Mobility and interactions of coronavirus nonstructural protein 4.

Article Details

Citation

Hagemeijer MC, Ulasli M, Vonk AM, Reggiori F, Rottier PJ, de Haan CA

Mobility and interactions of coronavirus nonstructural protein 4.

J Virol. 2011 May;85(9):4572-7. doi: 10.1128/JVI.00042-11. Epub 2011 Feb 23.

PubMed ID
21345958 [ View in PubMed
]
Abstract

Green fluorescent protein (GFP)-tagged mouse hepatitis coronavirus nonstructural protein 4 (nsp4) was shown to localize to the endoplasmic reticulum (ER) and to be recruited to the coronavirus replicative structures. Fluorescence loss in photobleaching and fluorescence recovery after photobleaching experiments demonstrated that while the membranes of the ER are continuous with those harboring the replicative structures, the mobility of nsp4 at the latter structures is relatively restricted. In agreement with that observation, nsp4 was shown to be engaged in homotypic and heterotypic interactions, the latter with nsp3 and nsp6. In addition, the coexpression of nsp4 with nsp3 affected the subcellular localization of the two proteins.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Replicase polyprotein 1abP0C6X7Details