Membrane Organization of Bluetongue Virus Nonstructural Glycoprotein NS3
نویسندگان
چکیده
منابع مشابه
Membrane organization of bluetongue virus nonstructural glycoprotein NS3.
The smallest RNA segment (S10) of bluetongue virus (an orbivirus, family Reoviridae) encodes two closely related nonstructural proteins, the 229-amino-acid (aa) NS3 and the 216-aa NS3A. The proteins are found in glycosylated and nonglycosylated forms in infected cells (X. Wu, H. Iwata, S.-Y. Chen, R. W. Compans and P. Roy J. Virol. 66:7104-7112, 1992). The NS3/NS3A proteins have two hydrophobic...
متن کاملBluetongue Virus Nonstructural Protein NS3/NS3a Is Not Essential for Virus Replication
Orbiviruses form the largest genus of the family Reoviridae consisting of at least 23 different virus species. One of these is the bluetongue virus (BTV) and causes severe hemorrhagic disease in ruminants, and is transmitted by bites of Culicoides midges. BTV is a non-enveloped virus which is released from infected cells by cell lysis and/or a unique budding process induced by nonstructural pro...
متن کاملThe membrane trafficking protein calpactin forms a complex with bluetongue virus protein NS3 and mediates virus release.
Bluetongue virus, an arbovirus of the Orbivirus genus, infects and replicates in both insect and mammalian cells. However, the cytopathic effect (cpe) on each host is very different. Mammalian cells show substantial cpe, most likely a result of the mechanism of virus release, whereas insect cells show little cpe and appear to release virus without cell lysis. Expression analysis of each infecte...
متن کاملNonstructural protein 3 of bluetongue virus assists virus release by recruiting ESCRT-I protein Tsg101.
The release of Bluetongue virus (BTV) and other members of the Orbivirus genus from infected host cells occurs predominantly by cell lysis, and in some cases, by budding from the plasma membrane. Two nonstructural proteins, NS3 and NS3A, have been implicated in this process. Here we show that both proteins bind to human Tsg101 and its ortholog from Drosophila melanogaster with similar strengths...
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The stoichiometry, cellular location, glycosylation, and hydrophobic properties of the components in the dystrophin-glycoprotein complex were examined. The 156, 59, 50, 43, and 35 kd dystrophin-associated proteins each possess unique antigenic determinants, enrich quantitatively with dystrophin, and were localized to the skeletal muscle sarcolemma. The 156, 50, 43, and 35 kd dystrophin-associat...
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ژورنال
عنوان ژورنال: Journal of Virology
سال: 1998
ISSN: 0022-538X,1098-5514
DOI: 10.1128/jvi.72.4.3362-3369.1998