메뉴 건너뛰기




Volumn 79, Issue 11, 2011, Pages 4308-4321

A naturally occurring single-residue mutation in the translocator domain of neisseria meningitidis NhhA affects trimerization, surface localization, and adhesive capabilities

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIUM ANTIBODY; MEMBRANE PROTEIN; NEISSERIA MENINGITIDIS NHHA PROTEIN; UNCLASSIFIED DRUG;

EID: 80855157277     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00198-11     Document Type: Article
Times cited : (9)

References (33)
  • 1
    • 78049447494 scopus 로고    scopus 로고
    • Adhesion, invasion, and agglutination mediated by two trimeric autotransporters in the human uropathogen Proteus mirabilis
    • Alamuri, P., et al. 2010. Adhesion, invasion, and agglutination mediated by two trimeric autotransporters in the human uropathogen Proteus mirabilis. Infect. Immun. 78:4882-4894.
    • (2010) Infect. Immun. , vol.78 , pp. 4882-4894
    • Alamuri, P.1
  • 2
    • 13444278985 scopus 로고    scopus 로고
    • Neisseria meningitidis NadA is a new invasin which promotes bacterial adhesion to and penetration into human epithelial cells
    • Capecchi, B., et al. 2005. Neisseria meningitidis NadA is a new invasin which promotes bacterial adhesion to and penetration into human epithelial cells. Mol. Microbiol. 55:687-698.
    • (2005) Mol. Microbiol. , vol.55 , pp. 687-698
    • Capecchi, B.1
  • 3
    • 0022498009 scopus 로고
    • Rapid microprocedure for isolating detergent-insoluble outer membrane proteins from Haemophilus species
    • Carlone, G. M., M. L. Thomas, H. S. Rumschlag, and F. O. Sottnek. 1986. Rapid microprocedure for isolating detergent-insoluble outer membrane proteins from Haemophilus species. J. Clin. Microbiol. 24:330-332.
    • (1986) J. Clin. Microbiol. , vol.24 , pp. 330-332
    • Carlone, G.M.1    Thomas, M.L.2    Rumschlag, H.S.3    Sottnek, F.O.4
  • 4
    • 0032985226 scopus 로고    scopus 로고
    • Characterization of the Moraxella catarrhalis uspA1 and uspA2 genes and their encoded products
    • Cope, L. D., et al. 1999. Characterization of the Moraxella catarrhalis uspA1 and uspA2 genes and their encoded products. J. Bacteriol. 181:4026-4034.
    • (1999) J. Bacteriol. , vol.181 , pp. 4026-4034
    • Cope, L.D.1
  • 5
    • 18044363515 scopus 로고    scopus 로고
    • Trimeric autotransporters: a distinct subfamily of autotransporter proteins
    • Cotter, S. E., N. K. Surana, and J. W. St. Geme III. 2005. Trimeric autotransporters: a distinct subfamily of autotransporter proteins. Trends Microbiol. 13:199-205.
    • (2005) Trends Microbiol. , vol.13 , pp. 199-205
    • Cotter, S.E.1    Surana, N.K.2    St. Geme III, J.W.3
  • 6
    • 21144449798 scopus 로고    scopus 로고
    • Architecture and adhesive activity of the Haemophilus influenzae Hsf adhesin
    • Cotter, S. E., H. J. Yeo, T. Juehne, and J. W. St. Geme III. 2005. Architecture and adhesive activity of the Haemophilus influenzae Hsf adhesin. J. Bacteriol. 187:4656-4664.
    • (2005) J. Bacteriol. , vol.187 , pp. 4656-4664
    • Cotter, S.E.1    Yeo, H.J.2    Juehne, T.3    St. Geme III, J.W.4
  • 7
    • 15144360247 scopus 로고    scopus 로고
    • Bactericidal monoclonal antibodies that define unique meningococcal B polysaccharide epitopes that do not cross-react with human polysialic acid
    • Granoff, D. M., et al. 1998. Bactericidal monoclonal antibodies that define unique meningococcal B polysaccharide epitopes that do not cross-react with human polysialic acid. J. Immunol. 160:5028-5036.
    • (1998) J. Immunol. , vol.160 , pp. 5028-5036
    • Granoff, D.M.1
  • 8
    • 37449002891 scopus 로고    scopus 로고
    • A conserved glycine residue of trimeric autotransporter domains plays a key role in Yersinia adhesin A autotransport
    • Grosskinsky, U., et al. 2007. A conserved glycine residue of trimeric autotransporter domains plays a key role in Yersinia adhesin A autotransport. J. Bacteriol. 189:9011-9019.
    • (2007) J. Bacteriol. , vol.189 , pp. 9011-9019
    • Grosskinsky, U.1
  • 9
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb-Viewer: an environment for comparative protein modeling
    • Guex, N., and M. C. Peitsch. 1997. SWISS-MODEL and the Swiss-Pdb-Viewer: an environment for comparative protein modeling. Electrophoresis 18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 10
    • 0034669051 scopus 로고    scopus 로고
    • Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins
    • Hoiczyk, E., A. Roggenkamp, M. Reichenbecher, A. Lupas, and J. Heesemann. 2000. Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins. EMBO J. 19:5989-5999.
    • (2000) EMBO J. , vol.19 , pp. 5989-5999
    • Hoiczyk, E.1    Roggenkamp, A.2    Reichenbecher, M.3    Lupas, A.4    Heesemann, J.5
  • 11
    • 18244408281 scopus 로고    scopus 로고
    • CrgA is an inducible LysR-type regulator of Neisseria meningitidis, acting both as a repressor and as an activator of gene transcription
    • Ieva, R., et al. 2005. CrgA is an inducible LysR-type regulator of Neisseria meningitidis, acting both as a repressor and as an activator of gene transcription. J. Bacteriol. 187:3421-3430.
    • (2005) J. Bacteriol. , vol.187 , pp. 3421-3430
    • Ieva, R.1
  • 13
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski, R. A., D. S. Moss, and J. M. Thornton. 1993. Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 231:1049-1067.
    • (1993) J. Mol. Biol. , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 14
    • 33744728321 scopus 로고    scopus 로고
    • Trimeric autotransporter adhesins: variable structure, common function
    • Linke, D., T. Riess, I. B. Autenrieth, A. Lupas, and V. A. Kempf. 2006. Trimeric autotransporter adhesins: variable structure, common function. Trends Microbiol. 14:264-270.
    • (2006) Trends Microbiol. , vol.14 , pp. 264-270
    • Linke, D.1    Riess, T.2    Autenrieth, I.B.3    Lupas, A.4    Kempf, V.A.5
  • 15
    • 4944264973 scopus 로고    scopus 로고
    • Putative vaccine antigens from Neisseria meningitidis recognized by serum antibodies of young children convalescing after meningococcal disease
    • Litt, D. J., et al. 2004. Putative vaccine antigens from Neisseria meningitidis recognized by serum antibodies of young children convalescing after meningococcal disease. J. Infect. Dis. 190:1488-1497.
    • (2004) J. Infect. Dis. , vol.190 , pp. 1488-1497
    • Litt, D.J.1
  • 16
    • 0037451178 scopus 로고    scopus 로고
    • Vaccination against Neisseria meningitidis using three variants of the lipoprotein GNA1870
    • Masignani, V., et al. 2003. Vaccination against Neisseria meningitidis using three variants of the lipoprotein GNA1870. J. Exp. Med. 197:789-799.
    • (2003) J. Exp. Med. , vol.197 , pp. 789-799
    • Masignani, V.1
  • 17
    • 56249146661 scopus 로고    scopus 로고
    • Repetitive architecture of the Haemophilus influenzae Hia trimeric autotransporter
    • Meng, G., J. W. St. Geme III, and G. Waksman. 2008. Repetitive architecture of the Haemophilus influenzae Hia trimeric autotransporter. J. Mol. Biol. 384:824-836.
    • (2008) J. Mol. Biol. , vol.384 , pp. 824-836
    • Meng, G.1    St. Geme III, J.W.2    Waksman, G.3
  • 18
    • 33745743311 scopus 로고    scopus 로고
    • Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter
    • Meng, G., N. K. Surana, J. W. St. Geme III, and G. Waksman. 2006. Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter. EMBO J. 25:2297-2304.
    • (2006) EMBO J , vol.25 , pp. 2297-2304
    • Meng, G.1    Surana, N.K.2    St. Geme III, J.W.3    Waksman, G.4
  • 19
    • 0032706010 scopus 로고    scopus 로고
    • Differences in surface expression of NspA among Neisseria meningitidis group B strains
    • Moe, G. R., S. Tan, and D. M. Granoff. 1999. Differences in surface expression of NspA among Neisseria meningitidis group B strains. Infect. Immun. 67:5664-5675.
    • (1999) Infect. Immun. , vol.67 , pp. 5664-5675
    • Moe, G.R.1    Tan, S.2    Granoff, D.M.3
  • 20
    • 0034089622 scopus 로고    scopus 로고
    • Identification and characterisation of a novel conserved outer membrane protein from Neisseria meningitidis
    • Peak, I. R., Y. Srikhanta, M. Dieckelmann, E. R. Moxon, and M. P. Jennings. 2000. Identification and characterisation of a novel conserved outer membrane protein from Neisseria meningitidis. FEMS Immunol. Med. Microbiol. 28:329-334.
    • (2000) FEMS Immunol. Med. Microbiol. , vol.28 , pp. 329-334
    • Peak, I.R.1    Srikhanta, Y.2    Dieckelmann, M.3    Moxon, E.R.4    Jennings, M.P.5
  • 21
    • 0034629284 scopus 로고    scopus 로고
    • Identification of vaccine candidates against serogroup B meningococcus by whole-genome sequencing
    • Pizza, M., et al. 2000. Identification of vaccine candidates against serogroup B meningococcus by whole-genome sequencing. Science 287:1816-1820.
    • (2000) Science , vol.287 , pp. 1816-1820
    • Pizza, M.1
  • 22
    • 9244259664 scopus 로고    scopus 로고
    • Bartonella adhesin a mediates a proangiogenic host cell response
    • Riess, T., et al. 2004. Bartonella adhesin a mediates a proangiogenic host cell response. J. Exp. Med. 200:1267-1278.
    • (2004) J. Exp. Med. , vol.200 , pp. 1267-1278
    • Riess, T.1
  • 23
    • 0038039279 scopus 로고    scopus 로고
    • Molecular analysis of transport and oligomerization of the Yersinia enterocolitica adhesin YadA
    • Roggenkamp, A., et al. 2003. Molecular analysis of transport and oligomerization of the Yersinia enterocolitica adhesin YadA. J. Bacteriol.185:3735-3744.
    • (2003) J. Bacteriol. , vol.185 , pp. 3735-3744
    • Roggenkamp, A.1
  • 24
    • 33748306074 scopus 로고    scopus 로고
    • Neisseria meningitidis NhhA is a multifunctional trimeric autotransporter adhesin
    • Scarselli, M., et al. 2006. Neisseria meningitidis NhhA is a multifunctional trimeric autotransporter adhesin. Mol. Microbiol. 61:631-644.
    • (2006) Mol. Microbiol. , vol.61 , pp. 631-644
    • Scarselli, M.1
  • 25
    • 77952700877 scopus 로고    scopus 로고
    • Trimer stability of YadA is critical for virulence of Yersinia enterocolitica
    • Schütz, M., et al. 2010. Trimer stability of YadA is critical for virulence of Yersinia enterocolitica. Infect. Immun. 78:2677-2690.
    • (2010) Infect. Immun. , vol.78 , pp. 2677-2690
    • Schütz, M.1
  • 26
    • 77649265923 scopus 로고    scopus 로고
    • Neisseria meningitidis GNA2132, a heparin-binding protein that induces protective immunity in humans
    • Serruto, D., et al. 2010. Neisseria meningitidis GNA2132, a heparin-binding protein that induces protective immunity in humans. Proc. Natl. Acad. Sci. U. S. A. 107:3770-3775.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 3770-3775
    • Serruto, D.1
  • 27
    • 66749138696 scopus 로고    scopus 로고
    • HadA is an atypical new multifunctional trimeric coiled-coil adhesin of Haemophilus influenzae biogroup aegyptius, which promotes entry into host cells
    • Serruto, D., et al. 2009. HadA is an atypical new multifunctional trimeric coiled-coil adhesin of Haemophilus influenzae biogroup aegyptius, which promotes entry into host cells. Cell Microbiol. 11:1044-1063.
    • (2009) Cell Microbiol. , vol.11 , pp. 1044-1063
    • Serruto, D.1
  • 28
    • 55849083867 scopus 로고    scopus 로고
    • Meningococcal outer membrane protein NhhA is essential for colonization and disease by preventing phagocytosis and complement attack
    • Sjölinder, H., J. Eriksson, L. Maudsdotter, H. Aro, and A. B. Jonsson. 2008. Meningococcal outer membrane protein NhhA is essential for colonization and disease by preventing phagocytosis and complement attack. Infect. Immun. 76:5412-5420.
    • (2008) Infect. Immun. , vol.76 , pp. 5412-5420
    • Sjölinder, H.1    Eriksson, J.2    Maudsdotter, L.3    Aro, H.4    Jonsson, A.B.5
  • 29
    • 0033765760 scopus 로고    scopus 로고
    • The Haemophilus influenzae Hia adhesin is an autotransporter protein that remains uncleaved at the C terminus and fully cell associated
    • St. Geme, J. W., III, and D. Cutter. 2000. The Haemophilus influenzae Hia adhesin is an autotransporter protein that remains uncleaved at the C terminus and fully cell associated. J. Bacteriol. 182:6005-6013.
    • (2000) J. Bacteriol. , vol.182 , pp. 6005-6013
    • St. Geme III, J.W.1    Cutter, D.2
  • 30
    • 2442507008 scopus 로고    scopus 로고
    • The Haemophilus influenzae Hia autotransporter contains an unusually short trimeric translocator domain
    • Surana, N. K., D. Cutter, S. J. Barenkamp, and J. W. St. Geme III. 2004. The Haemophilus influenzae Hia autotransporter contains an unusually short trimeric translocator domain. J. Biol. Chem. 279:14679-14685.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14679-14685
    • Surana, N.K.1    Cutter, D.2    Barenkamp, S.J.3    St. Geme III, J.W.4
  • 31
    • 63049088278 scopus 로고    scopus 로고
    • Pathogenic neisseriae: surface modulation, pathogenesis and infection control
    • Virji, M. 2009. Pathogenic neisseriae: surface modulation, pathogenesis and infection control. Nat. Rev. Microbiol. 7:274-286.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 274-286
    • Virji, M.1
  • 32
    • 79952789687 scopus 로고    scopus 로고
    • Role of the periplasmic chaperones Skp, SurA, and DegQ in outer membrane protein biogenesis in Neisseria meningitidis
    • Volokhina, E. B., et al. 2011. Role of the periplasmic chaperones Skp, SurA, and DegQ in outer membrane protein biogenesis in Neisseria meningitidis. J. Bacteriol. 193:1612-1621.
    • (2011) J. Bacteriol. , vol.193 , pp. 1612-1621
    • Volokhina, E.B.1
  • 33
    • 35648941263 scopus 로고    scopus 로고
    • Additive and synergistic bactericidal activity of antibodies directed against minor outer membrane proteins of Neisseria meningitidis
    • Weynants, V. E., et al. 2007. Additive and synergistic bactericidal activity of antibodies directed against minor outer membrane proteins of Neisseria meningitidis. Infect. Immun. 75:5434-5442.
    • (2007) Infect. Immun. , vol.75 , pp. 5434-5442
    • Weynants, V.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.