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CHIKV-FBDD SIGNED

Structural investigation into functionality of Chikungunya virus nsP2 in replication complex and screening of small molecules for its inhibition

Total Cost €

0

EC-Contrib. €

0

Partnership

0

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 CHIKV-FBDD project word cloud

Explore the words cloud of the CHIKV-FBDD project. It provides you a very rough idea of what is the project "CHIKV-FBDD" about.

identification    elucidate    ns    discovered    positive    reveal    genome    drug    causes    organization    crystallographic    recombinant    togaviridae    interfere    small    counteracting    pain    central    alphavirus    newly    replication    persisting    first    explored    molecules    inhibitory    polyprotein    fragments    functional    arthritis    defence    existent    antiviral    enzymatic    limited    chemical    fluorescence    leads    elaboration    druggability    libraries    exhibiting    cycle    biophysical    revealed    form    joint    interaction    techniques    chikungunya    people    proteins    assays    millions    world    surface    characterizing    released    whereas    viral    pathogen    create    protein    ground    regarding    medically    chikv    single    variety    intense    attractive    multifunctional    sensitive    proteolytic    fever    initially    structural    chronic    binding    largely    rna    sense    nsp2    family    precursor    eliminating    contacts    virus    pockets    biology    screening    stranded    infection    plays    vitro    platforms    clear    inhibitors    spatial    compounds    cellular    mechanisms   

Project "CHIKV-FBDD" data sheet

The following table provides information about the project.

Coordinator
THE CHANCELLOR MASTERS AND SCHOLARSOF THE UNIVERSITY OF CAMBRIDGE 

Organization address
address: TRINITY LANE THE OLD SCHOOLS
city: CAMBRIDGE
postcode: CB2 1TN
website: www.cam.ac.uk

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country United Kingdom [UK]
 Total cost 195˙454 €
 EC max contribution 195˙454 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2015
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2016
 Duration (year-month-day) from 2016-06-07   to  2018-06-06

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    THE CHANCELLOR MASTERS AND SCHOLARSOF THE UNIVERSITY OF CAMBRIDGE UK (CAMBRIDGE) coordinator 195˙454.00

Map

 Project objective

Chikungunya virus (CHIKV) is a medically important pathogen that affected millions of people around the world. CHIKV infection causes high fever, intense joint pain and often leads to chronic virus-induced arthritis, thus there is a clear necessity to develop antiviral compounds capable of eliminating persisting virus. CHIKV is an alphavirus from Togaviridae family with single-stranded positive-sense RNA genome, which replication is carried out by a complex of four viral non-structural (ns) proteins, initially produced in a form of ns-polyprotein precursor and released by proteolytic processing. Because multifunctional nsP2 plays a central role in a replication cycle of CHIKV by exhibiting various enzymatic activities and counteracting cellular defence mechanisms, it represents the most attractive target for drug design and screening. Currently, the structural information regarding CHIKV ns-proteins is limited, whereas the platforms for in vitro testing the potential inhibitors are largely non-existent. Therefore the first aims of this project will be to apply structural biology approaches to elucidate spatial organization of nsP2 and to reveal its contacts with other ns-proteins in the replication complex. The druggability of nsP2 will be then explored by screening recombinant proteins against libraries of chemical fragments and characterizing binding of small molecules using sensitive biophysical techniques and crystallographic analysis. The potential of selected compounds to interfere with enzymatic or interaction properties of nsP2 will be revealed using variety of fluorescence-based assays developed in this project. The newly discovered knowledge about structural features of CHIKV nsP2, identification of novel protein surface pockets and binding molecules, and the development of functional assays for the analysis of their inhibitory potential are expected to create the ground for future elaboration of novel specific inhibitors of CHIKV.

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