IDENTIFICATION OF A NOVEL ADHESIN-LIKE GLYCOPROTEIN FROM MYCOPLASMA-HYOPNEUMONIAE

This study identifies an adhesin-like glycoprotein, which was a 110 kD a protein (P110) under HPLC-GPC assay. This adhesin consisted of one P 54 and two P28 subunits. In addition, N-glycosidase F could cleave all N-linked oligosaccharides on the P54 subunit. Experimental results in dicated that P110 with native conformations significantly inhibited th e adherence of biotin-labeled porcine tracheal epithelial cell extract s to the intact M. hyopneumoniae cells (p<0.01). Furthermore, the biot in-labeled porcine tracheal epithelial cell extracts specifically boun d to P54 and P28 subunits. This binding could be competitively inhibit ed by unlabeled porcine tracheal epithelial extracts and SPF porcine a ntisera against Mycoplasma hyopneumoniae. Both P54 and P28 subunits we re constitutively expressed in different strains of M. hyopneumoniae. Their production was negligibly changed at various passages during in vitro cultivation. The significant role of this adhesin-like glycoprot ein in the pathogenesis of swine pneumonia is under study. (C) 1998 El sevier Science B.V. All rights reserved.