|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0019704,
umls-concept:C0678640,
umls-concept:C1332714,
umls-concept:C1514562,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1550548,
umls-concept:C1555714,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1705654,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
|
|
pubmed:issue |
8
|
|
pubmed:dateCreated |
2002-7-29
|
|
pubmed:abstractText |
CD4, a member of the immunoglobulin superfamily of receptors that mediates cell-cell interactions in the immune system, is the primary receptor for HIV-1. The extracellular portion of CD4 is a concatenation of four immunoglobulin-like domains, D1 to D4. The D1, D2 and D4 domains each contain a disulfide bond. We show here that the D2 disulfide bond is redox-active. The redox state of the thiols (disulfide versus dithiol) appeared to be regulated by thioredoxin, which is secreted by CD4(+) T cells. Locking the CD4 and the thioredoxin active-site dithiols in the reduced state with a hydrophilic trivalent arsenical blocked entry of HIV-1 into susceptible cells. These findings indicate that redox changes in CD4 D2 are important for HIV-1 entry and represent a new target for HIV-1 entry inhibitors.
|
|
pubmed:commentsCorrections |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3-(N-maleimidopropionyl)biocytin,
http://linkedlifedata.com/resource/pubmed/chemical/4-(N-(S-glutathionylacetyl)amino)phe...,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD4,
http://linkedlifedata.com/resource/pubmed/chemical/Arsenicals,
http://linkedlifedata.com/resource/pubmed/chemical/Biotin,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Maleimides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, HIV,
http://linkedlifedata.com/resource/pubmed/chemical/Succinimides,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfhydryl Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Thioredoxins,
http://linkedlifedata.com/resource/pubmed/chemical/biotinyl-N-hydroxysulfosuccinimide...
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Aug
|
|
pubmed:issn |
1529-2908
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
3
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
727-32
|
|
pubmed:dateRevised |
2007-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:12089508-Antigens, CD4,
pubmed-meshheading:12089508-Arsenicals,
pubmed-meshheading:12089508-Biotin,
pubmed-meshheading:12089508-CD4-Positive T-Lymphocytes,
pubmed-meshheading:12089508-Cysteine,
pubmed-meshheading:12089508-Glutathione,
pubmed-meshheading:12089508-HIV-1,
pubmed-meshheading:12089508-Humans,
pubmed-meshheading:12089508-Immunoblotting,
pubmed-meshheading:12089508-Lysine,
pubmed-meshheading:12089508-Maleimides,
pubmed-meshheading:12089508-Mutation,
pubmed-meshheading:12089508-Oxidation-Reduction,
pubmed-meshheading:12089508-Protein Structure, Tertiary,
pubmed-meshheading:12089508-Receptors, HIV,
pubmed-meshheading:12089508-Succinimides,
pubmed-meshheading:12089508-Sulfhydryl Compounds,
pubmed-meshheading:12089508-Thioredoxins
|
|
pubmed:year |
2002
|
|
pubmed:articleTitle |
Disulfide exchange in domain 2 of CD4 is required for entry of HIV-1.
|
|
pubmed:affiliation |
Centre for Thrombosis and Vascular Research, School of Medical Sciences, University of New South Wales and Department of Haematology, Prince of Wales Hospital, Sydney, NSW 2052, Australia.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
