Protective immunoglobulin A and G antibodies bind to overlapping intersubunit epitopes in the head domain of type 1 reovirus adhesin sigma1

Journal of Virology
Anna HelanderMax L Nibert

Abstract

Nonfusogenic mammalian orthoreovirus (reovirus) is an enteric pathogen of mice and a useful model for studies of how an enteric virus crosses the mucosal barrier of its host and is subject to control by the mucosal immune system. We recently generated and characterized a new murine immunoglobulin A (IgA)-class monoclonal antibody (MAb), 1E1, that binds to the adhesin fiber, sigma1, of reovirus type 1 Lang (T1L) and thereby neutralizes the infectivity of that strain in cell culture. 1E1 is produced in hybridoma cultures as a mixture of monomers, dimers, and higher polymers and is protective against peroral challenges with T1L either when the MAb is passively administered or when it is secreted into the intestines of mice bearing subcutaneous hybridoma tumors. In the present study, selection and analysis of mutants resistant to neutralization by 1E1 identified the region of T1L sigma1 to which the MAb binds. The region bound by a previously characterized type 1 sigma1-specific neutralizing IgG MAb, 5C6, was identified in the same way. Each of the 15 mutants isolated and analyzed was found to be much less sensitive to neutralization by either 1E1 or 5C6, suggesting the two MAbs bind to largely overlapping regions of sigma1. The te...Continue Reading

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Citations

Aug 17, 2011·Applied Biochemistry and Biotechnology·Bong-Gwan KimHyung Joo Suh
Oct 7, 2011·Mucosal Immunology·N J MantisB Corthésy
Feb 8, 2006·Immunologic Research·Dina Montufar-Solis, John R Klein
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Mar 27, 2019·Cell & Bioscience·Xue WangJing-Dong Xu
Mar 22, 2018·Frontiers in Immunology·Ioanna PettaMarkus Kleinewietfeld

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