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Longhi’s Team Projects

Molecular partnership of the intrinsically disorder C-terminal domain of the measles virus nucleoprotein (NTAIL)

Heads Sonia LONGHI

 Determining the 3D structure of the ternary complex between hsp70, hsp40 and the Box2-Box3 region of measles virus NTAIL

People involved: A Doizy (PhD student, fellowship of the French-Italian University), Prof. M. Lotti (Universita’ degli Studi Milano-Bicocca)

Previous studies showed that the major inducible heat shock protein (hsp70) stimulates MeV transcription and replication, with this ability relying on interaction between hsp70 and NTAIL [14]

Subsequently, we showed that the hsp40 co-chaperone enhances the affinity of the hsp70-NTAIL binding reaction, with this increase in the affinity requiring primarily the nucleotide binding domain of hsp70 and with hsp40 displaying no significant affinity for NTAIL. We also showed that hsp40 directly enhanced hsp70 ATPase activity in an NTAIL-dependent manner, while our coworker M. Oglesbee (Ohio State University) showed that formation of hsp40-hsp70-NTAIL intracellular complexes requires the presence of NTAIL Box2 (aa 489-506 of N) and Box3 (aa 517-525) [15]. We are currently setting up the optimal conditions for formation of a ternary complex consisting of hsp70, hsp40 and the Box2-Box3 region of NTAIL in view of crystallization trials and structure determination by X-ray crystallography.


[14] Zhang X, Bourhis JM, Longhi S, Carsillo T, Buccellato M, Morin B, Canard B, Oglesbee M (2005) Virology 337 162-74

[15] Couturier M, Buccellato M, Costanzo S, Bourhis JM, Shu Y, Nicaise M, Desmadril M, Flaudrops C, Longhi S, Oglesbee M (2010) J Mol Recognit 23(3) 301-15
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