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Department of Microbiology, State University of New York at Stony Brook, Stony Brook, New York 11794-8621, U.S.A.
We have shown recently that the human poliovirus receptors (hPVRs) expressed on the surface of cultured cells are 80K glycoproteins, whereas the previously reported 67K forms are partially glycosylated intermediate glycoforms. Both the membrane-bound 80K and 67K forms of hPVR are glycosylated derivatives of the two isoforms hPVR
and hPVR
, where the latter two can be resolved only by SDS-PAGE upon enzymatic deglycosylation. Here we report the N-terminal sequence analysis of the mature 80K as well as the intermediate 67K glycoforms of hPVR which has allowed us to identify the signal peptidase cleavage site of the unprocessed hPVR. The signal sequence that directs translocation of hPVR across the membrane of the endoplasmic reticulum on its route to the glycoprocessing pathway has thus been defined. We compare this signal sequence with those of the putative monkey poliovirus receptor and the mouse poliovirus receptor homologue.
Present address: Laboratory of Molecular and Cellular Neuroscience, The Rockefeller University, 1230 York Avenue, New York, New York 10021-6399, U.S.A.
Received 26 November 1993;
accepted 3 March 1994.
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