SrasV1, PubMed, Checkpoint, bibRecord, 003442

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

Identifieur interne : 003442 ( PubMed/Checkpoint ); précédent : 003441; suivant : 003443

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

Auteurs : E L Oleszak ; S. Perlman ; J L Leibowitz

Source :

Virology [ 0042-6822 ] ; 1992.

RBID : pubmed:1309271

Descripteurs français

KwdFr :
- Analyse de mutations d'ADN, Animaux, Anticorps monoclonaux (immunologie), Antigènes de différenciation (immunologie), Antigènes de différenciation (métabolisme), Cellules cultivées, Fragments Fc des immunoglobulines (métabolisme), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Protéines de fusion virale (immunologie), Protéines de fusion virale (métabolisme), Protéines de l'enveloppe virale (immunologie), Protéines de l'enveloppe virale (métabolisme), Protéines de la matrice virale, Protéines recombinantes (immunologie), Protéines recombinantes (métabolisme), Relation structure-activité, Réactions croisées, Récepteur Fc (immunologie), Récepteur Fc (métabolisme), Récepteurs du fragment Fc des IgG, Tests de neutralisation, Virus de l'hépatite murine (immunologie), Virus de l'hépatite murine (métabolisme).
MESH :

English descriptors

KwdEn :
- Animals, Antibodies, Monoclonal (immunology), Antigens, Differentiation (immunology), Antigens, Differentiation (metabolism), Cells, Cultured, Cross Reactions, DNA Mutational Analysis, Humans, Immunoglobulin Fc Fragments (metabolism), Membrane Glycoproteins, Murine hepatitis virus (immunology), Murine hepatitis virus (metabolism), Neutralization Tests, Receptors, Fc (immunology), Receptors, Fc (metabolism), Receptors, IgG, Recombinant Proteins (immunology), Recombinant Proteins (metabolism), Spike Glycoprotein, Coronavirus, Structure-Activity Relationship, Viral Envelope Proteins (immunology), Viral Envelope Proteins (metabolism), Viral Fusion Proteins (immunology), Viral Fusion Proteins (metabolism), Viral Matrix Proteins.
MESH :
- chemical , immunology : Antibodies, Monoclonal, Antigens, Differentiation, Receptors, Fc, Recombinant Proteins, Viral Envelope Proteins, Viral Fusion Proteins.
- chemical , metabolism : Antigens, Differentiation, Immunoglobulin Fc Fragments, Receptors, Fc, Recombinant Proteins, Viral Envelope Proteins, Viral Fusion Proteins.
- immunology : Murine hepatitis virus.
- metabolism : Murine hepatitis virus.
- Animals, Cells, Cultured, Cross Reactions, DNA Mutational Analysis, Humans, Membrane Glycoproteins, Neutralization Tests, Receptors, IgG, Spike Glycoprotein, Coronavirus, Structure-Activity Relationship, Viral Matrix Proteins.

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.

DOI: 10.1016/0042-6822(92)90066-x
PubMed: 1309271

Affiliations:

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Le document en format XML

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<front><div type="abstract" xml:lang="en">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.</div>
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<Abstract><AbstractText>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.</AbstractText>
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MHV S peplomer protein expressed by a recombinant vaccinia virus vector exhibits IgG Fc-receptor activity.

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

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