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  • team
  • department
  • center
  • program_project
  • nrc
  • whocc
  • project
  • software
  • tool
  • patent
  • Administrative Staff
  • Assistant Professor
  • Associate Professor
  • Clinical Research Assistant
  • Clinical Research Nurse
  • Clinician Researcher
  • Department Manager
  • Dual-education Student
  • Full Professor
  • Honorary Professor
  • Lab assistant
  • Master Student
  • Non-permanent Researcher
  • Nursing Staff
  • Permanent Researcher
  • Pharmacist
  • PhD Student
  • Physician
  • Post-doc
  • Prize
  • Project Manager
  • Research Associate
  • Research Engineer
  • Retired scientist
  • Technician
  • Undergraduate Student
  • Veterinary
  • Visiting Scientist
  • Deputy Director of Center
  • Deputy Director of Department
  • Deputy Director of National Reference Center
  • Deputy Head of Facility
  • Director of Center
  • Director of Department
  • Director of Institute
  • Director of National Reference Center
  • Group Leader
  • Head of Facility
  • Head of Operations
  • Head of Structure
  • Honorary President of the Departement
  • Labex Coordinator
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Scientific Fields
Diseases
Organisms
Applications
Technique
Starting Date
04
Jul 2015
Status
Ongoing
Members
3
Structures
2

About

Envelope glycoproteins of herpesviruses

    Herpesviridae are a large family of double-stranded DNA viruses, counting more than 200 members that infect humans and a wide range of invertebrates and vertebrates. Herpesviruses carry a large linear DNA genome of 100 – 200 Kb, which is packed in an icosahedral capsid. The nucleocapsid is immersed in a protein rich matrix called tegument, which is enveloped by a lipid bilayer decorated with a dozen of surface glycoproteins involved in virus attachment and entry.

Herpesviruses enter cells by fusion of the viral and plasma membranes. Membrane fusion is triggered by binding of a viral envelope protein to a specific cellular receptor, and is catalyzed by a three-part fusion machinery composed of the envelope glycoproteins B (gB) and hetero-dimeric non-covalent complex made of glycoproteins H and L (gH/gL). The fusion apparatus of herpesviruses (gB-gH/gL) is conserved.

We are interested in understanding the molecular mechanism of herpesvirus entry -how does the binding to a receptor activate the fusion machinery, and how does a complex of gB and gH/gL mediate the merger of lipid bilayers. We are using a combination of biochemical, biophysical and structural biology methods to address these questions. One of the main goals is to determine three dimensional structures of the proteins involved in the entry process by X-ray crystallography. We are currently expressing a range of recombinant proteins from alpha-herpesviruses Herpes simplex virus 1, human herpesvirus 8, also known as Kaposi Sarcoma Associated Herpesvirus, and others.

HHV-8 gH/gL (grey and blue) bound to cellular receptor (purple)
Crystal structure of human herpesvirus 8 glycoproteins H and L bound to EphA2 cellular receptor

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