Linked Life Data

21343309

Source:http://linkedlifedata.com/resource/pubmed/id/21343309

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
2011-4-18
pubmed:abstractText
CD81 is a tetraspanin protein that is involved in several essential cellular functions, as well as in the hepatitis C virus (HCV) infection. CD81 interacts with a high stoichiometry with its partner proteins EWI-2, EWI-2wint, and EWI-F. These latter proteins modify the functions of CD81 and can thereby potentially inhibit infection or modulate cell migration. Here, we characterized the cleavage of EWI-2 leading to the production of EWI-2wint, which has been shown to inhibit HCV infection. We determined the regions of EWI-2/EWI-2wint and CD81 that are important for their interaction and their functionality. More precisely, we identified a glycine zipper motif in the transmembrane domain of EWI-2/EWI-2wint that is essential for the interaction with CD81. In addition, we found that palmitoylation on two juxtamembranous cysteines in the cytosolic tail of EWI-2/EWI-2wint is required for their interaction with CD81 as well as with CD9, another tetraspanin. Thus, we have shown that palmitoylation of a tetraspanin partner protein can influence the interaction with a tetraspanin. We therefore propose that palmitoylation not only of tetraspanins, but also of their partner proteins is important in regulating the composition of complexes in tetraspanin networks. Finally, we identified the regions in CD81 that are necessary for its functionality in HCV entry and we demonstrated that EWI-2wint needs to interact with CD81 to exert its inhibitory effect on HCV infection.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1083-351X
pubmed:author
pubmed:issnType
Electronic
pubmed:day
22
pubmed:volume
286
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13954-65
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:21343309-Amino Acid Motifs, pubmed-meshheading:21343309-Animals, pubmed-meshheading:21343309-Antigens, CD, pubmed-meshheading:21343309-Antigens, CD81, pubmed-meshheading:21343309-Antigens, CD9, pubmed-meshheading:21343309-Biotinylation, pubmed-meshheading:21343309-CHO Cells, pubmed-meshheading:21343309-Cell Membrane, pubmed-meshheading:21343309-Cricetinae, pubmed-meshheading:21343309-Cricetulus, pubmed-meshheading:21343309-Cytosol, pubmed-meshheading:21343309-Glycine, pubmed-meshheading:21343309-Hepacivirus, pubmed-meshheading:21343309-Hepatitis C, pubmed-meshheading:21343309-Humans, pubmed-meshheading:21343309-Membrane Glycoproteins, pubmed-meshheading:21343309-Membrane Proteins, pubmed-meshheading:21343309-Protein Binding, pubmed-meshheading:21343309-Protein Structure, Tertiary, pubmed-meshheading:21343309-Tetraspanins
pubmed:year
2011
pubmed:articleTitle
Interacting regions of CD81 and two of its partners, EWI-2 and EWI-2wint, and their effect on hepatitis C virus infection.
pubmed:affiliation
Center for Infection and Immunity of Lille, Hepatitis C Laboratory, University Lille Nord de France, CNRS UMR8204, INSERM U1019, Pasteur Institute of Lille, 59021 Lille, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't