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pubmed-article:11277690pubmed:abstractTextCoronavirus small envelope protein E has two known biological functions: it plays a pivotal role in virus envelope formation, and the murine coronavirus E protein induces apoptosis in E protein-expressing cultured cells. The E protein is an integral membrane protein. Its C-terminal region extends cytoplasmically in the infected cell and in the virion toward the interior. The N-terminal two-thirds of the E protein is hydrophobic and lies buried within the membrane, but its orientation in the lipid membrane is not known. Immunofluorescent analyses of cells expressing biologically active murine coronavirus E protein with a hydrophilic short epitope tag at the N-terminus showed that the epitope tag was exposed cytoplasmically. Immunoprecipitation analyses of the purified microsomal membrane vesicles that contain the same tagged E protein revealed the N-terminal epitope tag outside the microsomal membrane vesicles. These analyses demonstrated that the epitope tag at the N-terminus of the E protein was exposed cytoplasmically. Our data were consistent with an E protein topology model, in which the N-terminal two-thirds of the transmembrane domain spans the lipid bilayer twice, exposing the C-terminal region to the cytoplasm or virion interior.lld:pubmed
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pubmed-article:11277690pubmed:copyrightInfoCopyright 2001 Academic Press.lld:pubmed
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pubmed-article:11277690pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:11277690pubmed:articleTitleMembrane topology of coronavirus E protein.lld:pubmed
pubmed-article:11277690pubmed:affiliationDepartment of Microbiology and Immunology, University of Texas Medical Branch at Galveston, Galveston, Texas 77555, USA.lld:pubmed
pubmed-article:11277690pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11277690pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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