Specific Selection of Host Cell Glycoproteins during Assembly of Murine Leukaemia Virus and Vesicular Stomatitis Virus: Presence of Thy-1 Glycoprotein and Absence of H-2, Pgp-1 and T-200 Glycoproteins on the Envelopes of these Virus Particles

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Abstract
Using the indirect immunoelectron microscopy technique, it was investigated whether during assembly of murine leukemia virus (MuLV) and vesicular stomatitis virus (VSV), the glycoproteins (gp) Thy-1, H-2, and T-200 present on the surface of mouse BW5147 and BuEL4 leukemia cell lines were incorporated into the virus envelopes. This work was done mainly with monoclonal antibodies against these gp to exclude the presence of antibodies against endogenous MuLV present in conventional mouse antisera. Thy-1 gp were incorporated into MuLV and VSV envelopes. H-2, Pgp-1 and T-200 gp were excluded from the budding of both virus particles. To study whether the presence of Thy-1 gp on the viral envelopes is due to some lateral affinity of this molecule with viral gp, the physical association of Thy-1.1 antigens and MuLV antigens was studied with antibody-induced redistribution of both antigens on the BW5147 cell surface. Antibody-induced patching of the viral antigens did not result in co-patching of the Thy-1.1 antigens. In the reciprocal tests no co-redistribution of viral antigens with Thy-1.1 antigens was seen. These studies show that the presence of Thy-1.1 gp on the MuLV envelope cannot be due to a lateral affinity of this molecule with viral gp and that a selection of surface gp takes place during assembly of MuLV and VSV.