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The Hantavirus Glycoprotein G1 Tail Contains Dual CCHC-type Classical Zinc Fingers

D Fernando Estrada1, Daniel M Boudreaux, Dalian Zhong

  • 1Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045.

The Journal of Biological Chemistry
|January 31, 2009
PubMed

Hantaviruses are distributed worldwide and can cause a hemorrhagic fever or a cardiopulmonary syndrome in humans. Mature virions consist of RNA genome, nucleocapsid protein, RNA polymerase, and two transmembrane glycoproteins, G1 and G2. The ectodomain of G1 is surface-exposed; however, it has a 142-residue C-terminal cytoplasmic tail that plays important roles in viral assembly and host-pathogen interaction. Here we show by NMR, circular dichroism spectroscopy, and mutagenesis that a highly conserved cysteine/histidine-rich region in the G1 tail of hantaviruses forms two CCHC-type classical zinc fingers. Unlike classical zinc fingers, however, the two G1 zinc fingers are intimately joined together, forming a compact domain with a unique fold. We discuss the implication of the hantaviral G1 zinc fingers in viral assembly and host-pathogen interaction.

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