Trimeric hantavirus nucleocapsid protein binds specifically to the viral RNA panhandle.

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 Virol

journal_title

Journal of virology

authors

Mir MA,Panganiban AT

doi

10.1128/JVI.78.15.8281-8288.2004

subject

Has Abstract

pub_date

2004-08-01 00:00:00

pages

8281-8

issue

15

eissn

0022-538X

issn

1098-5514

pii

78/15/8281

journal_volume

78

pub_type

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