Biochemical characterization of the small hydrophobic protein of avian metapneumovirus.
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.
Department of Veterinary and Biomedical Sciences, South Dakota State University, Brookings, SD 57007, United States.
Qiji
Q
Deng
Minxun
M
Song
Andrew
A
Demers
Yuejin
Y
Weng
Wuxun
W
Lu
Dan
D
Wang
Radhey S
RS
Kaushik
Qingzhong
Q
Yu
Feng
F
Li
D000818:Animals; D019556:COS Cells; D002522:Chlorocebus aethiops; D004220:Disulfides; D006031:Glycosylation; D057927:Hydrophobic and Hydrophilic Interactions; D029121:Metapneumovirus / Q000502:physiology*; D011134:Polysaccharides / Q000378:metabolism; D055503:Protein Multimerization; D011499:Protein Processing, Post-Translational; D014763:Viral Matrix Proteins / Q000737:chemistry / Q000378:metabolism*
D004220:Disulfides; D011134:Polysaccharides; D014763:Viral Matrix Proteins