Biochemical characterization of the small hydrophobic protein of avian metapneumovirus

Qiji Deng, Minxun Song, Andrew Demers, Yuejin Weng, Wuxun Lu, Dan Wang, Radhey S. Kaushik, Qingzhong Yu, Feng Li

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

Avian metapneumovirus (AMPV) is a paramyxovirus that has three membrane proteins (G, F, and SH). Among them, the SH protein is a small type II integral membrane protein that is incorporated into virions and is only present in certain paramyxoviruses. In the present study, we show that the AMPV SH protein is modified by N-linked glycans and can be released into the extracellular environment. Furthermore, we demonstrate that glycosylated AMPV SH proteins form homodimers through cysteine-mediated disulfide bonds, which has not been reported previously for SH proteins of paramyxoviruses.

Original languageEnglish
Pages (from-to)297-301
Number of pages5
JournalVirus Research
Volume167
Issue number2
DOIs
StatePublished - Aug 2012

Bibliographical note

Funding Information:
We thank Elizabeth Kolb for editing the manuscript and Xiuqin Xia for outstanding technical assistance. This work was supported by the SD AES ( 3AH203 to FL), NIH 5K02AI076125-02 award to FL, and USDA , ARS CRIS project 6612-32000-056-00D (to QY).

Keywords

  • Avian metapneumovirus
  • Glycosylation
  • Homodimer
  • Paramyxoviruses
  • RNA viruses
  • SH protein

ASJC Scopus subject areas

  • Cancer Research
  • Virology
  • Infectious Diseases

Fingerprint

Dive into the research topics of 'Biochemical characterization of the small hydrophobic protein of avian metapneumovirus'. Together they form a unique fingerprint.

Cite this