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J Gen Virol. 2016 Nov;97(11):3007-3016. doi: 10.1099/jgv.0.000616. Epub 2016 Sep 27.

Herpes simplex virus particles interact with chemokines and enhance cell migration.

Author information

1
1​Centro de Biología Molecular Severo Ochoa, Consejo Superior de Investigaciones Científicas - Universidad Autónoma de Madrid, Madrid, Spain.

Abstract

Herpes simplex virus type 1 and type 2 (HSV-1 and HSV-2, respectively) are among the most prevalent human pathogens, causing a variety of diseases. HSV modulation of the chemokine network remains poorly understood. We have previously identified secreted glycoprotein G (SgG) as the first viral chemokine-binding protein that enhances chemokine function as a novel viral immunomodulatory mechanism. However, gG is also present at the viral envelope and its role in the virus particle remains unknown. Here we have addressed the chemokine-binding capacity of HSV particles and the functionality of such interaction in vitro. We adapted surface plasmon resonance assays and demonstrated the ability of HSV particles to bind a specific set of human chemokines with high affinity. Moreover, we identified gG as the envelope glycoprotein mediating such interaction, as shown by the lack of binding to a HSV-1 gG mutant. In contrast to HSV-1, HSV-2 gG is cleaved and the chemokine-binding domain is secreted (SgG2). However, we found that HSV-2 particles retain the ability to bind chemokines, potentially through SgG2 associated to the viral envelope or non-processed precursor protein. Moreover, we found that HSV particles increase cell migration independently of chemokine binding to envelope gG. This work provides insights into HSV manipulation of the host immune system.

PMID:
27692045
DOI:
10.1099/jgv.0.000616
[Indexed for MEDLINE]

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