A role for caveolin 1 in assembly and budding of the paramyxovirus parainfluenza virus 5.

Journal of Virology
Dana RavidRobert A Lamb

Abstract

Caveolin 1 (Cav-1) is an integral membrane protein that forms the coat structure of plasma membrane caveolae and regulates caveola-dependent functions. Caveolae are enriched in cholesterol and sphingolipids and are related to lipid rafts. Many studies implicate rafts as sites of assembly and budding of enveloped virus. We show that Cav-1 colocalizes with the paramyxovirus parainfluenza virus 5 (PIV-5) nucleocapsid (NP), matrix (M), and hemagglutinin-neuraminidase (HN) proteins. Moreover, electron microscopy shows that Cav-1 is clustered at sites of viral budding. HN, M, and F(1)/F(2) are associated with detergent-resistant membranes, and these proteins float on sucrose gradients with Cav-1-rich fractions. A complex containing Cav-1 with M, NP, and HN from virus-infected cells and a complex containing Cav-1 and M from M-transfected cells were found on coimmunoprecipitation. A role of Cav-1 in the PIV-5 life cycle was investigated by utilizing MCF-7 human breast cancer cells that stably express Cav-1 (MCF-7/Cav-1). PIV-5 entry into MCF-7 and MCF-7/Cav-1 was found to be Cav-1 independent. However, the interaction between HN and M proteins was dramatically reduced in the Cav-1 null MCF-7 cells, and PIV-5 grown in MCF-7 cells had a ...Continue Reading

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Citations

Jan 20, 2012·Journal of Virology·Megan S HarrisonAnthony P Schmitt
Oct 9, 2012·Journal of Cellular Physiology·Sven SaldanhaAnja Nohe
Sep 25, 2017·Nature Communications·Daryll VanoverPhilip J Santangelo
Jan 1, 2011·Frontiers in Biology·Saijun MoZongbin Cui
Feb 6, 2017·Journal of Cell Science·Alexander LudwigRichard J Sugrue
Nov 17, 2020·Frontiers in Cell and Developmental Biology·Maria DudãuMihail E Hinescu

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