Human parainfluenza virus type 2 V protein inhibits and antagonizes tetherin

Tetherin (BST-2/CD317/HM1.24) is an antiviral membrane protein that prevents the release of enveloped viruses from the cell surface. We found that the growth of human parainfluenza virus type 2 (hPIV-2), but not that of V protein-deficient recombinant hPIV-2, was inhibited by tetherin. V protein imm...

Full description

Saved in:
Bibliographic Details
Published in:Journal of general virology 2016-03, Vol.97 (3), p.561-570
Main Authors: Ohta, K, Goto, H, Yumine, N, Nishio, M
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Antigens, CD - chemistry
Antigens, CD - genetics
Antigens, CD - metabolism
Croup - genetics
Croup - metabolism
Croup - virology
GPI-Linked Proteins - antagonists & inhibitors
GPI-Linked Proteins - chemistry
GPI-Linked Proteins - genetics
GPI-Linked Proteins - metabolism
Host-Pathogen Interactions
Humans
Parainfluenza Virus 2, Human - chemistry
Parainfluenza Virus 2, Human - genetics
Parainfluenza Virus 2, Human - metabolism
Paramyxoviridae
Protein Binding
Viral Proteins - chemistry
Viral Proteins - genetics
Viral Proteins - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Tetherin (BST-2/CD317/HM1.24) is an antiviral membrane protein that prevents the release of enveloped viruses from the cell surface. We found that the growth of human parainfluenza virus type 2 (hPIV-2), but not that of V protein-deficient recombinant hPIV-2, was inhibited by tetherin. V protein immunoprecipitates with tetherin, and this interaction requires its C-terminal Trp residues. The glycosyl phosphatidylinositol attachment signal of tetherin, but not its cytoplasmic tail, was necessary for its binding with V. The distribution of the V protein clearly changed when co-expressed with tetherin in plasmid-transfected cells. hPIV-2 infection of HeLa cells reduced cell surface tetherin without affecting total cellular tetherin. This reduction also occurred in HeLa cells constitutively expressing V, whereas mutated V protein did not affect the cell surface tetherin. Our results suggest that hPIV-2 V protein antagonizes tetherin by binding it and reducing its presence at the cell surface.
ISSN:0022-1317
1465-2099
DOI:10.1099/jgv.0.000373