Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
3424519 | Virology | 2011 | 9 Pages |
We recently characterized the interaction between the intraviral domains of envelope glycoproteins (Gn and Gc) and ribonucleoprotein (RNP) of Puumala and Tula hantaviruses (genus Hantavirus, family Bunyaviridae). Herein we report a direct interaction between spike-forming glycoprotein and nucleic acid. We show that the envelope glycoprotein Gn of hantaviruses binds genomic RNA through its cytoplasmic tail (CT). The nucleic acid binding of Gn-CT is unspecific, as demonstrated by interactions with unrelated RNA and with single-stranded DNA. Peptide scan and protein deletions of Gn-CT mapped the nucleic acid binding to regions that overlap with the previously characterized N protein binding sites and demonstrated the carboxyl-terminal part of Gn-CT to be the most potent nucleic acid-binding site. We conclude that recognition of the RNP complex by the Gn-CT could be mediated by interactions with both genomic RNA and the N protein. This would provide the required selectivity for the genome packaging of hantaviruses.
► Genomic RNA binding activity of hantavirus Gn. ► Gn cytoplasmic tails of Puumala and Tula hantaviruses bind RNA and DNA. ► No evidence for specificity. ► Nucleic acid-binding activity of Gn tail is mainly located to its C-terminal part. ► Possible role in virus assembly and/or transcription.