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Volumn 17, Issue 8, 2009, Pages 355-360

A prototype two-partner secretion pathway: the Haemophilus influenzae HMW1 and HMW2 adhesin systems

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; BACTERIAL PROTEIN; GLYCOPROTEIN;

EID: 68749094023     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tim.2009.06.002     Document Type: Review
Times cited : (40)

References (41)
  • 1
    • 0021235776 scopus 로고
    • The pathogenicity of Haemophilus influenzae
    • Turk D.C. The pathogenicity of Haemophilus influenzae. J. Med. Microbiol. 18 (1984) 1-16
    • (1984) J. Med. Microbiol. , vol.18 , pp. 1-16
    • Turk, D.C.1
  • 2
    • 0032897059 scopus 로고    scopus 로고
    • Molecular determinants of the pathogenesis of disease due to nontypable Haemophilus influenzae
    • Rao V.K., et al. Molecular determinants of the pathogenesis of disease due to nontypable Haemophilus influenzae. FEMS Microbiol. Rev. 23 (1999) 99-129
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 99-129
    • Rao, V.K.1
  • 3
    • 0030904385 scopus 로고    scopus 로고
    • Invasive disease due to nontypable Haemophilus influenzae
    • Krasan G.P., and St. Geme III J.W. Invasive disease due to nontypable Haemophilus influenzae. Rep. Pediatr. Infect. Dis. 7 (1997) 11-12
    • (1997) Rep. Pediatr. Infect. Dis. , vol.7 , pp. 11-12
    • Krasan, G.P.1    St. Geme III, J.W.2
  • 4
    • 0023628543 scopus 로고
    • Outer membrane protein and lipooligosaccharide analysis of paired nasopharyngeal and middle ear isolates in otitis media due nontypeable Haemophilus influenzae: pathogenic and epidemiologic observations
    • Murphy T.F., et al. Outer membrane protein and lipooligosaccharide analysis of paired nasopharyngeal and middle ear isolates in otitis media due nontypeable Haemophilus influenzae: pathogenic and epidemiologic observations. J. Infect. Dis. 5 (1987) 723-731
    • (1987) J. Infect. Dis. , vol.5 , pp. 723-731
    • Murphy, T.F.1
  • 5
    • 0031985210 scopus 로고    scopus 로고
    • Prevalence and distribution of the hmw and hia genes and the HMW and Hia proteins among genetically diverse strains of nontypeable Haemophilus influenzae
    • St. Geme III J.W., et al. Prevalence and distribution of the hmw and hia genes and the HMW and Hia proteins among genetically diverse strains of nontypeable Haemophilus influenzae. Infect. Immun. 66 (1998) 364-368
    • (1998) Infect. Immun. , vol.66 , pp. 364-368
    • St. Geme III, J.W.1
  • 6
    • 0025215785 scopus 로고
    • Development of serum bactericidal activity following nontypable Haemophilus influenzae acute otitis media
    • Barenkamp S.J., and Bodor F.F. Development of serum bactericidal activity following nontypable Haemophilus influenzae acute otitis media. Pediatr. Infect. Dis. J. 9 (1990) 333-339
    • (1990) Pediatr. Infect. Dis. J. , vol.9 , pp. 333-339
    • Barenkamp, S.J.1    Bodor, F.F.2
  • 7
    • 0026587935 scopus 로고
    • Cloning, expression, and DNA sequence analysis of genes encoding nontypeable Haemophilus influenzae high-molecular-weight surface-exposed proteins related to filamentous hemagglutinin of Bordetella pertussis
    • Barenkamp S.J., and Leininger E. Cloning, expression, and DNA sequence analysis of genes encoding nontypeable Haemophilus influenzae high-molecular-weight surface-exposed proteins related to filamentous hemagglutinin of Bordetella pertussis. Infect. Immun. 60 (1992) 1302-1313
    • (1992) Infect. Immun. , vol.60 , pp. 1302-1313
    • Barenkamp, S.J.1    Leininger, E.2
  • 8
    • 0039279692 scopus 로고
    • Filamentous hemagglutinin of Bordetella pertussis: nucleotide sequence and crucial role in adherence
    • Relman D.A., et al. Filamentous hemagglutinin of Bordetella pertussis: nucleotide sequence and crucial role in adherence. Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 2637-2641
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 2637-2641
    • Relman, D.A.1
  • 9
    • 0025189514 scopus 로고
    • Bordetella pertussis filamentous hemagglutinin: evaluation as a protective antigen and colonization factor in a mouse respiratory infection model
    • Kimura A., et al. Bordetella pertussis filamentous hemagglutinin: evaluation as a protective antigen and colonization factor in a mouse respiratory infection model. Infect. Immun. 58 (1990) 7-16
    • (1990) Infect. Immun. , vol.58 , pp. 7-16
    • Kimura, A.1
  • 10
    • 0028122022 scopus 로고
    • Genes encoding high molecular weight adhesion proteins of nontypeable Haemophilus influenzae are part of gene clusters
    • Barenkamp S.J., and St. Geme III J.W. Genes encoding high molecular weight adhesion proteins of nontypeable Haemophilus influenzae are part of gene clusters. Infect. Immun. 62 (1994) 3320-3328
    • (1994) Infect. Immun. , vol.62 , pp. 3320-3328
    • Barenkamp, S.J.1    St. Geme III, J.W.2
  • 11
    • 0031963491 scopus 로고    scopus 로고
    • Secretion of the Haemophilus influenzae HMW1 and HMW2 adhesins involves a periplasmic intermediate and requires the HMWB and HMWC proteins
    • St. Geme III J.W., and Grass S. Secretion of the Haemophilus influenzae HMW1 and HMW2 adhesins involves a periplasmic intermediate and requires the HMWB and HMWC proteins. Mol. Microbiol. 27 (1998) 617-630
    • (1998) Mol. Microbiol. , vol.27 , pp. 617-630
    • St. Geme III, J.W.1    Grass, S.2
  • 12
    • 3042662440 scopus 로고    scopus 로고
    • Evolutionary and functional relationships among the nontypeable Haemophilus influenzae HMW family of adhesins
    • Buscher A.Z., et al. Evolutionary and functional relationships among the nontypeable Haemophilus influenzae HMW family of adhesins. J. Bacteriol. 186 (2004) 4209-4217
    • (2004) J. Bacteriol. , vol.186 , pp. 4209-4217
    • Buscher, A.Z.1
  • 13
    • 0027400465 scopus 로고
    • High-molecular-weight proteins of nontypable Haemophilus influenzae mediate attachment to human epithelial cells
    • St. Geme III J.W., et al. High-molecular-weight proteins of nontypable Haemophilus influenzae mediate attachment to human epithelial cells. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 2875-2879
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 2875-2879
    • St. Geme III, J.W.1
  • 14
    • 0027158766 scopus 로고
    • Pilus and nonpilus bacterial adhesins: assembly and function in cell recognition
    • Hultgren S.J., et al. Pilus and nonpilus bacterial adhesins: assembly and function in cell recognition. Cell 73 (1993) 887-901
    • (1993) Cell , vol.73 , pp. 887-901
    • Hultgren, S.J.1
  • 15
    • 0028108617 scopus 로고
    • The HMW1 adhesin of nontypeable Haemophilus influenzae recognizes sialylated glycoprotein receptors on cultured human epithelial cells
    • St. Geme III J.W. The HMW1 adhesin of nontypeable Haemophilus influenzae recognizes sialylated glycoprotein receptors on cultured human epithelial cells. Infect. Immun. 62 (1994) 3881-3889
    • (1994) Infect. Immun. , vol.62 , pp. 3881-3889
    • St. Geme III, J.W.1
  • 16
    • 0035167301 scopus 로고    scopus 로고
    • Mapping of binding domains of nontypeable Haemophilus influenzae HMW1 and HMW2 adhesins
    • Dawid S., et al. Mapping of binding domains of nontypeable Haemophilus influenzae HMW1 and HMW2 adhesins. Infect. Immun. 69 (2001) 307-314
    • (2001) Infect. Immun. , vol.69 , pp. 307-314
    • Dawid, S.1
  • 17
    • 0035035580 scopus 로고    scopus 로고
    • Two-partner secretion in Gram-negative bacteria: a thrifty, specific pathway for large virulence proteins. Protein secretion through autotransporter and two-partner pathways
    • Jacob-Dubuisson F., et al. Two-partner secretion in Gram-negative bacteria: a thrifty, specific pathway for large virulence proteins. Protein secretion through autotransporter and two-partner pathways. Mol. Microbiol. 40 (2001) 306-313
    • (2001) Mol. Microbiol. , vol.40 , pp. 306-313
    • Jacob-Dubuisson, F.1
  • 18
    • 36048935998 scopus 로고    scopus 로고
    • New insight into the molecular mechanisms of two-partner secretion
    • Mazar J., and Cotter P.A. New insight into the molecular mechanisms of two-partner secretion. Trends Microbiol. 15 (2007) 508-515
    • (2007) Trends Microbiol. , vol.15 , pp. 508-515
    • Mazar, J.1    Cotter, P.A.2
  • 19
    • 0037012970 scopus 로고    scopus 로고
    • Protein-translocating outer membrane porins of Gram-negative bacteria
    • Yen M.R., et al. Protein-translocating outer membrane porins of Gram-negative bacteria. Biochim. Biophys. Acta 1562 (2002) 6-31
    • (2002) Biochim. Biophys. Acta , vol.1562 , pp. 6-31
    • Yen, M.R.1
  • 20
    • 35948954841 scopus 로고    scopus 로고
    • First glimpse of the crystal structure of YaeT's POTRA domains
    • Misra R. First glimpse of the crystal structure of YaeT's POTRA domains. ACS Chem. Biol. 2 (2007) 649-651
    • (2007) ACS Chem. Biol. , vol.2 , pp. 649-651
    • Misra, R.1
  • 21
    • 0034034907 scopus 로고    scopus 로고
    • Maturation and secretion of the nontypable Haemophilus influenzae HMW1 adhesin: Roles of the N-terminal and C-terminal domains
    • Grass S., and St. Geme III J.W. Maturation and secretion of the nontypable Haemophilus influenzae HMW1 adhesin: Roles of the N-terminal and C-terminal domains. Mol. Microbiol. 36 (2000) 55-67
    • (2000) Mol. Microbiol. , vol.36 , pp. 55-67
    • Grass, S.1    St. Geme III, J.W.2
  • 22
    • 0029166295 scopus 로고
    • SepA, the major extracellular protein of Shigella flexneri: autonomous secretion and involvement in tissue invasion
    • Benjelloun-Touimi Z., et al. SepA, the major extracellular protein of Shigella flexneri: autonomous secretion and involvement in tissue invasion. Mol. Microbiol. 17 (1995) 123-135
    • (1995) Mol. Microbiol. , vol.17 , pp. 123-135
    • Benjelloun-Touimi, Z.1
  • 23
    • 33748512158 scopus 로고    scopus 로고
    • Surface anchoring of a bacterial adhesin secreted by the two-partner secretion system
    • Buscher A.Z., et al. Surface anchoring of a bacterial adhesin secreted by the two-partner secretion system. Mol. Microbiol. 61 (2006) 470-483
    • (2006) Mol. Microbiol. , vol.61 , pp. 470-483
    • Buscher, A.Z.1
  • 24
    • 0034819295 scopus 로고    scopus 로고
    • Identification of a locus involved in systemic dissemination of Yersinia enterocolitica
    • Nelson K.M., et al. Identification of a locus involved in systemic dissemination of Yersinia enterocolitica. Infect. Immun. 69 (2001) 6201-6208
    • (2001) Infect. Immun. , vol.69 , pp. 6201-6208
    • Nelson, K.M.1
  • 25
    • 0029044848 scopus 로고
    • A gene cluster involved in the utilization of both free heme and heme: hemopexin by Haemophilus influenzae type b
    • Cope L.D., et al. A gene cluster involved in the utilization of both free heme and heme: hemopexin by Haemophilus influenzae type b. J. Bacteriol. 177 (1995) 2644-2653
    • (1995) J. Bacteriol. , vol.177 , pp. 2644-2653
    • Cope, L.D.1
  • 26
    • 0027582285 scopus 로고
    • Activation and secretion of Serratia hemolysin
    • Braun V., et al. Activation and secretion of Serratia hemolysin. Zentralbl. Bakteriol. 278 (1993) 306-315
    • (1993) Zentralbl. Bakteriol. , vol.278 , pp. 306-315
    • Braun, V.1
  • 27
    • 0029616070 scopus 로고
    • Cloning and characterization of the genes encoding the hemolysin of Haemophilus ducreyi
    • Palmer K.L., and Munson Jr. R.S. Cloning and characterization of the genes encoding the hemolysin of Haemophilus ducreyi. Mol. Microbiol. 18 (1995) 821-830
    • (1995) Mol. Microbiol. , vol.18 , pp. 821-830
    • Palmer, K.L.1    Munson Jr., R.S.2
  • 28
    • 0025253321 scopus 로고
    • Nucleotide sequencing of the Proteus mirabilis calcium-independent hemolysin genes (hpmA and hemB) reveals sequence similarity with the Serratia marcescens hemolysin genes (shlA and shlB)
    • Uphoff T.S., and Welch R.A. Nucleotide sequencing of the Proteus mirabilis calcium-independent hemolysin genes (hpmA and hemB) reveals sequence similarity with the Serratia marcescens hemolysin genes (shlA and shlB). J. Bacteriol. 172 (1990) 1206-1216
    • (1990) J. Bacteriol. , vol.172 , pp. 1206-1216
    • Uphoff, T.S.1    Welch, R.A.2
  • 29
    • 0033621401 scopus 로고    scopus 로고
    • Channel formation by FhaC, the outer membrane protein involved in the secretion of the Bordetella pertussis filamentous hemagglutinin
    • Jacob-Dubuisson F., et al. Channel formation by FhaC, the outer membrane protein involved in the secretion of the Bordetella pertussis filamentous hemagglutinin. J. Biol. Chem. 274 (1999) 37731-37735
    • (1999) J. Biol. Chem. , vol.274 , pp. 37731-37735
    • Jacob-Dubuisson, F.1
  • 30
    • 0032991297 scopus 로고    scopus 로고
    • The haemolysin-secreting ShlB protein of the outer membrane of Serratia marcescens: determination of surface-exposed residues and formation of ion-permeable pores by ShlB mutants in artificial lipid bilayer membranes
    • Konninger U.W., et al. The haemolysin-secreting ShlB protein of the outer membrane of Serratia marcescens: determination of surface-exposed residues and formation of ion-permeable pores by ShlB mutants in artificial lipid bilayer membranes. Mol. Microbiol. 32 (1999) 1212-1225
    • (1999) Mol. Microbiol. , vol.32 , pp. 1212-1225
    • Konninger, U.W.1
  • 31
    • 5144228928 scopus 로고    scopus 로고
    • Evidence for conserved architecture and physical properties of Omp85-like proteins throughout evolution
    • Surana N.K., et al. Evidence for conserved architecture and physical properties of Omp85-like proteins throughout evolution. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 14497-14502
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 14497-14502
    • Surana, N.K.1
  • 32
    • 47049118705 scopus 로고    scopus 로고
    • The TpsB translocator HMW1B of Haemophilus influenzae forms a large conductance channel
    • Duret G., et al. The TpsB translocator HMW1B of Haemophilus influenzae forms a large conductance channel. J. Biol. Chem. 283 (2008) 15771-15778
    • (2008) J. Biol. Chem. , vol.283 , pp. 15771-15778
    • Duret, G.1
  • 33
    • 35048861987 scopus 로고    scopus 로고
    • Structure of the Haemophilus influenzae HMW1B translocator protein: Evidence for a twin-pore
    • Li H., et al. Structure of the Haemophilus influenzae HMW1B translocator protein: Evidence for a twin-pore. J. Bacteriol. 189 (2007) 7497-7502
    • (2007) J. Bacteriol. , vol.189 , pp. 7497-7502
    • Li, H.1
  • 34
    • 34548128883 scopus 로고    scopus 로고
    • Structure of the membrane protein FhaC: A member of the Omp85-TpsB transporter superfamily
    • Clantin B., et al. Structure of the membrane protein FhaC: A member of the Omp85-TpsB transporter superfamily. Science 317 (2007) 957-961
    • (2007) Science , vol.317 , pp. 957-961
    • Clantin, B.1
  • 35
    • 9244243105 scopus 로고    scopus 로고
    • The outer membrane usher forms a twin-pore secretion complex
    • Li H., et al. The outer membrane usher forms a twin-pore secretion complex. J. Mol. Biol. 344 (2004) 1397-1407
    • (2004) J. Mol. Biol. , vol.344 , pp. 1397-1407
    • Li, H.1
  • 36
    • 43049171700 scopus 로고    scopus 로고
    • Fiber formation across the bacterial outer membrane by the chaperone/usher pathway
    • Remaut H., et al. Fiber formation across the bacterial outer membrane by the chaperone/usher pathway. Cell 133 (2008) 640-652
    • (2008) Cell , vol.133 , pp. 640-652
    • Remaut, H.1
  • 37
    • 33745818313 scopus 로고    scopus 로고
    • Translocator proteins in the two-partner secretion family have multiple domains
    • Surana N.K., et al. Translocator proteins in the two-partner secretion family have multiple domains. J. Biol. Chem. 281 (2006) 18051-18058
    • (2006) J. Biol. Chem. , vol.281 , pp. 18051-18058
    • Surana, N.K.1
  • 38
    • 0037673430 scopus 로고    scopus 로고
    • The Haemophilus influenzae HMW1 adhesin is glycosylated in a process that requires the HMW1C protein and an enzyme important for lipooligosaccharide biosynthesis
    • Grass S., et al. The Haemophilus influenzae HMW1 adhesin is glycosylated in a process that requires the HMW1C protein and an enzyme important for lipooligosaccharide biosynthesis. Mol. Microbiol. 48 (2003) 737-751
    • (2003) Mol. Microbiol. , vol.48 , pp. 737-751
    • Grass, S.1
  • 39
    • 54449094921 scopus 로고    scopus 로고
    • The Haemophilus influenzae HMW1 adhesin is a glycoprotein with an unusual N-linked carbohydrate modification
    • Gross J., et al. The Haemophilus influenzae HMW1 adhesin is a glycoprotein with an unusual N-linked carbohydrate modification. J. Biol. Chem. 283 (2008) 26010-26015
    • (2008) J. Biol. Chem. , vol.283 , pp. 26010-26015
    • Gross, J.1
  • 40
    • 35649021756 scopus 로고    scopus 로고
    • The structure of the Haemophilus influenzae HMW1 pro-piece reveals a structural domain that is essential for bacterial two-partner secretion
    • Yeo H.-J., et al. The structure of the Haemophilus influenzae HMW1 pro-piece reveals a structural domain that is essential for bacterial two-partner secretion. J. Biol. Chem. 42 (2007) 31076-31084
    • (2007) J. Biol. Chem. , vol.42 , pp. 31076-31084
    • Yeo, H.-J.1
  • 41
    • 1942437434 scopus 로고    scopus 로고
    • The crystal structure of the filamentous hemagglutinin secretion domain and its implications for the two-partner secretion pathway
    • Clantin B., et al. The crystal structure of the filamentous hemagglutinin secretion domain and its implications for the two-partner secretion pathway. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 6194-6199
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 6194-6199
    • Clantin, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.