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

doi:10.1016/j.virusres.2012.05.013

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

Veterinary Science

Research output: Contribution to journal › Article › peer-review

2 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 language	English
Pages (from-to)	297-301
Number of pages	5
Journal	Virus Research
Volume	167
Issue number	2
DOIs	https://doi.org/10.1016/j.virusres.2012.05.013
State	Published - 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

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.virusres.2012.05.013

Cite this

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title = "Biochemical characterization of the small hydrophobic protein of avian metapneumovirus",

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.",

keywords = "Avian metapneumovirus, Glycosylation, Homodimer, Paramyxoviruses, RNA viruses, SH protein",

author = "Qiji Deng and Minxun Song and Andrew Demers and Yuejin Weng and Wuxun Lu and Dan Wang and Kaushik, {Radhey S.} and Qingzhong Yu and Feng Li",

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).",

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doi = "10.1016/j.virusres.2012.05.013",

language = "English",

volume = "167",

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AU - Deng, Qiji

AU - Song, Minxun

AU - Demers, Andrew

AU - Weng, Yuejin

AU - Lu, Wuxun

AU - Wang, Dan

AU - Kaushik, Radhey S.

AU - Yu, Qingzhong

AU - Li, Feng

N1 - 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).

PY - 2012/8

Y1 - 2012/8

N2 - 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.

AB - 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.

KW - Avian metapneumovirus

KW - Glycosylation

KW - Homodimer

KW - Paramyxoviruses

KW - RNA viruses

KW - SH protein

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SP - 297

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ER -

Biochemical characterization of the small hydrophobic protein of avian metapneumovirus

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

UN SDGs

Access to Document

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