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Structural Disorder and Molecular Recognition

Head Sonia LONGHI

Latest Publications

  1. Identification of a Region in the Common Amino-terminal Domain of Hendra Virus P, V, and W Proteins Responsible for Phase Transition and Amyloid Formation (2021) Salladini E, Gondelaud F, Nilsson JF, Pesce G, Bignon C, Murrali MG, Fabre R, Pierattelli R, Kajava AV, Horvat B, Gerlier D, Mathieu C, Longhi S. Biomolecules 11(9) 1324 PMID:34572537
  2. Insights into the evolutionary forces that shape the codon usage in the viral genome segments encoding intrinsically disordered protein regions. (2021) Kumar N, Kaushik R, Tennakoon C, Uversky VN, Longhi S, Zhang KYJ, Bhatia S. Brief Bioinform in press PMID:33866372
  3. Comprehensive Intrinsic Disorder Analysis of 6108 Viral Proteomes: From the Extent of Intrinsic Disorder Penetrance to Functional Annotation of Disordered Viral Proteins (2021) Kumar N, Kaushik R, Tennakoon C, Uversky VN, Longhi S, Zhang KYJ, Bhatia S. J Prot Res 20 2704-2713 PMID:33719450
  4. Structural and Functional Characterization of the ABA-Water Deficit Stress Domain from Wheat and Barley: An Intrinsically Disordered Domain behind the Versatile Functions of the Plant Abscissic Acid, Stress and Ripening Protein Family (2021) Yacoubi I, Hamdi K, Fourquet P, Bignon C, Longhi S. Int J Mol Sci 22 2314 PMID:33652546
  5. Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy. (2021) Kodera N, Noshiro D, Dora SK, Mori T, Habchi J, Blocquel D, Gruet A, Dosnon M, Salladini E, Bignon C, Fujioka Y, Oda T, Noda NN, Sato M, Lotti M, Mizuguchi M, Longhi S, Ando T. Nat Nanotechnol 16 181-189 PMID:33230318
  6. Liquid-Liquid Phase Separation by Intrinsically Disordered Protein Regions of Viruses: Roles in Viral Life Cycle and Control of Virus Host Interactions (2020) Brocca S, Grandori R, Longhi S, Uversky V. Int J Mol Sci 21 9045 PMID:33260713
...All publications

The group focuses on the identification, characterization and elucidation of the functional role of disordered regions within proteins relevant in terms of human health. In particular, we are interested in proteins of the replicative complex of human pathogenic viruses, such as the measles virus and the recently emerged Nipah and Hendra viruses.

During the last fifteen years, the so-called structure-function paradigm was challenged by the discovery of intrinsically disordered proteins (IDPs), i.e. proteins that lack stable secondary and tertiary structure under physiological conditions of pH and salinity in the absence of a partner or ligand. Nevertheless, they are functional and are extremely abundant in living world. The group played a pioneering role in discovering that the nucleoprotein (N) and phosphoprotein (P) of measles virus posses long disordered regions (up to 250 residues), and subsequently extended these results to the N and P proteins from the Nipah and Hendra viruses, two recently emerged BSL4 pathogens. This discovery opens numerous interesting perspectives from a fundamental point of view but also in terms of potential therapeutic applications. The originality and main strength of the researches carried out by the group resides in the multidisciplinarity through the integration of bioinformatics, biochemistry, biophysics and structural biology.

The research activities of the team embrace four major axes:

  • The identification of disordered regions and the elucidation of the functional role of structural disorder within the replicative machinery of paramyxoviruses and its relevance in virus-host cell interactions.
  • The unraveling of the molecular mechanisms of folding coupled to binding events.
  • The elucidation of the molecular mechanisms and the functional impact of phase separations or transitions and of fibrillation by viral proteins.

Christophe BIGNON
Giulia PESCE

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