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Topology and cellular localization of the small hydrophobic protein of avian metapneumovirus

文献类型： 外文期刊

作者： Deng, Qiji 1 ; Weng, Yuejin 1 ; Lu, Wuxun 2 ; Demers, Andrew 2 ; Song, Minxun 4 ; Wang, Dan 2 ; Yu, Qingzhong 5 ; Li, Fen 1 ;

作者机构： 1.S Dakota State Univ, Dept Vet & Biomed Sci, Brookings, SD 57007 USA

2.S Dakota State Univ, Dept Biol & Microbiol, Brookings, SD 57007 USA

3.S Dakota State Univ, Ctr Infect Dis Res & Vaccinol, Brookings, SD 57007 USA

4.Shandong Acad Agr Sci, Inst Poultry Sci, Jinan 250023, Peoples R China

5.ARS, SE Poultry

关键词： Avian metapneumovirus;Topology;Subcellular localization;Transport

期刊名称：VIRUS RESEARCH （ 影响因子：3.303； 五年影响因子：3.445 ）

ISSN： 0168-1702

年卷期： 2011 年 160 卷 1-2 期

页码：

收录情况： SCI

摘要： The small hydrophobic protein (SH) is a type II integral membrane protein that is packaged into virions and is only present in certain paramyxoviruses including metapneumovirus. In addition to a highly divergent primary sequence, SH proteins vary significantly in size amongst the different viruses. Human respiratory syncytial virus (HRSV) encodes the smallest SH protein consisting of only 64 amino acids, while metapneumoviruses have the longest SH protein ranging from 174 to 179 amino acids in length. Little is currently known about the cellular localization and topology of the metapneumovirus SH protein. Here we characterize for the first time metapneumovirus SH protein with respect to topology, subcellular localization, and transport using avian metapneumovirus subgroup C (AMPV-C) as a model system. We show that AMPV-C SH is an integral membrane protein with N(in)C(out) orientation located in both the plasma membrane as well as within intracellular compartments, which is similar to what has been described previously for SH proteins of other paramyxoviruses. Furthermore, we demonstrate that AMPV-C SH protein localizes in the endoplasmic reticulum (ER), Golgi, and cell surface, and is transported through ER-Golgi secretory pathway. (C) 2011 Elsevier B.V. All rights reserved.

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