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

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

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...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry Vol. 284; no. 13; pp. 8654 - 8660
Main Authors: Estrada, D.Fernando, Boudreaux, Daniel M., Zhong, Dalian, St. Jeor, Stephen C., De Guzman, Roberto N.
Format: Journal Article
Language:English
Published: United States Elsevier Inc 27-03-2009
American Society for Biochemistry and Molecular Biology
Subjects:
Cell Membrane - chemistry
Cell Membrane - metabolism
Cytoplasm - chemistry
Cytoplasm - metabolism
Hantavirus
Hantavirus - chemistry
Hantavirus - physiology
Hantavirus Pulmonary Syndrome - metabolism
Hemorrhagic Fevers, Viral - metabolism
Host-Pathogen Interactions - physiology
Humans
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Tertiary - physiology
Viral Envelope Proteins - chemistry
Viral Envelope Proteins - metabolism
Virus Assembly - physiology
Zinc Fingers - physiology
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M808081200