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Oral strains ofActinomyces spp. express type 1 fimbriae, which are composed of major FimP subunits, and bind preferentially to salivary acidic proline-rich proteins (APRPs) or to statherin. We have mapped genetic differences in thefimP subunit genes and the peptide recognition motifs within the host proteins associated with these differential binding specificities. ThefimP genes were amplified by PCR fromActinomyces viscosus ATCC 19246, with preferential binding to statherin, and fromActinomyces naeslundii LY7, P-1-K, and B-1-K, with preferential binding to APRPs. ThefimP gene from the statherin-binding strain 19246 is novel and has about 80% nucleotide and amino acid sequence identity to the highly conservedfimP genes of the APRP-binding strains (about 98 to 99% sequence identity). The novel FimP protein contains an amino-terminal signal peptide, randomly distributed single-amino-acid substitutions, and structurally different segments and ends with a cell wall-anchoring and a membrane-spanning region. When agarose beads with CNBr-linked host determinant-specific decapeptides were used,A. viscosus 19246 bound to the Thr42 Phe43 terminus of statherin andA. naeslundii LY7 bound to the Pro149 Gln150 termini of APRPs. Furthermore, while the APRP-bindingA. naeslundii strains originate from the human mouth,A. viscosus strains isolated from the oral cavity of rat and hamster hosts showed preferential binding to statherin and contained the novelfimP gene. Thus,A. viscosus andA. naeslundii display structurally variantfimP genes whose protein products are likely to interact with different peptide motifs and to determine animal host tropism.

infection and immunity

Strains of <i>Actinomyces naeslundii</i> and <i>Actinomyces viscosus</i> Exhibit Structurally Variant Fimbrial Subunit Proteins and Bind to Different Peptide Motifs in Salivary Proteins

Strains of Actinomyces naeslundii and Actinomyces viscosus Exhibit Structurally Variant Fimbrial Subunit Proteins and Bind to Different Peptide Motifs in Salivary Proteins