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

ABSTRACT: 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.

SUBMITTER: Estrada DF

PROVIDER: S-EPMC2659224 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature

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

Estrada D Fernando DF Boudreaux Daniel M DM Zhong Dalian D St Jeor Stephen C SC De Guzman Roberto N RN

The Journal of biological chemistry 20090129 13

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 con ...[more]

PMID: 19179334

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