The N-terminal domain of the R28 protein promotes emm28 group A Streptococcus adhesion to host cells via direct binding to three integrins

摘要: Group A Streptococcus (GAS) is a human-specific pathogen responsible for wide range of diseases, ranging from superficial to life-threatening invasive infections, including endometritis, and autoimmune sequelae. GAS strains express vast repertoire virulence factors that varies depending on the strain genotype, many adhesin proteins enable adhere host cells are restricted some genotypes. emm28 third most prevalent genotype in infections France associated with gyneco-obstetrical infections. harbor R28, cell wall-anchored surface protein has previously been reported promote adhesion cervical epithelial cells. Here, using cellular biochemical approaches, we sought determine whether R28 supports also other characterize its cognate receptor. We show through N-terminal domain, R28Nt, promotes bacterial both endometrial-epithelial endometrial-stromal R28Nt was further subdivided into two domains, found involved binding. subdomains interacted directly laminin-binding α3β1, α6β1, α6β4 integrins; interestingly, these bindings events did not require divalent cations. first bind integrins expressed Finally, promoted binding keratinocytes pulmonary cells, suggesting it may be supporting prevalence genotype.