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@ARTICLE{Lalibert:282595,
author = {Laliberté, Alexandre and Prelli Bozzo, Caterina and
Acharya, Dhiraj and De Luna, Aurora and Hirschenberger,
Maximilian and Zhu, Junji and Volcic, Meta and Stolp,
Bettina and Rodriguez-Quinteros, Cristina M and Fackler,
Oliver T and Gack, Michaela U and Sparrer, Konstantin M J
and Kirchhoff, Frank},
title = {{N}ef stabilizes actin to prevent {HIV}-1 sensing by
{RIG}-{I}-like receptors.},
journal = {Nature Communications},
volume = {16},
number = {1},
issn = {2041-1723},
address = {[London]},
publisher = {Springer Nature},
reportid = {DZNE-2025-01353},
pages = {10945},
year = {2025},
abstract = {Sensing of viral pathogens by RIG-I-like receptors (RLRs)
requires their priming via dephosphorylation mediated by the
protein phosphatase 1 regulatory subunit 12 C (R12C), which
is activated upon virus-induced actin rearrangements. Here,
we show that the HIV-1 accessory protein Nef prevents
R12C-mediated RLR priming, thereby suppressing viral
sensing. HIV-1 variants containing single point mutations in
Nef (F/R191A) that ablate its ability to bind the
actin-modulating kinase PAK2 trigger increased interferon
(IFN) responses in primary CD4+ T cells, macrophages, and
dendritic cells. Neutralization of IFN suppresses innate
immune activation and enhances the replication of
Nef-mutated HIV-1. We further demonstrate that HIV-1
encoding Nef F/R191A is sensed by MDA5 after proviral
integration in an R12C-dependent manner. Mechanistically,
PAK2 binding by Nef promotes actin repair and stabilization,
thereby preventing re-localization of R12C to MDA5 and RIG-I
and their subsequent dephosphorylation. Our data identify
Nef as an antagonist of actin-R12C-mediated RLR priming,
enabling HIV-1 to escape immune control.},
keywords = {Humans / HIV-1: immunology / HIV-1: genetics / nef Gene
Products, Human Immunodeficiency Virus: metabolism / nef
Gene Products, Human Immunodeficiency Virus: genetics / nef
Gene Products, Human Immunodeficiency Virus: immunology /
Actins: metabolism / Receptors, Immunologic / DEAD Box
Protein 58: metabolism / HIV Infections: immunology / HIV
Infections: virology / HIV Infections: metabolism /
p21-Activated Kinases: metabolism / Interferon-Induced
Helicase, IFIH1: metabolism / CD4-Positive T-Lymphocytes:
immunology / CD4-Positive T-Lymphocytes: virology / HEK293
Cells / Immunity, Innate / Dendritic Cells: immunology /
Phosphorylation / Macrophages: immunology / Macrophages:
virology / Protein Phosphatase 1: metabolism / Interferons:
metabolism / Interferons: immunology / Virus Replication /
nef Gene Products, Human Immunodeficiency Virus (NLM
Chemicals) / Actins (NLM Chemicals) / Receptors, Immunologic
(NLM Chemicals) / DEAD Box Protein 58 (NLM Chemicals) / nef
protein, Human immunodeficiency virus 1 (NLM Chemicals) /
p21-Activated Kinases (NLM Chemicals) / RIGI protein, human
(NLM Chemicals) / Interferon-Induced Helicase, IFIH1 (NLM
Chemicals) / PAK2 protein, human (NLM Chemicals) / IFIH1
protein, human (NLM Chemicals) / Protein Phosphatase 1 (NLM
Chemicals) / Interferons (NLM Chemicals)},
cin = {AG Sparrer},
ddc = {500},
cid = {I:(DE-2719)1910003},
pnm = {351 - Brain Function (POF4-351)},
pid = {G:(DE-HGF)POF4-351},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:41354661},
doi = {10.1038/s41467-025-67028-5},
url = {https://pub.dzne.de/record/282595},
}