LPxTG surface proteins of enterococci

Trends in Microbiology

Volumn 17, Issue 9, 2009, Pages 423-430

  Hendrickx, Antoni P A ^a   Willems, Rob J L ^a   Bonten, Marc J M ^a   van Schaik, Willem ^a  

^a UNIVERSITY MEDICAL CENTER UTRECHT   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN OF COLLAGEN FROM ENTEROCOCCUS FAECALIS PROTEIN; ADHESIN OF COLLAGEN FROM ENTEROCOCCUS FAECIUM PROTEIN; AGGREGATION SUBSTANCE; BACTERIAL PROTEIN; ENTEROCOCCAL SURFACE PROTEIN; MEMBRANE PROTEIN; POLYPEPTIDE; PROTEIN EBPA; PROTEIN EBPB; PROTEIN EBPC; PROTEIN PILA; PROTEIN PILB; SECOND COLLAGEN ADHESIN OF ENTEROCOCCUS FAECIUM PROTEIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; BACTERIAL VIRULENCE; BIOFILM; CELL SURFACE; ENTEROCOCCUS FAECALIS; ENTEROCOCCUS FAECIUM; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN MOTIF; REVIEW;

ANIMALS; BACTERIAL PROTEINS; BIOFILMS; ENTEROCOCCUS; HUMANS; MEMBRANE PROTEINS; VIRULENCE;

ENTEROCOCCUS FAECALIS; ENTEROCOCCUS FAECIUM; PILA;

EID: 69749108226     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tim.2009.06.004     Document Type: Review

References (69)

1. Werner, G. et al. (2008) Emergence and spread of vancomycin resistance among enterococci in Europe. Euro Surveill. 13 (47). Pii: 19046
2. Hidron A.I., et al. NHSN annual update: antimicrobial-resistant pathogens associated with healthcare-associated infections: annual summary of data reported to the National Healthcare Safety Network at the Centers for Disease Control and Prevention, 2006-2007. Infect. Control Hosp. Epidemiol. 29 (2008) 996-1011
3. Arias C.A., and Murray B.E. Antibiotic-resistant bugs in the 21st century - a clinical super-challenge. N. Engl. J. Med. 360 (2009) 439-443
4. Lentino J.R., et al. New antimicrobial agents as therapy for resistant gram-positive cocci. Eur. J. Clin. Microbiol. Infect. Dis. 27 (2008) 3-15
5. Dramsi S., et al. Covalent attachment of proteins to peptidoglycan. FEMS Microbiol. Rev. 32 (2008) 307-320
6. Theilacker C., et al. Glycolipids are involved in biofilm accumulation and prolonged bacteremia in Enterococcus faecalis. Mol. Microbiol. 71 (2009) 1055-1069
7. Rich R.L., et al. Ace is a collagen-binding MSCRAMM from Enterococcus faecalis. J. Biol. Chem. 274 (1999) 26939-26945
8. Shankar V., et al. Infection-derived Enterococcus faecalis strains are enriched in esp, a gene encoding a novel surface protein. Infect. Immun. 67 (1999) 193-200
9. Nallapareddy S.R., et al. Endocarditis and biofilm-associated pili of Enterococcus faecalis. J. Clin. Invest. 116 (2006) 2799-2807
10. Dunny G.M. The peptide pheromone-inducible conjugation system of Enterococcus faecalis plasmid pCF10: cell-cell signalling, gene transfer, complexity and evolution. Philos. Trans. R. Soc. Lond. B Biol. Sci. 362 (2007) 1185-1193
11. Rice L.B., et al. A potential virulence gene, hylEfm, predominates in Enterococcus faecium of clinical origin. J. Infect. Dis. 187 (2003) 508-512
12. Leavis H., et al. A novel putative enterococcal pathogenicity island linked to the esp virulence gene of Enterococcus faecium and associated with epidemicity. J. Bacteriol. 186 (2004) 672-682
13. Hendrickx A.P., et al. Expression of two distinct types of pili by a hospital-acquired Enterococcus faecium isolate. Microbiology 154 (2008) 3212-3223
14. Hendrickx A.P., et al. Five genes encoding surface-exposed LPXTG proteins are enriched in hospital-adapted Enterococcus faecium clonal complex 17 isolates. J. Bacteriol. 189 (2007) 8321-8332
15. Kozlowicz B.K., et al. Pheromone-inducible conjugation in Enterococcus faecalis: a model for the evolution of biological complexity?. Int. J. Med. Microbiol. 296 (2006) 141-147
16. Chandler J.R., et al. A paracrine peptide sex pheromone also acts as an autocrine signal to induce plasmid transfer and virulence factor expression in vivo. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 15617-15622
17. Wirth R. The sex pheromone system of Enterococcus faecalis. More than just a plasmid-collection mechanism?. Eur. J. Biochem. 222 (1994) 235-246
18. Waters C.M., et al. An amino-terminal domain of Enterococcus faecalis aggregation substance is required for aggregation, bacterial internalization by epithelial cells and binding to lipoteichoic acid. Mol. Microbiol. 52 (2004) 1159-1171
19. Waters C.M., et al. The aggregation domain of aggregation substance, not the RGD motifs, is critical for efficient internalization by HT-29 enterocytes. Infect. Immun. 71 (2003) 5682-5689
20. Sartingen S., et al. Aggregation substance increases adherence and internalization, but not translocation, of Enterococcus faecalis through different intestinal epithelial cells in vitro. Infect. Immun. 68 (2000) 6044-6047
21. Wells C.L., et al. Inducible expression of Enterococcus faecalis aggregation substance surface protein facilitates bacterial internalization by cultured enterocytes. Infect. Immun. 68 (2000) 7190-7194
22. Rakita R.M., et al. Enterococcus faecalis bearing aggregation substance is resistant to killing by human neutrophils despite phagocytosis and neutrophil activation. Infect. Immun. 67 (1999) 6067-6075
23. Vanek N.N., et al. Enterococcus faecalis aggregation substance promotes opsonin-independent binding to human neutrophils via a complement receptor type 3-mediated mechanism. FEMS Immunol. Med. Microbiol. 26 (1999) 49-60
24. Sussmuth S.D., et al. Aggregation substance promotes adherence, phagocytosis, and intracellular survival of Enterococcus faecalis within human macrophages and suppresses respiratory burst. Infect. Immun. 68 (2000) 4900-4906
25. Rozdzinski E., et al. Aggregation substance-mediated adherence of Enterococcus faecalis to immobilized extracellular matrix proteins. Microb. Pathog. 30 (2001) 211-220
26. Johnson J.R., et al. Enterococcal aggregation substance and binding substance are not major contributors to urinary tract colonization by Enterococcus faecalis in a mouse model of ascending unobstructed urinary tract infection. Infect. Immun. 72 (2004) 2445-2448
27. Chuang O.N., et al. Multiple functional domains of Enterococcus faecalis aggregation substance Asc10 contribute to endocarditis virulence. Infect. Immun. 77 (2009) 539-548
28. McCormick J.K., et al. Antibodies to a surface-exposed. N-terminal domain of aggregation substance are not protective in the rabbit model of Enterococcus faecalis infective endocarditis. Infect. Immun. 69 (2001) 3305-3314
29. Cucarella C., et al. Bap, a Staphylococcus aureus surface protein involved in biofilm formation. J. Bacteriol. 183 (2001) 2888-2896
30. Stalhammar-Carlemalm M., et al. The R28 protein of Streptococcus pyogenes is related to several group B streptococcal surface proteins, confers protective immunity and promotes binding to human epithelial cells. Mol. Microbiol. 33 (1999) 208-219
31. Stalhammar-Carlemalm M., et al. Protein rib: a novel group B streptococcal cell surface protein that confers protective immunity and is expressed by most strains causing invasive infections. J. Exp. Med. 177 (1993) 1593-1603
32. Michel J.L., et al. Large, identical, tandem repeating units in the C protein α antigen gene, bca, of group B streptococci. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 10060-10064
33. Lindahl G., et al. Surface proteins of Streptococcus agalactiae and related proteins in other bacterial pathogens. Clin. Microbiol. Rev. 18 (2005) 102-127
34. Heikens E., et al. Enterococcal surface protein Esp is important for biofilm formation of Enterococcus faecium E1162. J. Bacteriol. 189 (2007) 8233-8240
35. Tendolkar P.M., et al. Enterococcal surface protein, Esp, enhances biofilm formation by Enterococcus faecalis. Infect. Immun. 72 (2004) 6032-6039
36. Heikens E., et al. Enterococcal surface protein Esp is not essential for cell adhesion and intestinal colonization of Enterococcus faecium in mice. BMC Microbiol. 9 (2009) 19
37. Pultz N.J., et al. Enterococcal surface protein Esp does not facilitate intestinal colonization or translocation of Enterococcus faecalis in clindamycin-treated mice. FEMS Microbiol. Lett. 242 (2005) 217-219
38. van Wamel W.J., et al. Growth condition-dependent Esp expression by Enterococcus faecium affects initial adherence and biofilm formation. Infect. Immun. 75 (2007) 924-931
39. Shankar N., et al. Role of Enterococcus faecalis surface protein Esp in the pathogenesis of ascending urinary tract infection. Infect. Immun. 69 (2001) 4366-4372
40. Tendolkar P.M., et al. The N-terminal domain of enterococcal surface protein, Esp, is sufficient for Esp-mediated biofilm enhancement in Enterococcus faecalis. J. Bacteriol. 187 (2005) 6213-6222
41. Sillanpaa J., et al. A family of putative MSCRAMMs from Enterococcus faecalis. Microbiology 150 (2004) 2069-2078
42. Sillanpaa J., et al. Identification and phenotypic characterization of a second collagen adhesin, Scm, and genome-based identification and analysis of 13 other predicted MSCRAMMs, including four distinct pilus loci, in Enterococcus faecium. Microbiology 154 (2008) 3199-3211
43. Kowalski W.J., et al. Enterococcus faecalis adhesin, Ace, mediates attachment to particulate dentin. J. Endodon. 32 (2006) 634-637
44. Nallapareddy S.R., et al. Enterococcus faecalis adhesin, ace, mediates attachment to extracellular matrix proteins collagen type IV and laminin as well as collagen type I. Infect. Immun. 68 (2000) 5218-5224
45. Nallapareddy S.R., et al. Clinical isolates of Enterococcus faecium exhibit strain-specific collagen binding mediated by Acm, a new member of the MSCRAMM family. Mol. Microbiol. 47 (2003) 1733-1747
46. Nallapareddy S.R., et al. Construction of improved temperature-sensitive and mobilizable vectors and their use for constructing mutations in the adhesin-encoding acm gene of poorly transformable clinical Enterococcus faecium strains. Appl. Environ. Microbiol. 72 (2006) 334-345
47. Nallapareddy S.R., et al. A functional collagen adhesin gene, acm, in clinical isolates of Enterococcus faecium correlates with the recent success of this emerging nosocomial pathogen. Infect. Immun. 76 (2008) 4110-4119
48. Zong Y., et al. A 'collagen hug' model for Staphylococcus aureus CNA binding to collagen. EMBO J. 24 (2005) 4224-4236
49. Ponnuraj K., and Narayana S.V. Crystal structure of ACE19, the collagen binding subdomain of Enterococus faecalis surface protein ACE. Proteins 69 (2007) 199-203
50. Nallapareddy S.R., et al. Inhibition of Enterococcus faecium adherence to collagen by antibodies against high-affinity binding subdomains of Acm. Infect. Immun. 75 (2007) 3192-3196
51. Liu Q., et al. The Enterococcus faecalis MSCRAMM ACE binds its ligand by the collagen hug model. J. Biol. Chem. 282 (2007) 19629-19637
52. Hall A.E., et al. Monoclonal antibodies recognizing the Enterococcus faecalis collagen-binding MSCRAMM Ace: conditional expression and binding analysis. Microb. Pathog. 43 (2007) 55-66
53. Nallapareddy S.R., et al. Contribution of the collagen adhesin Acm to pathogenesis of Enterococcus faecium in experimental endocarditis. Infect. Immun. 76 (2008) 4120-4128
54. Nallapareddy S.R., et al. Diversity of ace, a gene encoding a microbial surface component recognizing adhesive matrix molecules, from different strains of Enterococcus faecalis and evidence for production of ace during human infections. Infect. Immun. 68 (2000) 5210-5217
55. Mandlik A., et al. Pili in Gram-positive bacteria: assembly, involvement in colonization and biofilm development. Trends Microbiol. 16 (2008) 33-40
56. Handley P.S., and Jacob A.E. Some structural and physiological properties of fimbriae of Streptococcus faecalis. J. Gen. Microbiol. 127 (1981) 289-293
57. Tendolkar P.M., et al. Putative surface proteins encoded within a novel transferable locus confer a high-biofilm phenotype to Enterococcus faecalis. J. Bacteriol. 188 (2006) 2063-2072
58. Cobo M.A., et al. Detection of ebp (endocarditis- and biofilm-associated pilus) genes in enterococcal isolates from clinical and non-clinical origin. Int. J. Food Microbiol. 126 (2008) 123-126
59. Bourgogne A., et al. EbpR is important for biofilm formation by activating expression of the endocarditis and biofilm-associated pilus operon (ebpABC) of Enterococcus faecalis OG1RF. J. Bacteriol. 189 (2007) 6490-6493
60. Hernday A., et al. Self-perpetuating epigenetic pili switches in bacteria. Proc. Natl. Acad. Sci. U. S. A. 99 Suppl. 4 (2002) 16470-16476
61. Kemp K.D., et al. Relative contributions of Enterococcus faecalis OG1RF sortase-encoding genes, srtA and bps (srtC), to biofilm formation and a murine model of urinary tract infection. Infect. Immun. 75 (2007) 5399-5404
62. Singh K.V., et al. Importance of the ebp (endocarditis- and biofilm-associated pilus) locus in the pathogenesis of Enterococcus faecalis ascending urinary tract infection. J. Infect. Dis. 195 (2007) 1671-1677
63. Seepersaud R., et al. Characterization of a novel leucine-rich repeat protein antigen from group B streptococci that elicits protective immunity. Infect. Immun. 73 (2005) 1671-1683
64. Gianfaldoni C., et al. Streptococcus pneumoniae pilus subunits protect mice against lethal challenge. Infect. Immun. 75 (2007) 1059-1062
65. Mora M., et al. Group A Streptococcus produce pilus-like structures containing protective antigens and Lancefield T antigens. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 15641-15646
66. Marraffini L.A., et al. Sortases and the art of anchoring proteins to the envelopes of Gram-positive bacteria. Microbiol. Mol. Biol. Rev. 70 (2006) 192-221
67. Ton-That H., and Schneewind O. Assembly of pili on the surface of Corynebacterium diphtheriae. Mol. Microbiol. 50 (2003) 1429-1438
68. Ton-That H., et al. Sortases and pilin elements involved in pilus assembly of Corynebacterium diphtheriae. Mol. Microbiol. 53 (2004) 251-261
69. Mandlik A., et al. The molecular switch that activates the cell wall anchoring step of pilus assembly in Gram-positive bacteria. Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 14147-14152