HK97 MATURATION

Structural studies of HK97 bacteriophage assembly and maturation

Coordinatore	INSTITUT PASTEUR    more  Organization address address: RUE DU DOCTEUR ROUX 25-28 city: PARIS CEDEX 15 postcode: 75724 contact info Titolo: Dr. Nome: Marie-Laure Cognome: Rosso Email: send email Telefono: +33 1 44 38 95 26 Fax: +33 1 40 61 39 40
Nazionalità Coordinatore	France [FR]
Totale costo	232˙676 €
EC contributo	232˙676 €
Programma	FP7-PEOPLE Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
Code Call	FP7-PEOPLE-2010-IOF
Funding Scheme	MC-IOF
Anno di inizio	2011
Periodo (anno-mese-giorno)	2011-09-01   -   2014-08-31

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	INSTITUT PASTEUR  Organization address address: RUE DU DOCTEUR ROUX 25-28 city: PARIS CEDEX 15 postcode: 75724 contact info Titolo: Dr. Nome: Marie-Laure Cognome: Rosso Email: send email Telefono: +33 1 44 38 95 26 Fax: +33 1 40 61 39 40	FR (PARIS CEDEX 15)	coordinator	232˙676.80
2	UNIVERSITE D'AIX MARSEILLE  Organization address address: Boulevard Charles Livon 58 city: Marseille postcode: 13284 contact info Titolo: Ms. Nome: Céline Cognome: Damon Email: send email Telefono: 33491998595	FR (Marseille)	participant	0.00

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 Obiettivo del progetto (Objective)

'Virus maturation is virtually universal and allows the transition from an initially assembled non-infectious and fragile particle to a robust infectious virion. Siphophage HK97 is an accessible model system, to study assembly and maturation, for which intermediates can be isolated and myriad structural, biophysical and biochemical data are available. The capsid protein fold similarity between HK97, all other dsDNA bacteriophages and some animal viruses suggests that they share common maturation principles. The proposed project seeks to unravel the mechano-chemical reorganization program underlying the structural transitions observed during HK97 procapsid maturation using hybrid methods. It relies on a multi-disciplinary approach involving X-ray crystallography, electron microscopy and tomography to obtain multi-scale data ranging from atom to whole-cell. We aim to obtain structures of three different HK97 procapsid maturation intermediates to shed light on mechanisms involved in initial assembly of an energy-loaded particle as well as on forces driving forward maturation. We will also use electron tomography to study in vivo aspects of HK97 assembly and maturation in Escherichia coli infected cells. The outcome will allow apprehending mechanisms, dynamics and energetics of viral maturation as well as provide a basis for the use of HK97 as a delivery system for nano-medical applications.'

Introduzione (Teaser)

Maturation of the capsid, the outside protein shell of the virus, is an essential step by which many viruses become infectious. Scientists shed light on mechanisms with important implications for antiviral therapies for numerous infectious diseases.