Hantavirus N Protein Exhibits Genus-Specific Recognition of the Viral RNA Panhandle

Department of Molecular Genetics and Microbiology, University of New Mexico Health Sciences Center, Albuquerque, NM 87131, USA.
Journal of Virology (Impact Factor: 4.44). 12/2006; 80(22):11283-92. DOI: 10.1128/JVI.00820-06
Source: PubMed


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 protein), which is encoded by the smallest of
the three negative-sense genomic RNA segments, 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 the Andes, Puumala, Prospect Hill, Seoul, and Sin Nombre viruses recognize their individual homologous
panhandles as well as other hantavirus panhandles with high affinity. In contrast, these hantavirus N proteins bind with markedly
reduced affinity to the panhandles from the genera Bunyavirus, Tospovirus, and Phlebovirus or Nairovirus. Interactions between most hantavirus N and heterologous hantavirus viral RNA panhandles are mediated by the nine terminal
conserved nucleotides of the panhandle, whereas Sin Nombre virus 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 while interacting 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.

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    • "Currently, some plant viruses belonging to families Bunyaviridae , Rhabdoviridae and Reoviridae are reported to infect and develop clinical disease symptoms in humans and it is expected that emergence or re-emergence of arboviruses had happened due to changes in climatic conditions especially in family Bunyaviridae (Le May and Bouloy, 2012). Some Plant viruses, such as Tospovirus, Rhabdovirus, Reovirus, Begomovirus and Nanovirus are suspected to have a minor host relationship with plants and animals (Mir et al., 2006; Hart et al., 2009; Mandal et al., 2012). Some reports have been published about the association of Plant viruses like Tobacco mosaic virus (TMV), Pepper mild mottle virus and Cowpea mosaic virus in human diseases like fever and abdominal pain causing health problems (Olszewska and Steward, 2003; Rae et al., 2005; Shriver et al., 2009; Colson et al., 2010; Mandal and Jain, 2010; Liu et al., 2013). "
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    Saudi Journal of Biological Sciences 11/2014; 30. DOI:10.1016/j.sjbs.2014.11.009 · 1.26 Impact Factor
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    • "The reported RNA-binding sites are dispersed throughout the N protein, and amino acids that contribute to binding are found at the N-terminal half (Severson et al., 2005), at residues 175–217 in the case of HTNV (Xu et al., 2002), and at the C-terminal region (Gött et al., 1993). Formation of the RNP complex is initiated by formation of a trimeric N-protein complex (Kaukinen et al., 2001), which recognizes the vRNA panhandle in a genus-specific manner (Mir et al., 2006). The conformation of N protein is altered as a result of binding to the panhandle, which probably drives oligomerization further (Hussein et al., 2011). "
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    ABSTRACT: Viruses of the genus Hantavirus, carried and transmitted by rodents and insectivores, are the exception in the vector-borne virus family Bunyaviridae, since viruses of the other genera are transmitted via arthropods. The single-stranded, negative-sense, RNA genome of hantaviruses is trisegmented into small, medium and large (S, M and L) segments. The segments, respectively, encode three structural proteins: nucleocapsid (N) protein, two glycoproteins Gn and Gc and an RNA-dependent RNA-polymerase. The genome segments, encapsidated by the N protein to form ribonucleoproteins, are enclosed inside a lipid envelope that is decorated by spikes composed of Gn and Gc. The virion displays round or pleomorphic morphology with a diameter of roughly 120-160 nm depending on the detection method. This review focuses on the structural components of hantaviruses, their interactions, the mechanisms behind virion assembly and the interactions that maintain virion integrity. We attempt to summarize recent results on the virion structure and to suggest mechanisms on how the assembly is driven. We also compare hantaviruses to other bunyaviruses with known structure.
    Journal of General Virology 05/2012; 93(Pt 8):1631-44. DOI:10.1099/vir.0.042218-0 · 3.18 Impact Factor
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    • "N protects the viral genome from degradation and prevents the formation of double stranded RNA intermediates during replication and transcription by encapsidating viral genomic and antigenomic RNA (Ruigrok et al., 2011). N also has RNA chaperone activity predicted to function during initiation of viral replication by unwinding an RNA helix that sequesters the self-complementary ends of the genome and allowing the polymerase to bind (Mir and Panganiban, 2006a, b). This activity could also remove higher order RNA structures that decrease the speed and efficiency of translation of viral mRNA. "
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