期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 112, 期 29, 页码 E3901-E3910出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1506846112
关键词
herpes simplex virus; glycoprotein; gH; gL; virus entry
资金
- ERC (European Research Council) [340060]
- Italian Association for Cancer Research (AIRC) [IG14535]
- Department of Experimental, Diagnostic and Specialty Medicine, University of Bologna
- Italian Ministry for Education, University and Research (Progetti di Ricerca di Interesse Nazionale)
- University of Bologna Ricerca Fondamentale Orientata (RFO)
Herpes simplex virus (HSV) is an important human pathogen. It enters cells through an orchestrated process that requires four essential glycoproteins, gD, gH/gL, and gB, activated in cascade fashion by receptor-binding and signaling. gH/gL heterodimer is conserved across the Herpesviridae family. HSV entry is enabled by gH/gL interaction with alpha v beta 6- or alpha v beta 8-integrin receptors. We report that the interaction of virion gH/gL with integrins resulted in gL dissociation and its release in the medium. gL dissociation occurred if all components of the entry apparatus-receptor-bound gD and gB-were present and was prevented if entry was blocked by a neutralizing monoclonal antibody to gH or by a mutation in gH. We propose that (i) gL dissociation from gH/gL is part of the activation of HSV glycoproteins, critical for HSV entry; and (ii) gL is a functional inhibitor of gH and maintains gH in an inhibited form until receptor-bound gD and integrins signal to gH/gL.
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