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Infect. Immun., 12 1997, 5157-5164, Vol 65, No. 12
RM Love, MD McMillan and HF Jenkinson
Cell surface proteins SspA and SspB in Streptococcus gordonii and SpaP in
Streptococcus mutans are members of the antigen I/II family of polypeptides
produced by oral streptococci. These proteins are adhesins and mediate
species-specific binding of cells to a variety of host and bacterial
receptors. Here we show that antigen I/II polypeptides are involved in the
attachment of oral streptococci to collagen and that they also determine
the ability of these bacteria to invade human root dentinal tubules.
Wild-type S. gordonii DL1 (Challis) cells showed heavy invasion of tubules
to a depth of approximately 200 microm, whereas the abilities of cells of
isogenic mutant strains OB220 (sspA) and OB219 (sspA sspB) to invade were
50 and >90% reduced, respectively. Likewise, wild-type S. mutans NG8
cells invaded dentinal tubules, whereas cells of isogenic mutant strain 834
(spaP) did not. The invasive abilities of strains OB220 and OB219 were
restored by heterologous expression of S. mutans SpaP polypeptide in these
strains. The extents of tubule invasion by various wild-type and mutant
strains correlated with their levels of adhesion to type I collagen, a
major component of dentin. Furthermore, S. gordonii DL1 cells exhibited a
growth response to collagen by forming long chains. This was not shown by
ssp mutants but was restored by the expression of SpaP in these cells. The
production of SspA polypeptide by S. gordonii DL1, but not production of
SspB polypeptide by strain OB220 (sspA), was enhanced in the presence of
collagen. These results are the first to demonstrate that antigen I/II
family polypeptides bind collagen and mediate a morphological growth
response of streptococci to collagen. These antigen I/II polypeptide
activities are critical for intratubular growth of streptococci and thus
for establishment of endodontic infections.
Copyright © 1997, American Society for Microbiology
Invasion of dentinal tubules by oral streptococci is associated with collagen recognition mediated by the antigen I/II family of polypeptides
Department of Oral Rehabilitation, School of Dentistry, University of Otago, Dunedin, New Zealand.
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