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J Gen Virol 64 (1983), 1241-1253; DOI 10.1099/0022-1317-64-6-1241
© 1983 Society for General Microbiology

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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

Jero Calafat, H. Janssen, P. Démant, J. Hilgers and J. Závada1

Division of Genetics, Antoni van Leeuwenhoekhuis, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands
and1 Institute of Virology, Slovak Academy of Sciences, Bratislava, Czechoslovakia

Using the indirect immunoelectron microscopy technique, it was investigated whether during assembly of murine leukaemia virus (MuLV) and vesicular stomatitis virus (VSV), the glycoproteins (gp) Thy-1, H-2, Pgp-1 and T-200 present on the surface of BW5147 and BuEL4 leukaemia cell lines were incorporated into the virus envelopes. This work was done mainly with monoclonal antibodies against these gps to exclude the presence of antibodies against endogenous MuLV present in conventional mouse antisera. Thy-1 gps were incorporated into MuLV and VSV envelopes. In contrast, H-2, Pgp-1 and T-200 gps were excluded from the budding of both virus particles. To study whether the presence of Thy-1 gps on the viral envelopes is due to some lateral affinity of this molecule with viral gps, 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 gps and that a selection of surface gps takes place during assembly of MuLV and VSV.

Keywords: MuLV, VSV, glycoprotein selection, Thy-1 glycoprotein

Received 16 November 1982; accepted 10 February 1983.


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