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Nuclear import of the respiratory syncytial virus matrix protein is mediated by importin beta1 independent of importin alpha.

التفاصيل البيبلوغرافية
العنوان: Nuclear import of the respiratory syncytial virus matrix protein is mediated by importin beta1 independent of importin alpha.
بيانات النشر: American Chemical Society (2540 Olentangy River Road, P.O. Box 3337, Columbus OH 43210-3337, United States) United States 2012-10-18
تفاصيل مُضافة: Dias M.M.
Bardin P.
Jans D.A.
Jans P.
Barton C.L.
Ghildyal R.
Ho A.
Wagstaff K.M.
نوع الوثيقة: Electronic Resource
مستخلص: The matrix (M) protein of respiratory syncytial virus (RSV) plays an important role in virus assembly through specific interactions with RSV nucleocapsids and envelope glycoproteins in the cytoplasm as well as with the host cell membrane. We have previously shown that M localizes to the nucleus of infected cells at an early stage in the RSV infection cycle, where it may be instrumental in inhibiting host cell processes. The present study uses transient expression of M as well as a truncated green fluorescent protein (GFP) fusion derivative to show for the first time that M is able to localize in the nucleus in the absence of other RSV gene products, through the action of amino acids 110-183, encompassing the nucleic acid binding regions of the protein, that are sufficient to target GFP to the nucleus. Using native PAGE, ELISA-based binding assays, a novel Alphascreen assay, and an in vitro nuclear transport assay, we show that M is recognized directly by the importin beta1 nuclear import receptor, which mediates its nuclear import in concert with the guanine nucleotide-binding protein Ran. Retention of M in the nucleus through binding to nuclear components, probably mediated by the putative zinc finger domain of M, also contributes to M nuclear accumulation. This is the first report of the importin binding and nuclear import properties of a gene product from a negative sense RNA virus, with implications for the function of RSV M and possibly other viral M proteins in the nucleus of infected cells. © 2005 American Chemical Society.
مصطلحات الفهرس: enzyme linked immunosorbent assay, animal cell, article, cell membrane, cell nucleus, cellular distribution, controlled study, nonhuman, priority journal, protein analysis, protein assembly, protein domain, protein interaction, Respiratory syncytial pneumovirus, RNA virus, virus infection, virus nucleocapsid, amino acid derivative, envelope protein/ec [Endogenous Compound], gene product/ec [Endogenous Compound], green fluorescent protein, guanine nucleotide binding protein/ec [Endogenous Compound], karyopherin alpha/ec [Endogenous Compound], karyopherin beta/ec [Endogenous Compound], M protein/ec [Endogenous Compound], virus protein/ec [Endogenous Compound], virus RNA/ec [Endogenous Compound], zinc finger protein/ec [Endogenous Compound], Article
URL: https://repository.monashhealth.org/monashhealthjspui/handle/1/32312
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الإتاحة: Open access content. Open access content
Copyright 2012 Elsevier B.V., All rights reserved.
أرقام أخرى: AUSHL oai:repository.monashhealth.org:1/32312
Biochemistry. 44 (38) (pp 12887-12895), 2005. Date of Publication: 27 Sep 2005.
0006-2960
https://repository.monashhealth.org/monashhealthjspui/handle/1/32312
16171404 [http://www.ncbi.nlm.nih.gov/pubmed/?term=16171404]
41377328
(Ho, Wagstaff, Dias, Barton, Jans, Jans) Department of Biochemistry and Molecular Biology, Monash University, Clayton, Vic. 3800, Australia (Ghildyal) Department of Microbiology, Monash University, Clayton, Vic., Australia (Ghildyal, Bardin) Department of Respiratory and Sleep Medicine, Monash Medical Centre, Clayton, Vic., Australia (Jans) Australian Research Council Centre of Excellence for Biotechnology and Development, Australia
Jans D.A.; David.Jans@med.monash.edu.au
1305131986
المصدر المساهم: MONASH HEALTH LIBRS
From OAIster®, provided by the OCLC Cooperative.
رقم الأكسشن: edsoai.on1305131986
قاعدة البيانات: OAIster
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