International Immunology, Vol 9, 53-64, Copyright © 1997 by Oxford University Press
T Morio, T Chatila and RS Geha
HIV major glycoprotein gp120 interacts with CD4 molecules and perturbs
signaling through the TCR-CD3 complex. We examined the effects of gp120 on
TCR-CD3-induced phosphorylation and activation of the src-type protein
tyrosine kinases (PTK), fyn and lck. gp120 caused minimal changes in lck
phosphorylation or lck enzymatic activity, but preincubation of Jurkat
cells with gp120 for 20 min strongly inhibited TCR-CD3-mediated
phosphorylation and activation of lck and fyn, as well as phosphorylation
of CD3 zeta. Inhibition of TCR-CD3 signaling in T cells preincubated with
gp120 was paralleled by inhibition of T cell proliferation to the antigen
tetanus toxoid. Neither surface CD4 expression nor CD4-lck association was
affected by gp120. Furthermore, gp120 inhibited lck phosphorylation induced
by cross-linking of TCR-CD3 and CD4 suggesting that the inhibition of lck
phosphorylation could not be simply accounted for by sequestration of CD4
molecules. gp120 selectively enhanced the phosphorylation of the lck
peptide containing the autoinhibitory tyrosine residue Tyr505 relative to
the lck peptide containing the positive regulatory residue Tyr394,
suggesting that a qualitative alteration in lck may underlie the inhibition
of TCR-CD3 signaling by gp120.
ARTICLES
HIV glycoprotein gp120 inhibits TCR-CD3-mediated activation of fyn and lck
Division of Immunology, Children's Hospital, Boston, MA 02115, USA.
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