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© Institut Pasteur
Structure de macromolécules : dimère d'aquométhémoglobine de cheval. Dérivé toxique oxydé de l'hémoglobine, représentant 1 à 2% du total.
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Science signaling - 19 Jan 2010

Préhaud C, Wolff N, Terrien E, Lafage M, Mégret F, Babault N, Cordier F, Tan GS, Maitrepierre E, Ménager P, Chopy D, Hoos S, England P, Delepierre M, Schnell MJ, Buc H, Lafon M

Link to Pubmed [PMID] – 20086240

Sci Signal 2010 Jan;3(105):ra5

The capacity of a rabies virus to promote neuronal survival (a signature of virulence) or death (a marker of attenuation) depends on the cellular partners recruited by the PDZ-binding site (PDZ-BS) of its envelope glycoprotein (G). Neuronal survival requires the selective association of the PDZ-BS of G with the PDZ domains of two closely related serine-threonine kinases, MAST1 and MAST2. Here, we found that a single amino acid change in the PDZ-BS triggered the apoptotic death of infected neurons and enabled G to interact with additional PDZ partners, in particular the tyrosine phosphatase PTPN4. Knockdown of PTPN4 abrogated virus-mediated apoptosis. Thus, we propose that attenuation of rabies virus requires expansion of the set of host PDZ proteins with which G interacts, which interferes with the finely tuned homeostasis required for survival of the infected neuron.

https://www.ncbi.nlm.nih.gov/pubmed/20086240