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

E L Oleszak; S Perlman; J L Leibowitz

doi:10.1016/0042-6822(92)90066-X

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

Journal article

Open access

Peer reviewed

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

E L Oleszak, S Perlman and J L Leibowitz

Virology, Vol.186(1), pp.122-132

01/1992

DOI: 10.1016/0042-6822(92)90066-X

PMID: 1309271

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Abstract

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 gamma receptor (Fc gamma R). To prove definitively that the S protein mediates Fc-binding activity, we have expressed the MHV S protein utilizing recombinant vaccinia viruses. The anti-Fc gamma R 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 Fc gamma R. These data are consistent with the hypothesis that a previously identified region of similarity between the S protein and the Fc gamma R 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-Fc gamma R monoclonal antibody neutralized MHV-JHM and inhibited syncytium formation induced by the MHV S protein.

Viral Fusion Proteins - metabolism

Immunoglobulin Fc Fragments - metabolism

Humans

Receptors, Fc - metabolism

Neutralization Tests

Structure-Activity Relationship

Viral Fusion Proteins - immunology

Murine hepatitis virus - immunology

DNA Mutational Analysis

Viral Envelope Proteins - metabolism

Antigens, Differentiation - metabolism

Membrane Glycoproteins

Antibodies, Monoclonal - immunology

Recombinant Proteins - metabolism

Viral Matrix Proteins

Murine hepatitis virus - metabolism

Cells, Cultured

Cross Reactions

Spike Glycoprotein, Coronavirus

Receptors, IgG

Animals

Receptors, Fc - immunology

Recombinant Proteins - immunology

Viral Envelope Proteins - immunology

Antigens, Differentiation - immunology

Details

Title: Subtitle: MHV S peplomer protein expressed by a recombinant vaccinia virus vector exhibits IgG Fc-receptor activity
Creators: E L Oleszak - Department of Pathology and Laboratory Medicine, University of Texas Health Science Center, Houston 77030
S Perlman
J L Leibowitz
Resource Type: Journal article
Publication Details: Virology, Vol.186(1), pp.122-132
DOI: 10.1016/0042-6822(92)90066-X
PMID: 1309271
NLM abbreviation: Virology
ISSN: 0042-6822
eISSN: 1096-0341
Publisher: United States
Grant note: NS 24401 / NINDS NIH HHS NS 01369 / NINDS NIH HHS
Language: English
Date published: 01/1992
Academic Unit: Microbiology and Immunology; Stead Family Department of Pediatrics; Iowa Neuroscience Institute; Infectious Disease (Pediatrics)
Record Identifier: 9983777345402771

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