title: The cytoplasmic tail of hantavirus Gn glycoprotein interacts with RNA.
abstract: 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.
authors.affiliation: Peptide and Protein Laboratory, Infection Biology Research Program, Haartman Institute, PO Box 21, FI-00014, University of Helsinki, Finland. tomas.strandin@helsinki.fi
authors.forename: Tomas
authors.initials: T
authors.lastname: Strandin
authors.forename: Jussi
authors.initials: J
authors.lastname: Hepojoki
authors.forename: Hao
authors.initials: H
authors.lastname: Wang
authors.forename: Antti
authors.initials: A
authors.lastname: Vaheri
authors.forename: Hilkka
authors.initials: H
authors.lastname: Lankinen
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002522:Chlorocebus aethiops; D006023:Glycoproteins / Q000378:metabolism*; D006476:Orthohantavirus / Q000502:physiology*; D008969:Molecular Sequence Data; D011485:Protein Binding; D029262:Puumala virus; D012367:RNA, Viral / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000378:metabolism; D017384:Sequence Deletion; D014709:Vero Cells; D014759:Viral Envelope Proteins / Q000378:metabolism*
chemical_list: D006023:Glycoproteins; D012367:RNA, Viral; D016601:RNA-Binding Proteins; D014759:Viral Envelope Proteins