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Department of Molecular Genetics and Microbiology, Department of Pathology, and the Infectious Disease and Inflammation Program, University of New Mexico Health Sciences Center, Albuquerque, NM 87131
* To whom correspondence should be addressed. Email:
apanganiban{at}salud.unm.edu.
A key genomic characteristic that helps define Hantavirus as a genus of the family Bunyaviridae is the presence of distinctive terminal complementary nucleotides that promote the folding of the viral genomic segments into "panhandle" hairpin structures. The hantavirus nucleocapsid protein (N), which is encoded by the smallest of the three negative sense genomic RNA segments (S), undergoes in vivo and in vitro trimerization. Trimeric hantavirus N protein specifically recognizes the panhandle structure formed by complementary base sequence of 5' and 3' ends of viral genomic RNA. N protein trimers from Andes, Puumala, Prospect Hill, Seoul, and Sin nombre virus recognize with high affinity their individual homologous panhandles as well as other hantavirus panhandles. In contrast, these hantavirus N proteins bind with markedly reduced affinity to the panhandles from the bunyavirus, tospovirus, and phlebovirus or nairovirus genera. Interactions between most hantavirus N and heterologous hantavirus vRNA panhandles are mediated by the terminal conserved nine nucleotides of the panhandle, whereas SNV N requires the first 23 nucleotides for high affinity binding. Trimeric hantavirus N complexes undergo a prominent conformational change while interacting with panhandles from members of the genus Hantavirus but not with panhandles from viruses of other genera of the family Bunyaviridae. These data indicate that high-affinity interactions between trimeric N and hantavirus panhandles are conserved within the genus Hantavirus.
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.
Hantavirus N Protein Exhibits Genus-Specific Recognition of the vRNA Panhandle
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Abstract
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