The galactosyl-(alpha 1-4)-galactose-binding adhesin of Streptococcus suis: occurrence in strains of different hemagglutination activities and induction of opsonic antibodies.

The occurrence of the galactose-(alpha 1-4)-galactose-specific adhesin in Streptococcus suis, a pig and human pathogen causing sepsis, meningitis, and other serious infections, was studied. Poly- and monoclonal anti-bodies to the purified adhesin, as well as pigeon ovomucoid, a specific probe for the adhesin activity, detected one single protein band in extracts of S. suis. The adhesin was detected in all 23 strains studied, representing pathogenic serotypes (1, 2, 4, 5, 7, 8, and nontypeable) and including several weakly hemagglutinating or nonhemagglutinating strains and phase variants. The amount of adhesin detected was not correlated with the hemagglutination activity of the intact bacteria. Extraction of cells showing no binding of pigeon ovomucoid by ultrasonic treatment resulted in extracts with pigeon ovomucoid binding activity, suggesting that the adhesin was not accessible to the probe on the intact cells. Analysis of the amount of capsular polysaccharide revealed an inverse relationship between the hemagglutination activity and expression of capsular polysaccharide, thus suggesting a factor influencing adhesin accessibility. The purified adhesin was highly immunogenic and induced in preliminary experiments bactericidal activity in mice. Thus, the adhesin, with its specific binding mechanism to host cells and a proposed pathogenic role, is widely expressed among strains of different serotypes and therefore appears to represent a novel promising candidate for the development of a vaccine against S. suis.