1887

Abstract

A serine-rich membrane protein named LppS from , the aetiological agent of infectious keratoconjunctivitis (IKC) of domestic and wild , was characterized. Gene cloning and sequence analysis of the gene revealed that it encoded a membrane protein precursor. The protein had a typical signal sequence and a signal peptidase II cleavage site followed by a cysteine residue representing a potential acylation site. The mature LppS protein had an apparent molecular mass of 150 kDa and was found in the detergent-associated fraction of Tween 20 extracted proteins. It possessed a serine-rich domain of 41 aa with 37 (90·2 %) serine residues. Twenty-seven of these serine residues were contiguous. The protein adhered to lamb joint synovial cells. Using an adhesion model, Fab fragments from IgG directed against recombinant purified LppS were shown to specifically inhibit adhesion of to lamb cells. Thus, LppS is likely to be an adhesin of that may play an important role in the pathogenesis of IKC.

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2003-01-01
2024-04-20
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