Cleavage site of the poliovirus receptor signal sequence.
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 alpha and hPVR delta, 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.
Bibb
J A
JA
Department of Microbiology, State University of New York at Stony Brook 11794-8621.
Bernhardt
G
G
Wimmer
E
E
D000595:Amino Acid Sequence; D002451:Cell Compartmentation; D010450:Endopeptidases / Q000378:metabolism; D006023:Glycoproteins; D006367:HeLa Cells; D006801:Humans; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D021382:Protein Sorting Signals / Q000737:chemistry / Q000378:metabolism*; D011991:Receptors, Virus / Q000737:chemistry / Q000378:metabolism*; D011994:Recombinant Proteins; D017421:Sequence Analysis; D012697:Serine Endopeptidases
D006023:Glycoproteins; D008565:Membrane Proteins; D021382:Protein Sorting Signals; D011991:Receptors, Virus; D011994:Recombinant Proteins; C066100:poliovirus receptor; D010450:Endopeptidases; D012697:Serine Endopeptidases; C026515:type I signal peptidase