Relationship between the ability of oral streptococci to interact with platelet glycoprotein Ibalpha and with the salivary low-molecular-weight mucin, MG2.
The oral streptococci Streptococcus sanguinis, Streptococcus gordonii and Streptococcus oralis are common aetiological agents of infective endocarditis, and their ability to adhere to and induce the aggregation of platelets is thought to be a virulence trait. The platelet glycoprotein GPIbalpha has been implicated as the adhesion receptor for S. sanguinis and S. gordonii, but it is not known if this is the case for S. oralis and other species. The aim of this study was to determine the GPIbalpha-interactive capability of a range of oral streptococci and to determine the relationship between this capability and their ability to interact with the salivary constituents that they would encounter in their normal habitat. All platelet-adhesive S. sanguinis strains and most S. gordonii strains adhered in a GPIbalpha-dependent manner, but strains of S. oralis, Streptococcus cristatus, Streptococcus parasanguinis and Streptococcus mitis had no direct affinity for platelets. Those strains that were able to bind GPIbalpha also bound to the low-molecular-weight submandibular salivary mucin, MG2, and this interaction was sialic acid-dependent. The data suggest that S. sanguinis and S. gordonii may be efficient colonizers of platelet vegetations because of their adaptation to recognize sialylated salivary mucins. In contrast, S. oralis does not interact with platelets and so is likely to colonize vegetations through an as yet unidentified mechanism.
Plummer
Christopher
C
Department of Oral Pathology, School of Clinical Dentistry, University of Sheffield, Sheffield, UK.
Douglas
Charles William Ian
CW
D001422:Bacterial Adhesion / Q000502:physiology*; D001792:Blood Platelets; D004697:Endocarditis, Bacterial / Q000382:microbiology*; D006801:Humans; D008562:Membrane Glycoproteins; D008565:Membrane Proteins / Q000502:physiology*; D009055:Mouth / Q000382:microbiology*; D055262:Mucin-2; D009077:Mucins / Q000502:physiology*; D019158:N-Acetylneuraminic Acid / Q000502:physiology; D019038:Platelet Glycoprotein GPIb-IX Complex; D012463:Saliva / Q000737:chemistry; D013291:Streptococcus / Q000472:pathogenicity* / Q000502:physiology; D014774:Virulence
C524625:MUC2 protein, human; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D055262:Mucin-2; D009077:Mucins; D019038:Platelet Glycoprotein GPIb-IX Complex; C094990:adhesion receptor; D019158:N-Acetylneuraminic Acid