3
  • 48
    • 84889570934 scopus 로고    scopus 로고
    • The negatively charged regions of lactoferrin binding protein B, an adaptation against anti-microbial peptides
    • In Press
    • Mogenthau A, Beddek A, Schryvers AB. The negatively charged regions of lactoferrin binding protein B, an adaptation against anti-microbial peptides. PLoS ONE (2013) (In Press).
    • (2013) Plos One
    • Mogenthau, A.1    Beddek, A.2    Schryvers, A.B.3
  • 49
    • 37749009078 scopus 로고    scopus 로고
    • A carcinoembryonic antigen-related cell adhesion molecule 1 homologue plays a pivotal role in nontypeable Haemophilus influenzae colonization of the chinchilla nasopharynx via the outer membrane protein P5-homologous adhesin
    • Bookwalter JE, Jurcisek JA, Gray-Owen SD, Fernandez S, McGillivary G, Bakaletz LO. A carcinoembryonic antigen-related cell adhesion molecule 1 homologue plays a pivotal role in nontypeable Haemophilus influenzae colonization of the chinchilla nasopharynx via the outer membrane protein P5-homologous adhesin. Infect. Immun. 76(1), 48-55 (2008).
    • (2008) Infect. Immun. , vol.76 , Issue.1 , pp. 48-55
    • Bookwalter, J.E.1    Jurcisek, J.A.2    Gray-Owen, S.D.3    Fernandez, S.4    McGillivary, G.5    Bakaletz, L.O.6
  • 50
    • 55849143614 scopus 로고    scopus 로고
    • Moraxella catarrhalis binding to host cellular receptors is mediated by sequence-specific determinants not conserved among all UspA1 protein variants
    • Brooks MJ, Sedillo JL, Wagner N et al. Moraxella catarrhalis binding to host cellular receptors is mediated by sequence-specific determinants not conserved among all UspA1 protein variants. Infect. Immun. 76(11), 5322-5329 (2008).
    • (2008) Infect. Immun. , vol.76 , Issue.11 , pp. 5322-5329
    • Brooks, M.J.1    Sedillo, J.L.2    Wagner, N.3


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