Abstract:
:Hantaviruses are tripartite negative-sense RNA viruses and members of the Bunyaviridae family. The nucleocapsid (N) protein is encoded by the smallest of the three genome segments (S). N protein is the principal structural component of the viral capsid and is central to the hantavirus replication cycle. We examined intermolecular N-protein interaction and RNA binding by using bacterially expressed Sin Nombre virus N protein. N assembles into di- and trimeric forms. The mono- and dimeric forms exist transiently and assemble into a trimeric form. In contrast, the trimer is highly stable and does not efficiently disassemble into the mono- and dimeric forms. The purified N-protein trimer is able to discriminate between viral and nonviral RNA molecules and, interestingly, recognizes and binds with high affinity the panhandle structure composed of the 3' and 5' ends of the genomic RNA. In contrast, the mono- and dimeric forms of N bind RNA to form a complex that is semispecific and salt sensitive. We suggest that trimerization of N protein is a molecular switch to generate a protein complex that can discriminate between viral and nonviral RNA molecules during the early steps of the encapsidation process.
journal_name
J Viroljournal_title
Journal of virologyauthors
Mir MA,Panganiban ATdoi
10.1128/JVI.78.15.8281-8288.2004subject
Has Abstractpub_date
2004-08-01 00:00:00pages
8281-8issue
15eissn
0022-538Xissn
1098-5514pii
78/15/8281journal_volume
78pub_type
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pub_type: 杂志文章
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journal_title:Journal of virology
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更新日期:1979-02-01 00:00:00
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journal_title:Journal of virology
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更新日期:1991-09-01 00:00:00
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pub_type: 杂志文章
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更新日期:1985-01-01 00:00:00