Strategies to interfere with PDZ-mediated interactions in neurons: What we can learn from the rabies virus

Progress in Biophysics and Molecular Biology
Célia Caillet-SaguyNicolas Wolff

Abstract

PDZ (PSD-95/Dlg/ZO-1) domains play a major role in neuronal homeostasis in which they act as scaffold domains regulating cellular trafficking, self-association and catalytic activity of essential proteins such as kinases and phosphatases. Because of their central role in cell signaling, cellular PDZ-containing proteins are preferential targets of viruses to hijack cellular function to their advantage. Here, we describe how the viral G protein of the rabies virus specifically targets the PDZ domain of neuronal enzymes during viral infection. By disrupting the complexes formed by cellular enzymes and their ligands, the virus triggers drastic effect on cell signaling and commitment of the cell to either survival (virulent strains) or death (vaccinal strains). We provide structural and biological evidences that the viral proteins act as competitors endowed with specificity and affinity in an essential cellular process by mimicking PDZ binding motif of cellular partners. Disruption of critical endogenous protein-protein interactions by viral protein drastically alters intracellular protein trafficking and catalytic activity of cellular proteins that control cell homeostasis. This work opens up many perspectives to mimic viral sequen...Continue Reading

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Citations

Dec 1, 2017·Nature Reviews. Disease Primers·Anthony R FooksAshley C Banyard
Jan 3, 2018·Current Opinion in Infectious Diseases·Gabriella Ugolini, Thiravat Hemachudha
Jan 20, 2021·Cellular and Molecular Neurobiology·Soheil GhassemiMohammad Sayyah
Apr 1, 2021·Journal of Neurovirology·Soheil GhassemiMohammad Sayyah
Apr 18, 2021·The FEBS Journal·Célia Caillet-SaguyNicolas Wolff
Jun 22, 2021·Frontiers in Molecular Biosciences·Yannick G SpillMichael Nilges
Jul 5, 2021·Iranian Biomedical Journal·Fatemeh ZandiBehrouz Vaziri

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