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Structural Disorder and Molecular Recognition

Head Sonia LONGHI

Latest Publications

  1. 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
  2. Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy. (2020) 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 in press PMID:33230318
  3. Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS (2020) Schiavina M, Salladini E, Murrali MG, Tria G, Felli I, Pierattelli R, Longhi S. Sci Rep 10 19574 PMID:33177626
  4. PED in 2021: a major update of the protein ensemble database for intrinsically disordered proteins (2020) Lazar T, Martinez-Perez E, Quaglia F, Hatos A, Chemes LB, Iserte JA, Mendez NA, Garrone NA, Saldano TE, Marchetti J, Velez Rueda AJ, Bernado P, Blackledge M, Cordeiro TN, Fagerberg E, Forman-Kay JD, Fornasari MS, Gibson TJ, Gomes GNW, Gradinaru CC, Head-Gordon T, Jensen M, Lemke EA, Longhi S, Marino-Buslje C, Minervini G, Mittag T, Monzon AM, Pappu RV, Parisi G, Ricard-Blum S, Ruff KM, Salladini E, Skepo M, Svergun D, Vallet SD, Varadi M, Tompa P, Tosatto SCE, Piovesan D. Nucleic Acids Res gkaa1021 PMID:33305318
  5. Predicting substitutions to modulate disorder and stability in coiled-coils (2020) Karami Y, Saighi P, Vanderhaegen R, Gerlier D, Longhi S, Laine E, Carbone A. BMC Bioinformatics 21(Suppl 19) 573 PMID:33349244
  6. Relevance of Electrostatic Charges in Compactness, Aggregation, and Phase Separation of Intrinsically Disordered Proteins (2020) Bianchi G, Longhi S, Grandori R, Brocca S. Int J Mol Sci 21 E6208 PMID:32867340
...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 understanding of the molecular bases of specificity and affinity in partner recognition by intrinsically disordered proteins (IDPs).
  • The discovery of compounds capable of blocking crucial interactions involving intrinsically disordered regions (IDRs).

Christophe BIGNON
Giulia PESCE

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