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Sphingomyelin-Sequestered Cholesterol Domain Recruits Formin-Binding Protein 17 for Constricting Clathrin-Coated Pits in Influenza Virus Entry

Bo Tang, En-Ze Sun, Zhi-Ling Zhang, Shu-Lin Liu, Jia Liu, Akihiro Kusumi, Zhi-Hong Hu, Tao Zeng, Ya-Feng Kang, Hong-Wu Tang, Dai-Wen Pang

2022Journal of Virology16 citationsDOIOpen Access PDF

Abstract

IAV infects cells by harnessing cellular endocytic machineries. A better understanding of the cellular machineries used for its entry might lead to the development of antiviral strategies and would also provide important insights into physiological endocytic processes. This work demonstrated that a special pool of cholesterol in the plasma membrane, SM-sequestered cholesterol, recruits FBP17 for the constriction of clathrin-coated pits in IAV entry. Meanwhile, the clathrin-independent cell entry of IAV is cholesterol independent. The internalization of transferrin, the gold-standard cargo endocytosed solely via CME, is much less dependent on the SM-cholesterol complex. These results provide new insights into IAV infection and the pathway/cargo-specific involvement of the cholesterol pool(s).

Topics & Concepts

EndocytosisEndocytic cycleBiologyCell biologyInternalizationCaveolaeInfluenza A virusActinViral entryVirologyVirusCell membraneCholesterolPinocytosisCiliumTranscytosisReceptor-mediated endocytosisEndosomeLipid raftTransferrinMembrane proteinLipid Membrane Structure and BehaviorCellular transport and secretionBiochemical and Structural Characterization
Sphingomyelin-Sequestered Cholesterol Domain Recruits Formin-Binding Protein 17 for Constricting Clathrin-Coated Pits in Influenza Virus Entry | Litcius