Conformational dynamics and antigenicity in the disordered malaria antigen merozoite surface protein 2
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F15%3A00082589" target="_blank" >RIV/00216224:14740/15:00082589 - isvavai.cz</a>
Výsledek na webu
<a href="http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0119899" target="_blank" >http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0119899</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1371/journal.pone.0119899" target="_blank" >10.1371/journal.pone.0119899</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Conformational dynamics and antigenicity in the disordered malaria antigen merozoite surface protein 2
Popis výsledku v původním jazyce
Merozoite surface protein 2 (MSP2) of Plasmodium falciparum is an abundant, intrinsically disordered protein that is GPI-anchored to the surface of the invasive blood stage of the malaria parasite. Recombinant MSP2 has been trialled as a component of a malaria vaccine, and is one of several disordered proteins that are candidates for inclusion in vaccines for malaria and other diseases. Nonetheless, little is known about the implications of protein disorder for the development of an effective antibody response. We have therefore undertaken a detailed analysis of the conformational dynamics of the two allelic forms of MSP2 (3D7 and FC27) using NMR spectroscopy. Chemical shifts and NMR relaxation data indicate that conformational and dynamic properties of the N- And C-terminal conserved regions in the two forms of MSP2 are essentially identical, but significant variation exists between and within the central variable regions.
Název v anglickém jazyce
Conformational dynamics and antigenicity in the disordered malaria antigen merozoite surface protein 2
Popis výsledku anglicky
Merozoite surface protein 2 (MSP2) of Plasmodium falciparum is an abundant, intrinsically disordered protein that is GPI-anchored to the surface of the invasive blood stage of the malaria parasite. Recombinant MSP2 has been trialled as a component of a malaria vaccine, and is one of several disordered proteins that are candidates for inclusion in vaccines for malaria and other diseases. Nonetheless, little is known about the implications of protein disorder for the development of an effective antibody response. We have therefore undertaken a detailed analysis of the conformational dynamics of the two allelic forms of MSP2 (3D7 and FC27) using NMR spectroscopy. Chemical shifts and NMR relaxation data indicate that conformational and dynamic properties of the N- And C-terminal conserved regions in the two forms of MSP2 are essentially identical, but significant variation exists between and within the central variable regions.
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
CE - Biochemie
OECD FORD obor
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Návaznosti výsledku
Projekt
<a href="/cs/project/ED1.1.00%2F02.0068" target="_blank" >ED1.1.00/02.0068: CEITEC - central european institute of technology</a><br>
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2015
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
PLOS ONE
ISSN
1932-6203
e-ISSN
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Svazek periodika
10
Číslo periodika v rámci svazku
3
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
18
Strana od-do
"nestránkováno"
Kód UT WoS článku
000350688100130
EID výsledku v databázi Scopus
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