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The Journal of Immunology, 2005, 174: 2235-2241.
Copyright © 2005 by The American Association of Immunologists

A Proinflammatory Peptide from Herpes Simplex Virus Type 2 Glycoprotein G Affects Neutrophil, Monocyte, and NK Cell Functions1

Lars Bellner*, Fredrik Thorén{dagger}, Erik Nygren{ddagger}, Jan-Åke Liljeqvist{dagger}, Anna Karlsson* and Kristina Eriksson2,*

Departments of * Rheumatology and Inflammation Research, {dagger} Clinical Virology, and {ddagger} Medical Microbiology and Immunology, Göteborg University, Göteborg, Sweden

We have identified a synthetic peptide derived from the secreted portion of HSV type 2 glycoprotein G, denoted gG-2p20, which has proinflammatory properties in vitro. The gG-2p20 peptide, corresponding to aa 190–205 of glycoprotein G-2, was a chemoattractant for both monocytes and neutrophils in a dose-dependent fashion, and also induced the release of reactive oxygen from these cells. The receptor mediating the responses was identified as the formyl peptide receptor. The gG-2p20-induced activation of phagocytes had a profound impact on NK cell functions. The reactive oxygen species produced by gG-2p20-activated phagocytes both inhibited NK cell cytotoxicity and accelerated the apoptotic cell death in NK cell-enriched lymphocyte populations. Hence, we have for the first time been able to identify a potential function of the secreted portion of HSV-2 glycoprotein G. We propose that the proinflammatory gG-2p20 peptide identified could contribute to a reduced function and viability of NK cells during HSV-2 infection due to its ability to recruit and activate phagocytic cells.




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