New cell surface protein involved in biofilm formation by Streptococcus parasanguinis.

Publisher: American Society For Microbiology Country of Publication: United States NLM ID: 0246127 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1098-5522 (Electronic) Linking ISSN: 00199567 NLM ISO Abbreviation: Infect Immun Subsets: MEDLINE

Publication: Washington, DC : American Society For Microbiology
Original Publication: [Bethesda, Md.] American Society for Microbiology.

Bacterial Adhesion*; Adhesins, Bacterial/*metabolism ; Bacterial Proteins/*metabolism ; Biofilms/*growth & development ; Membrane Proteins/*metabolism ; Streptococcus/*physiology; Adhesins, Bacterial/genetics ; Bacterial Proteins/genetics ; Binding Sites ; DNA, Bacterial/chemistry ; DNA, Bacterial/genetics ; Fimbriae Proteins/genetics ; Fimbriae Proteins/metabolism ; Gene Deletion ; Humans ; Membrane Proteins/genetics ; Molecular Sequence Data ; Protein Binding ; Protein Interaction Mapping ; Protein Multimerization ; Protein Structure, Tertiary ; Sequence Analysis, DNA ; Sequence Homology, Amino Acid ; Streptococcus/genetics ; Streptococcus/growth & development ; Streptococcus/metabolism

Dental biofilm formation is critical for maintaining the healthy microbial ecology of the oral cavity. Streptococci are predominant bacterial species in the oral cavity and play important roles in the initiation of plaque formation. In this study, we identified a new cell surface protein, BapA1, from Streptococcus parasanguinis FW213 and determined that BapA1 is critical for biofilm formation. Sequence analysis revealed that BapA1 possesses a typical cell wall-sorting signal for cell surface-anchored proteins from Gram-positive bacteria. No functional orthologue was reported in other streptococci. BapA1 possesses nine putative pilin isopeptide linker domains which are crucial for pilus assembly in a number of Gram-positive bacteria. Deletion of the 3' portion of bapA1 generated a mutant that lacks surface-anchored BapA1 and abolishes formation of short fibrils on the cell surface. The mutant failed to form biofilms and exhibited reduced adherence to an in vitro tooth model. The BapA1 deficiency also inhibited bacterial autoaggregation. The N-terminal muramidase-released-protein-like domain mediated BapA1-BapA1 interactions, suggesting that BapA1-mediated cell-cell interactions are important for bacterial autoaggregation and biofilm formation. Furthermore, the BapA1-mediated bacterial adhesion and biofilm formation are independent of a fimbria-associated serine-rich repeat adhesin, Fap1, demonstrating that BapA1 is a new streptococcal adhesin.

J Bacteriol. 2007 Apr;189(8):3166-75. (PMID: 17277061)
Microbiol Mol Biol Rev. 1999 Mar;63(1):174-229. (PMID: 10066836)
Infect Immun. 1985 Mar;47(3):752-9. (PMID: 2857684)
J Biol Chem. 2010 Oct 15;285(42):32446-57. (PMID: 20584910)
Microbiology (Reading). 2009 Nov;155(Pt 11):3572-3580. (PMID: 19661180)
Scand J Dent Res. 1987 Oct;95(5):369-80. (PMID: 3477852)
J Microbiol Methods. 2008 Mar;72(3):249-56. (PMID: 18201786)
Mol Microbiol. 2002 Jan;43(1):147-57. (PMID: 11849543)
Oral Microbiol Immunol. 2003 Feb;18(1):45-9. (PMID: 12588458)
J Bacteriol. 2001 Apr;183(8):2543-52. (PMID: 11274114)
J Appl Microbiol. 2002;93(3):448-55. (PMID: 12174043)
Infect Immun. 2005 Jun;73(6):3351-7. (PMID: 15908361)
Infect Immun. 1985 Jun;48(3):617-24. (PMID: 2860066)
Proc Natl Acad Sci U S A. 2009 Oct 6;106(40):16967-71. (PMID: 19805181)
Periodontol 2000. 2006;42:47-79. (PMID: 16930306)
Infect Immun. 2008 Nov;76(11):5049-61. (PMID: 18794289)
J Biol Chem. 2009 Jul 31;284(31):20729-37. (PMID: 19497855)
Infect Immun. 2007 May;75(5):2181-8. (PMID: 17296746)
Gene. 1993 Aug 16;130(1):81-90. (PMID: 8344531)
Mol Microbiol. 2004 Apr;52(1):189-203. (PMID: 15049820)
Science. 2003 Mar 28;299(5615):2071-4. (PMID: 12663927)
PLoS Pathog. 2010 Aug 12;6(8):e1001044. (PMID: 20714350)
J Dent Res. 1976 Jan;55:A142-53. (PMID: 1060637)
Microbiol Mol Biol Rev. 2009 Sep;73(3):407-50, Table of Contents. (PMID: 19721085)
Science. 2007 Dec 7;318(5856):1625-8. (PMID: 18063798)
Infect Immun. 1992 Jun;60(6):2361-7. (PMID: 1587602)
J Clin Microbiol. 1999 Dec;37(12):4081-5. (PMID: 10565935)
Infect Immun. 2009 Jan;77(1):419-28. (PMID: 18955469)
Infect Immun. 1991 Sep;59(9):3156-62. (PMID: 1879937)
J Biol Chem. 2010 Apr 16;285(16):12405-15. (PMID: 20147289)
J Bacteriol. 2009 Sep;191(18):5603-12. (PMID: 19592583)
Infect Immun. 2007 Dec;75(12):5740-7. (PMID: 17893126)
Annu Rev Microbiol. 2000;54:49-79. (PMID: 11018124)
Arch Oral Biol. 1970 Dec;15(12):1143-8. (PMID: 5280120)
Nucleic Acids Res. 2006 Jan 1;34(Database issue):D247-51. (PMID: 16381856)
Proc Natl Acad Sci U S A. 2008 Dec 9;105(49):19456-61. (PMID: 19047636)
J Biol Chem. 2010 Oct 29;285(44):33858-66. (PMID: 20729215)
Methods. 2001 Dec;25(4):402-8. (PMID: 11846609)
J Biol Chem. 2010 Apr 9;285(15):11235-42. (PMID: 20139067)
J Biol Chem. 2010 Apr 2;285(14):10616-26. (PMID: 20123991)
Infect Immun. 2001 Apr;69(4):2512-9. (PMID: 11254614)
Mol Microbiol. 1994 Oct;14(1):115-21. (PMID: 7830549)
Science. 1999 May 21;284(5418):1318-22. (PMID: 10334980)
Clin Microbiol Rev. 2002 Apr;15(2):167-93. (PMID: 11932229)
Vet Microbiol. 2003 Feb 2;91(2-3):157-68. (PMID: 12458165)
Infect Immun. 2005 Apr;73(4):1954-63. (PMID: 15784535)
J Bacteriol. 2009 Feb;191(3):832-43. (PMID: 19047354)

R01 DE017474 United States DE NIDCR NIH HHS; R01 DE017954 United States DE NIDCR NIH HHS; R01DE017954 United States DE NIDCR NIH HHS

GENBANK JF345716

0 (Adhesins, Bacterial)
0 (Bacterial Proteins)
0 (DNA, Bacterial)
0 (Membrane Proteins)
147680-16-8 (Fimbriae Proteins)

Date Created: 20110518 Date Completed: 20110913 Latest Revision: 20211020

20240829

PMC3147580

10.1128/IAI.00029-11

21576336