The surface protein gp70 of an ecotropic murine retrovirus was followed during entry of [H]glucosamine-labelled virions into SC-1 mouse fibroblasts. Upon entry, gp70 was cleaved into fragments with molecular weights 35K, 30K and 17K. The 35K and 17K fragments were also observed after trypsin or thermolysin cleavage of the virion, indicating that certain locations on the gp70 molecule are easily accessible from the outside of the virion. The conformation of gp70 on the membrane was shown to have a major effect on the cleavage. This protein is known to be important for early interactions with the cell (binding and membrane fusion). The results indicate that gp70 cleavage may be important for membrane fusion.


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