Isolation and characterization of Fap1, a fimbriae-associated adhesin of Streptococcus parasanguis FW213

作者：Wu H; Mintz KP; Ladha M; Fives Taylor PM^*

来源：Molecular Microbiology, 1998, 28(3): 487-500.

DOI：10.1046/j.1365-2958.1998.00805.x

An adhesin of Streptococcus parasanguis FW213, a primary colonizer of the tooth surface, has been purified from the culture medium by immunoaffinity chromatography. The purified protein has a molecular mass of 200 kDa and stains positively for carbohydrate. The amino-terminal sequence indicated that this protein represented a unique streptococcal surface protein. Immunogold labelling of the bacterium indicated that this protein was associated with fimbriae and designated Fap1 (fimbriae-associated protein). A polymerase chain reaction (PCR) product based on the amino terminus of Fap1 was used to probe an FW213 genomic library. A 9 kb fragment containing the fap1 gene was isolated and 2.5 kb have been sequenced. Generation of fap1 mutants by a single cross-over (Campbell insertion) or a non-polar allelic exchange abolished the expression of Fap1. The inactivation of fap1 resulted in a dramatic reduction in the expression of the long peritrichous fimbriae and adhesion to saliva-coated hydroxylapatite (SHA). Northern blots probed with an internal gene fragment of fap1 hybridized to a 9 kb transcript, which suggests that fap1 is transcribed as a polycistronic message. These data demonstrate that Fap1 is a unique streptococcal adhesin that is involved in the assembly of S. parasanguis FW213 fimbriae and adhesion to SHA.

• 出版日期1998-5