PROCESSING OF VIRAL GLYCOPROTEINS BY THE SUBTILISIN-LIKE ENDOPROTEASE FURIN AND ITS INHIBITION BY SPECIFIC PEPTIDYLCHLOROALKYLLKETONES

被引：142

作者：

GARTEN, W ^{[1
]}

HALLENBERGER, S ^{[1
]}

ORTMANN, D ^{[1
]}

SCHAFER, W ^{[1
]}

VEY, M ^{[1
]}

ANGLIKER, H ^{[1
]}

SHAW, E ^{[1
]}

KLENK, HD ^{[1
]}

机构：

[1] FRIEDRICH MIESCHER INST,CH-4002 BASEL,SWITZERLAND

来源：

BIOCHIMIE | 1994年 / 76卷 / 3-4期

关键词：

VIRAL GLYCOPROTEINS; PROTEOLYTIC ACTIVATION; FURIN; PEPTIDYLCHLOROALKYLKETONES;

D O I：

10.1016/0300-9084(94)90149-X

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：

The spike glycoproteins of many enveloped viruses are proteolytically cleaved at the carboxytermini of sequences containing the basic motif R-X-K/R-R. Cleavage is often necessary for the fusion capacity of the glycoproteins and, thus, for virus infectivity. Among these viruses are pathogenic avian influenza viruses, human parainfluenza virus, human cytomegalovirus, and human immunodeficiency virus; it has been demonstrated that these viruses can be activated by furin. Indigenous furin has been identified in T-lymphocytes, which are host cells for HIV. Furin has been localized in the TGN and on the surface of cells after vectorial expression. Peptidylchloroalkylketones have been designed that inhibit with high specificity cleavage and fusion activity of viral glycoproteins, as well as virus replication.

引用

页码：217 / 225

页数：9

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[41] MULTIPLE TARGETS FOR BREFELDIN-A [J].