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MHV S peplomer protein expressed by a recombinant vaccinia virus vector exhibits IgG Fc-receptor activity

We have previously shown that cells infected with mouse hepatitis virus (MHV) bind rabbit, mouse, and rat IgG by the Fc portion of the IgG molecule. This Fc-binding activity appeared to be mediated by the MHV S protein. S protein could also be precipitated from MHV-infected cells by a monoclonal ant...

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Autores principales: Oleszak, Emilia L., Perlman, Stanley, Leibowitz, Julian L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Published by Elsevier Inc. 1992
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7131518/
https://www.ncbi.nlm.nih.gov/pubmed/1309271
http://dx.doi.org/10.1016/0042-6822(92)90066-X
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author Oleszak, Emilia L.
Perlman, Stanley
Leibowitz, Julian L.
author_facet Oleszak, Emilia L.
Perlman, Stanley
Leibowitz, Julian L.
author_sort Oleszak, Emilia L.
collection PubMed
description We have previously shown that cells infected with mouse hepatitis virus (MHV) bind rabbit, mouse, and rat IgG by the Fc portion of the IgG molecule. This Fc-binding activity appeared to be mediated by the MHV S protein. S protein could also be precipitated from MHV-infected cells by a monoclonal antibody directed against the murine Fc γ receptor (FcγR). To prove definitively that the S protein mediates Fc-binding activity, we have expressed the MHV S protein utilizing recombinant vaccinia viruses. The anti-FcγR monoclonal antibody, 2.4G2, precipitated recombinant S protein in cells of murine, human, and rabbit origin. Since the anti-Fc receptor monoclonal antibody does not react with human and rabbit Fc receptors these results demonstrate that the epitope recognized by this antibody is carried on the MHV S protein and is not murine in origin. Examination of various MHV isolates and escape mutants failed to identify the precise sequences in S responsible for the molecular mimicry of the murine FcγR. These data are consistent with the hypothesis that a previously identified region of similarity between the S protein and the FcγR mediates this activity. The Fc binding activity of S was expressed on the cell surface, since MHV-JHM-infected cells, but not uninfected cells, formed rosettes with anti-sheep red blood cell (SRBC) antibody-coated SRBC. The anti-FcγR monoclonal antibody neutralized MHV-JHM and inhibited syncytium formation induced by the MHV S protein.
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spelling pubmed-71315182020-04-08 MHV S peplomer protein expressed by a recombinant vaccinia virus vector exhibits IgG Fc-receptor activity Oleszak, Emilia L. Perlman, Stanley Leibowitz, Julian L. Virology Article We have previously shown that cells infected with mouse hepatitis virus (MHV) bind rabbit, mouse, and rat IgG by the Fc portion of the IgG molecule. This Fc-binding activity appeared to be mediated by the MHV S protein. S protein could also be precipitated from MHV-infected cells by a monoclonal antibody directed against the murine Fc γ receptor (FcγR). To prove definitively that the S protein mediates Fc-binding activity, we have expressed the MHV S protein utilizing recombinant vaccinia viruses. The anti-FcγR monoclonal antibody, 2.4G2, precipitated recombinant S protein in cells of murine, human, and rabbit origin. Since the anti-Fc receptor monoclonal antibody does not react with human and rabbit Fc receptors these results demonstrate that the epitope recognized by this antibody is carried on the MHV S protein and is not murine in origin. Examination of various MHV isolates and escape mutants failed to identify the precise sequences in S responsible for the molecular mimicry of the murine FcγR. These data are consistent with the hypothesis that a previously identified region of similarity between the S protein and the FcγR mediates this activity. The Fc binding activity of S was expressed on the cell surface, since MHV-JHM-infected cells, but not uninfected cells, formed rosettes with anti-sheep red blood cell (SRBC) antibody-coated SRBC. The anti-FcγR monoclonal antibody neutralized MHV-JHM and inhibited syncytium formation induced by the MHV S protein. Published by Elsevier Inc. 1992-01 2004-02-06 /pmc/articles/PMC7131518/ /pubmed/1309271 http://dx.doi.org/10.1016/0042-6822(92)90066-X Text en Copyright © 1992 Published by Elsevier Inc. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Oleszak, Emilia L.
Perlman, Stanley
Leibowitz, Julian L.
MHV S peplomer protein expressed by a recombinant vaccinia virus vector exhibits IgG Fc-receptor activity
title MHV S peplomer protein expressed by a recombinant vaccinia virus vector exhibits IgG Fc-receptor activity
title_full MHV S peplomer protein expressed by a recombinant vaccinia virus vector exhibits IgG Fc-receptor activity
title_fullStr MHV S peplomer protein expressed by a recombinant vaccinia virus vector exhibits IgG Fc-receptor activity
title_full_unstemmed MHV S peplomer protein expressed by a recombinant vaccinia virus vector exhibits IgG Fc-receptor activity
title_short MHV S peplomer protein expressed by a recombinant vaccinia virus vector exhibits IgG Fc-receptor activity
title_sort mhv s peplomer protein expressed by a recombinant vaccinia virus vector exhibits igg fc-receptor activity
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7131518/
https://www.ncbi.nlm.nih.gov/pubmed/1309271
http://dx.doi.org/10.1016/0042-6822(92)90066-X
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