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  • whocc
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  • Associate Professor
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  • Department Manager
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  • Pharmacist
  • PhD Student
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  • Post-doc
  • Project Manager
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  • 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
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© Research
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in PLoS biology - 09 Sep 2021

Light TP, Brun D, Guardado-Calvo P, Pederzoli R, Haouz A, Neipel F, Rey FA, Hristova K, Backovic M,

Link to Pubmed [PMID] – 34499637

Link to DOI – 10.1371/journal.pbio.3001392

PLoS Biol 2021 Sep; 19(9): e3001392

Human herpesvirus 8 (HHV-8) is an oncogenic virus that enters cells by fusion of the viral and endosomal cellular membranes in a process mediated by viral surface glycoproteins. One of the cellular receptors hijacked by HHV-8 to gain access to cells is the EphA2 tyrosine kinase receptor, and the mechanistic basis of EphA2-mediated viral entry remains unclear. Using X-ray structure analysis, targeted mutagenesis, and binding studies, we here show that the HHV-8 envelope glycoprotein complex H and L (gH/gL) binds with subnanomolar affinity to EphA2 via molecular mimicry of the receptor’s cellular ligands, ephrins (Eph family receptor interacting proteins), revealing a pivotal role for the conserved gH residue E52 and the amino-terminal peptide of gL. Using FSI-FRET and cell contraction assays, we further demonstrate that the gH/gL complex also functionally mimics ephrin ligand by inducing EphA2 receptor association via its dimerization interface, thus triggering receptor signaling for cytoskeleton remodeling. These results now provide novel insight into the entry mechanism of HHV-8, opening avenues for the search of therapeutic agents that could interfere with HHV-8-related diseases.

https://pubmed.ncbi.nlm.nih.gov/34499637