A New Type of Signal Peptidase Cleavage Site Identified in an RNA Virus Polyprotein

被引:32
作者
Bintintan, Ioana [1 ]
Meyers, Gregor [1 ]
机构
[1] Friedrich Loeffler Inst, Inst Immunol, D-72001 Tubingen, Germany
关键词
VIRAL-DIARRHEA-VIRUS; SWINE-FEVER VIRUS; GLYCOPROTEIN E-RNS; BREFELDIN-A; PESTIVIRUS GLYCOPROTEIN; SECRETORY PROTEINS; INTRACELLULAR-TRANSPORT; MONOCLONAL-ANTIBODIES; ENDOPLASMIC-RETICULUM; GENE-EXPRESSION;
D O I
10.1074/jbc.M109.083394
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Pestiviruses, a group of enveloped positive strand RNA viruses belonging to the family Flaviviridae, express their genes via a polyprotein that is subsequently processed by proteases. The structural protein region contains typical signal peptidase cleavage sites. Only the site at the C terminus of the glycoprotein E-rns is different because it does not contain a hydrophobic transmembrane region but an amphipathic helix functioning as the Erns membrane anchor. Despite the absence of a hydrophobic region, the site between the C terminus of E-rns and E1, the protein located downstream in the polyprotein, is cleaved by signal peptidase, as demonstrated by mutagenesis and inhibitor studies. Thus, E(rns)E1 is processed at a novel type of signal peptidase cleavage site showing a different membrane topology. Prevention of glycosylation or introduction of mutations into the C-terminal region of E-rns severely impairs processing, presumably by preventing proper membrane interaction or disturbing a conformation critical for the protein to be accepted as a substrate by signal peptidase.
引用
收藏
页码:8572 / 8584
页数:13
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