PuSH - Publikationsserver des Helmholtz Zentrums München

Export: TXT Text RIS Endnote (RIS) BIB BibTeX
Dehn, S.* ; Burkhard, R.* ; Leyens, J.* ; Kaiser, T.* ; Brandimarte, S.* ; Heiligensetzer, D.* ; Koppensteiner, H. ; Bajoghli, B.* ; Hailfinger, S.* ; Schilbach, K.* ; Schindler, M.

HIV-1 manipulates CD96 on CD4+ T cells to subvert antiviral immunity.

Sci. Adv. 11:eadx7485 (2025)
Verlagsversion Forschungsdaten DOI PMC
Open Access Gold
Creative Commons Lizenzvertrag
HIV-1 evades immune responses by modulating plasma membrane receptors. Using a flow cytometry-based screening, we profiled 332 surface receptors on HIV-1-infected primary CD4+ T cells and identified 23 down-regulated receptors, including known targets such as CD4, MHCI, CCR7, and CD62L. CD96, an inhibitory natural killer (NK) cell receptor poorly studied in human CD4+ T cells, was markedly down-regulated. This modulation, mediated by the viral proteins Nef and Vpu, surpassed that of other NK-associated receptors such as CD155 and NTB-A and is conserved across lentiviruses. CD96Hi CD4+ T cells exhibited a proinflammatory TH1/TH17 phenotype characterized by IFN-γ and IL-17 secretion and displayed impaired migration in vivo. Furthermore, CD96 ligation enhanced IFN-γ release upon viral peptide stimulation and promoted the secretion of TH1/TH17-associated cytokines. Our findings suggest that CD96 regulates antiviral immune responses and maintains proinflammatory properties in CD4+ T cells. Thus, its down-regulation represents a previously unknown HIV-1 immune evasion strategy, with implications for exploiting CD96 as immunotherapeutic target.
Impact Factor
Scopus SNIP
Altmetric
12.500
0.000
Tags
Anmerkungen
Besondere Publikation
Auf Hompepage verbergern

Zusatzinfos bearbeiten
Eigene Tags bearbeiten
Privat
Eigene Anmerkung bearbeiten
Privat
Auf Publikationslisten für
Homepage nicht anzeigen
Als besondere Publikation
markieren
Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Human-immunodeficiency-virus; Down-modulation; Type-1 Nef; Surface Expression; Vpu; Receptor; Protein; Activation; Adhesion; Tigit
Sprache englisch
Veröffentlichungsjahr 2025
HGF-Berichtsjahr 2025
ISSN (print) / ISBN 2375-2548
e-ISSN 2375-2548
Zeitschrift Science Advances
Quellenangaben Band: 11, Heft: 36, Seiten: , Artikelnummer: eadx7485 Supplement: ,
Verlag American Association for the Advancement of Science (AAAS)
Verlagsort Washington, DC [u.a.]
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Virology (VIRO)
POF Topic(s) 30203 - Molecular Targets and Therapies
Forschungsfeld(er) Immune Response and Infection
PSP-Element(e) G-502700-006
Förderungen Helmholtz Center Munich
University Hospital Tubingen
Deutsche Forschungsgemeinschaft
DOI 10.1126/sciadv.adx7485
WOS ID 001566911500024
Scopus ID 105015636468
PubMed ID 40911682
Erfassungsdatum 2025-10-17
[➜Korrektur melden]