Journal
VIRUS RESEARCH
Volume 190, Issue -, Pages 97-103Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.virusres.2014.07.003
Keywords
DC-SIGN; Human herpesvirus 8
Categories
Funding
- NIH [R01 CA 82053, U01 AI 35041]
- Univeristy of Pittsburgh Cancer Institute Cytometry Facility [P30CA047904]
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We have previously shown that human herpesvirus 8 (HHV-8) uses DC-SIGN as an entry receptor for dendritic cells, macrophages and B cells. The viral attachment protein for DC-SIGN is unknown. HHV-8 virions contain five conserved herpesvirus glycoproteins, a single unique glycoprotein, and two predicted glycoproteins. Previous studies have shown that DC-SIGN binds highly mannosylated glycoproteins. The HHV-8 glycoprotein B (gB) has been reported to be highly mannosylated, and therefore we hypothesized that gB will bind to DC-SIGN. In this report we confirm that gB has a high mannose carbohydrate structure and demonstrate for the first time that it binds DC-SIGN in a dose-dependent manner. We also identify key amino acids in the DC-SIGN carbohydrate recognition domain that are required for HHV-8 infection and compare these results with published binding regions for ICAM-2/3 and HIV-1 gp120. These results clarify some of the initial events in HHV-8 entry and can be used for the design of targeted preventive therapies. (C) 2014 Elsevier B.V. All rights reserved.
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