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Biochemical characterization of the small hydrophobic protein of avian metapneumovirus
- Deng, Qiji, Song, Minxun, Demers, Andrew, Weng, Yuejin, Lu, Wuxun, Wang, Dan, Kaushik, Radhey S., Yu, Qingzhong, Li, Feng
- Virus Research 2012 v.167 no.2 pp. 297
- Avian metapneumovirus, disulfide bonds, glycoproteins, glycosylation, hydrophobicity, membrane proteins, polysaccharides, protein structure, viral proteins, virion
- 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.