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Many enteric pathogens are equipped with multiple cell adhesion factors which are important for host tissue colonization and virulence.  Y. enterocolitica , a common food-borne pathogen with invasive properties, uses the surface proteins invasin and YadA for host cell binding and entry. In this study, we demonstrate unique cell adhesion and invasion properties of  Y. enterocolitica  serotype O:3 strains, the most frequent cause of human yersiniosis, and show that these differences are mainly attributable to variations affecting the function and expression of invasin in response to temperature. In contrast to other enteric  Yersinia  strains, invasin production in O:3 strains is constitutive and largely enhanced compared to other  Y. enterocolitica  serotypes, in which  invA  expression is temperature-regulated and significantly reduced at 37°C. Increase of invasin levels is caused by (i) an IS1667 insertion into the  invA  promoter region, which includes an additional promoter and RovA and H-NS binding sites, and (ii) a P98S substitution in the  invA  activator protein RovA rendering the regulator less susceptible to proteolysis. Both variations were shown to influence bacterial colonization in a murine infection model. Furthermore, we found that co-expression of YadA and down-regulation of the O-antigen at 37°C is required to allow efficient internalization by the InvA protein. We conclude that even small variations in the expression of virulence factors can provoke a major difference in the virulence properties of closely related pathogens which may confer better survival or a higher pathogenic potential in a certain host or host environment.

Unique Cell Adhesion and Invasion Properties of Yersinia enterocolitica O:3, the Most Frequent Cause of Human Yersiniosis