Journal
EMBO JOURNAL
Volume 31, Issue 21, Pages 4204-4220Publisher
WILEY
DOI: 10.1038/emboj.2012.262
Keywords
endocytosis; HSV1; Rab11; Rab5; trans-Golgi network
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Funding
- Medical Research Council
- MRC [G1000207, G0601605] Funding Source: UKRI
- Medical Research Council [G0601605, G1000207] Funding Source: researchfish
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Enveloped viruses employ diverse and complex strategies for wrapping at cellular membranes, many of which are poorly understood. Here, an ultrastructural study of herpes simplex virus 1 (HSV1)-infected cells revealed envelopment in tubular membranes. These tubules were labelled by the fluid phase marker horseradish peroxidase (HRP), and were observed to wrap capsids as early as 2 min after HRP addition, indicating that the envelope had recently cycled from the cell surface. Consistent with this, capsids did not colocalise with either the trans-Golgi network marker TGN46 or late endosomal markers, but showed coincidence with the transferrin receptor. Virus glycoproteins were retrieved from the plasma membrane (PM) to label wrapping capsids, a process that was dependent on both dynamin and Rab5. Combined depletion of Rab5 and Rab11 reduced virus yield to <1%, resulting in aberrant localisation of capsids. These results suggest that endocytosis from the PM into endocytic tubules provides the main source of membrane for HSV1, and reveal a new mechanism for virus exploitation of the endocytic pathway. The EMBO Journal (2012) 31, 4204-4220. doi: 10.1038/emboj.2012.262; Published online 18 September 2012
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