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*
Laboratory of Immunology, National Institute for Cancer Research, Genoa, Italy;
Laboratory of Tumor Immunology and
Department of Pathology, Scientific Institute San Raffaele, Milan, Italy;
Laboratory of Clinical Immunology, Division of Infectious Diseases, Centro San Luigi, Milan, Italy; and
¶ Unit of Protein Biology, National Institute for Cancer Research, Genoa, Italy
In this study, we show that binding to autologous dendritic cells
(DC) induces a calcium influx in NK cells, followed by activation of
the calcium-calmodulin kinase II (CAMKII), release of perforin and
granzymes, and IFN-
secretion. CAMKII is induced via LFA-1: indeed,
oligomerization of LFA-1 leads to CAMKII induction in NK cells.
Moreover, release of lytic enzymes and cytotoxic activity is strongly
reduced by masking LFA-1 or by adding CAMKII inhibitors such as KN62
and KN93, at variance with the inactive compound KN92. NK cell-mediated
lysis of DC and IFN- release by NK cells upon NK/DC contact are
inhibited by exogenous HIV-1 Tat: the protein blocks calcium influx and
impairs CAMKII activation elicited via LFA-1 in NK cells, eventually
inhibiting degranulation. Experiments performed with synthetic,
overlapping Tat-derived peptides showed that the C-terminal domain of
the protein is responsible for inhibition. Finally, both KN62 and Tat
reduced the extension of NK/DC contacts, possibly affecting NK cell
granule polarization toward the target. These data provide evidence
that exogenous Tat inhibits NK cell activation occurring upon contact
with DC: this mechanism might contribute to the impairment of natural
immunity in HIV-1 infection.
This article has been cited by other articles:
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