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Hiv-1 Envelope Overcomes Nlrp3-Mediated Inhibition Of F-Actin Polymerization For Viral Entry, Audrey Paoletti, Awatef Allouch, Marina Caillet, Hela Saïdi, Frédéric Subra, Roberta Nardacci, Qiuji Wu, Zeinaf Muradova, Laurent Voisin, Syed Qasim Raza, Frédéric Law, Maxime Thoreau, Haithem Dakhli, Olivier Delelis, Béatrice Poirier-Beaudouin, Nathalie Dereuddre-Bosquet, Roger Le Grand, Olivier Lambotte, Asier Saez-Cirion, Gianfranco Pancino, David M. Ojcius, Eric Solary, Eric Deutsch, Mauro Piacentini, Marie Lise Gougeon, Guido Kroemer, Jean Luc Perfettini
Hiv-1 Envelope Overcomes Nlrp3-Mediated Inhibition Of F-Actin Polymerization For Viral Entry, Audrey Paoletti, Awatef Allouch, Marina Caillet, Hela Saïdi, Frédéric Subra, Roberta Nardacci, Qiuji Wu, Zeinaf Muradova, Laurent Voisin, Syed Qasim Raza, Frédéric Law, Maxime Thoreau, Haithem Dakhli, Olivier Delelis, Béatrice Poirier-Beaudouin, Nathalie Dereuddre-Bosquet, Roger Le Grand, Olivier Lambotte, Asier Saez-Cirion, Gianfranco Pancino, David M. Ojcius, Eric Solary, Eric Deutsch, Mauro Piacentini, Marie Lise Gougeon, Guido Kroemer, Jean Luc Perfettini
All Dugoni School of Dentistry Faculty Articles
© 2019 The Author(s) Purinergic receptors and nucleotide-binding domain leucine-rich repeat containing (NLR) proteins have been shown to control viral infection. Here, we show that the NLR family member NLRP3 and the purinergic receptor P2Y2 constitutively interact and regulate susceptibility to HIV-1 infection. We found that NLRP3 acts as an inhibitory factor of viral entry that represses F-actin remodeling. The binding of the HIV-1 envelope to its host cell receptors (CD4, CXCR4, and/or CCR5) overcomes this restriction by stimulating P2Y2. Once activated, P2Y2 enhances its interaction with NLRP3 and stimulates the recruitment of the E3 ubiquitin ligase CBL to NLRP3, …