Non-neutralizing monoclonal antibodies to a trypsin-sensitive site on the major glycoprotein of rotavirus which discriminate between virus serotypes

Abstract

Monoclonal antibodies were derived to a human rotavirus purified from stools. Three of the antibodies immunoprecipitated the rotavirus outer capsid glycoprotein gp 34 and were non-neutralizing. These antibodies reacted by enzyme immunoassay with cultivable rotaviruses showing the “long” RNA electropherotype but were inefficient as detectors of “long” RNA pattern rotaviruses in stools. Treatment of SA 11 rotavirus with 7.5 µg/ml porcine trypsin for 30 minutes at 37° C irreversibly reduced binding of the antibodies to SA 11 rotavirus in enzyme immunoassays by 50 per cent. Binding was abolished in the presence of rotavirus-negative faecal extracts. These results indicate that non-neutralizing sites on gp 34 of rotaviruses can vary with RNA electropherotype and serotype, and that levels of trypsin currently in use to assist growth of rotaviruses in cell culture may alter the serological profile of the viruses.

DOI: 10.1007/BF01310974

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Cite this paper

@article{Coulson1987NonneutralizingMA, title={Non-neutralizing monoclonal antibodies to a trypsin-sensitive site on the major glycoprotein of rotavirus which discriminate between virus serotypes}, author={Barbara S. Coulson and Kerry J. Fowler and James Robert White and Richard G. H. Cotton}, journal={Archives of Virology}, year={1987}, volume={93}, pages={199-211} }