|Deng, Qiji -|
|Song, Minxun -|
|Demers, Andrew -|
|Weng, Yuejin -|
|Lu, Wuxun -|
|Wang, Dan -|
|Kaushik, Radhey -|
|Li, Feng -|
Submitted to: Virus Research
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: May 16, 2012
Publication Date: August 1, 2012
Citation: Deng, Q., Song, M., Demers, A., Weng, Y., Lu, W., Wang, D., Kaushik, R.S., Yu, Q., Li, F. 2012. Biochemical characterization of the small hydrophobic protein of avian metapneumovirus. Virus Research. 167:297-301. Interpretive Summary: Avian metapneumovirus (aMPV), previously known as turkey rhinotracheitis virus or avian pneumovirus, is a paramyxovirus that causes acute respiratory disease in turkeys and has recently emerged as a major economic problem for the world-wide poultry industry. Like some of paramyxoviruses, aMPV has a membrane-associate small hydrophobic protein (SH). Sequence analyses have shown that SH proteins among the different paramyxoviruses vary significantly in size as well as the primary sequence. However, little is known about the function of the SH protein in virus pathogenesis. In the present study, we characterized aMPV SH protein with respect to its biological properties. We showed that the aMPV SH protein is modified by N-linked sugars and can be released into the extracellular environment. Furthermore, we demonstrated that sugar linked aMPV SH proteins form homodimers through cysteine-mediated disulfide bonds, which has not been reported previously for the SH proteins of paramyxoviruses. Taken together, our study has demonstrated some important biochemical properties of metapneumovirus SH protein and represents the first step toward defining the role of SH protein in metapneumovirus replication and pathogenesis.
Technical Abstract: Avian metapneumovirus (aMPV) is a paramyxovirus that has three membrane-associate proteins: glycoprotein (G), fusion (F), and small hydrophobic (SH) proteins. 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 showed that the aMPV SH protein is modified by N-linked glycans and can be released into the extracellular environment. Furthermore, we demonstrated that glycosylated aMPV SH proteins form homodimers through cysteine-mediated disulfide bonds, which has not been reported previously for the SH proteins of paramyxoviruses.