Interaction between hantaviral nucleocapsid protein and the cytoplasmic tail of surface glycoprotein Gn.
Hantaviral N and Gn proteins were shown to interact, thus providing the long-awaited evidence for one of the crucial steps in the virus replication at which RNPs are directed to the site of the virus assembly. Using pull-down assay and point mutagenesis it was demonstrated that intact, properly folded zinc fingers in the Gn protein cytoplasmic tail as well as the middle domain of the N protein (that includes aa residues 80-248) are essential for the interaction.
Wang
Hao
H
Department of Virology, Infection Biology Research Program, Haartman Institute, University of Helsinki, Finland. hao.wang@helsinki.fi
Alminaite
Agne
A
Vaheri
Antti
A
Plyusnin
Alexander
A
D000595:Amino Acid Sequence; D002460:Cell Line; D006476:Orthohantavirus / Q000502:physiology*; D006801:Humans; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019590:Nucleocapsid Proteins / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D025941:Protein Interaction Mapping; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D014764:Viral Proteins / Q000378:metabolism*
D008562:Membrane Glycoproteins; D019590:Nucleocapsid Proteins; D014764:Viral Proteins