Modulation of CD4 lateral interaction with lymphocyte surface molecules induced by HIV-1 gp120

European Journal of Immunology
U DianzaniA Pileri

Abstract

CD4, a lymphocyte surface glycoprotein, serves as co-receptor for antigen with the T cell receptor (TCR). It is also the lymphocyte receptor for HIV by binding the gp120 viral envelope protein. Interaction of gp120 with CD4 is crucial for viral infection, but is not sufficient to allow viral entry into cells. Recombinant gp120 alters CD4+ T cell responsiveness to activation stimuli. To express its co-receptor function fully, CD4 must be laterally associated with the TCR and CD45 to form multi-receptor complexes competent to transduce potent activation signals. Here, we examine the possibility that gp120/CD4 binding alters lateral associations of CD4 with other lymphocyte surface molecules, and that assembly of abnormal multi-molecular complexes is involved in the gp120-induced CD4+ T cell dysfunction and in viral entry. In the absence of gp120, CD4 displayed high association with CD3, CD5, CD45RC, CD25, CD28, CD44, and CD53; weak association with CD2, CD38, CD45RB, CD62L, and CD26; and no association with CD45RA, CD45RO, CD11b, CD11a, CD54, CD7, CD48, CD98, CD59 CD55, HLA class I and class II molecules. Treatment with gp120 significantly increased CD4 association with CD3, CD45RA, CD45RB, CD59, CD38, CD26 and HLA class I, and d...Continue Reading

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Citations

Aug 4, 1999·Immunology Today·I De MeesterS Scharpé
Apr 27, 2012·Molecular Biology of the Cell·Mónica Gordón-AlonsoFrancisco Sánchez-Madrid
Dec 28, 2002·Journal of Virology·Angélique B van 't WoutJames I Mullins
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Jun 3, 2016·Scientific Reports·Ting LiYong Juan Zhao
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Aug 9, 2013·The Journal of Biological Chemistry·Mónica Gordón-AlonsoFrancisco Sánchez-Madrid
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Oct 4, 2006·The Journal of Immunology : Official Journal of the American Association of Immunologists·Mónica Gordón-AlonsoFrancisco Sánchez-Madrid
Jan 23, 2020·Cells·Estibaliz Glaría, Annabel F Valledor

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