Inhibition of Mycoplasma bovis cytadherence by a monoclonal antibody and various carbohydrate substances

Abstract

The attachment of Mycoplasma bovis to permanent embryonic bovine lung (EBL) cells was studied in order to identify factors participating in the adhesion process. A monoclonal antibody directed against a 26 kDa protein of M. bovis was shown to reduce cytadherence of strains 120 and 454 by 46% and 70%, respectively. In uninhibited assays, strain 120 which exhibits an intense 26 kDa band in electrophoretic protein patterns adhere more strongly to EBL cell monolayers than strain 454 whose corresponding band is considerably weaker. The findings indicate involvement of the 26 kDa protein in M. bovis adherence. In further inhibition experiments, the ability of N-acetyl-neuraminlactose, glycophorin and dextran sulfate to significantly reduce adherence could be demonstrated. This suggests participation of sialic acid residues and probably also sulfatide groups as binding receptors. The data point to a complex adhesion mechanism with similarities to M. pneumoniae.