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J. Virol., 01 1997, 778-784, Vol 71, No. 1
PA Goepfert, KL Shaw, GD Ritter Jr and MJ Mulligan
We recently identified an endoplasmic reticulum (ER) retrieval signal- the
dilysine motif-in the glycoproteins of all five foamy viruses (FVs) for
which sequences were available (P. A. Goepfert, G. Wang, and M. J.
Mulligan, Cell 82:543-544, 1995). In the present study, expression of
recombinant human FV (HFV) glycoprotein and analyses of oligosaccharide
modifications and precursor cleavage indicated that the protein was
localized to the ER. HFV glycoproteins encoding seven different dilysine
motif mutations were then expressed. The results indicated that disruptions
of the dilysine motif resulted in higher levels of forward transport of the
HFV glycoprotein from the ER through the Golgi apparatus to the plasma
membrane. We conclude that the dilysine motif is responsible for ER sorting
of the FV glycoprotein. Signal-mediated ER localization has not previously
been described for a retroviral glycoprotein.
Copyright © 1997, American Society for Microbiology
A sorting motif localizes the foamy virus glycoprotein to the endoplasmic reticulum
Department of Medicine, University of Alabama at Birmingham, 35294- 2170, USA.
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