About: covid:ann/target/0f8c54af6b35d8dfe3aa7e64c4befa8d8efbc94b

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About: covid:ann/target/0f8c54af6b35d8dfe3aa7e64c4befa8d8efbc94b Goto Sponge NotDistinct Permalink

An Entity of Type : owl:Thing, within Data Space : covidontheweb.inria.fr associated with source document(s)

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hasSource	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 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.
hasSelector	covid:ann/selector/0f8c54af6b35d8dfe3aa7e64c4befa8d8efbc94b
is hasTarget of	named entity 'IDENTIFIED'

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