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Regulatory Mechanisms of the Mucin-Like Region on Herpes Simplex Virus during Cellular Attachment
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2019 (English)In: ACS Chemical Biology, ISSN 1554-8929, E-ISSN 1554-8937, Vol. 14, no 3, p. 534-542Article in journal (Refereed) Published
Abstract [en]

Mucin-like regions, characterized by a local high density of O-linked glycosylation, are found on the viral envelope glycoproteins of many viruses. Herpes simplex virus type 1 (HSV-1), for example, exhibits a mucin-like region on its glycoprotein gC, a viral protein involved in initial recruitment of the virus to the cell surface via interaction with sulfated glycosaminoglycans. So far, this mucin-like region has been proposed to play a key role in modulating the interactions with cellular glycosaminoglycans, and in particular to promote release of HSV-1 virions from infected cells. However, the molecular mechanisms and the role as a pathogenicity factor remains unclear. Using single virus particle tracking, we show that the mobility of chondroitin sulfate-bound HSV-1 virions is decreased in absence of the mucin-like region. This decrease in mobility correlates with an increase in HSV-1-chondroitin sulfate binding forces as observed using atomic force microscopy-based force spectroscopy. Our data suggest that the mucin-like region modulates virus-glycosaminoglycan interactions by regulating the affinity, type, and number of glycoproteins involved in the virus glycosaminoglycan interaction. This study therefore presents new evidence for a role of the mucin-like region in balancing the interaction of HSV-1 with glycosaminoglycans and provides further insights into the molecular mechanisms used by the virus to ensure both successful cell entry and release from the infected cell.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2019. Vol. 14, no 3, p. 534-542
National Category
Cell and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-157964DOI: 10.1021/acschembio.9b00064ISI: 000461844100026PubMedID: 30735356OAI: oai:DiVA.org:umu-157964DiVA, id: diva2:1305288
Available from: 2019-04-16 Created: 2019-04-16 Last updated: 2019-04-16Bibliographically approved

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Bally, Marta

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Department of Clinical MicrobiologyWallenberg Centre for Molecular Medicine at Umeå University (WCMM)
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