Rab6 Dependent Post-Golgi Trafficking of HSV1 Envelope Proteins to Sites of Virus Envelopment

Overview

Journal Traffic

Publisher Wiley

Specialties Biology
Physiology

Date 2013 Oct 25

PMID 24152084

Citations 37

Authors

Helen L Johns

Claudia Gonzalez-Lopez

Charlotte L Sayers

Michael Hollinshead

Gillian Elliott

Affiliations

Soon will be listed here.

Abstract

Herpes simplex virus 1 (HSV1) is an enveloped virus that uses undefined transport carriers for trafficking of its glycoproteins to envelopment sites. Screening of an siRNA library against 60 Rab GTPases revealed Rab6 as the principal Rab involved in HSV1 infection, with its depletion preventing Golgi-to-plasma membrane transport of HSV1 glycoproteins in a pathway used by several integral membrane proteins but not the luminal secreted protein Gaussia luciferase. Knockdown of Rab6 reduced virus yield to 1% and inhibited capsid envelopment, revealing glycoprotein exocytosis as a prerequisite for morphogenesis. Rab6-dependent virus production did not require the effectors myosin-II, bicaudal-D, dynactin-1 or rabkinesin-6, but was facilitated by ERC1, a factor involved in linking microtubules to the cell cortex. Tubulation and exocytosis of Rab6-positive, glycoprotein-containing membranes from the Golgi was substantially augmented by infection, resulting in enhanced and targeted delivery to cell tips. This reveals HSV1 morphogenesis as one of the first biological processes shown to be dependent on the exocytic activity of Rab6.

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