MACRAILD, Christopher A., Milan ZACHRDLA, Dean ANDREW, Bankala KRISHNARJUNA, Jiří NOVÁČEK, Lukáš ŽÍDEK, Vladimír SKLENÁŘ, Jack S. RICHARDS, James G. BEESON, Robin F. ANDERS and Raymond S. NORTON. Conformational dynamics and antigenicity in the disordered malaria antigen merozoite surface protein 2. PLOS ONE. San Francisco: Public Library Science, 2015, vol. 10, No 3, p. "nestránkováno", 18 pp. ISSN 1932-6203. Available from: https://dx.doi.org/10.1371/journal.pone.0119899.
Other formats:   BibTeX LaTeX RIS
Basic information
Original name Conformational dynamics and antigenicity in the disordered malaria antigen merozoite surface protein 2
Authors MACRAILD, Christopher A. (36 Australia), Milan ZACHRDLA (203 Czech Republic, belonging to the institution), Dean ANDREW (36 Australia), Bankala KRISHNARJUNA (36 Australia), Jiří NOVÁČEK (203 Czech Republic, belonging to the institution), Lukáš ŽÍDEK (203 Czech Republic, guarantor, belonging to the institution), Vladimír SKLENÁŘ (203 Czech Republic, belonging to the institution), Jack S. RICHARDS (36 Australia), James G. BEESON (36 Australia), Robin F. ANDERS (36 Australia) and Raymond S. NORTON (36 Australia).
Edition PLOS ONE, San Francisco, Public Library Science, 2015, 1932-6203.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 3.057
RIV identification code RIV/00216224:14740/15:00082589
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1371/journal.pone.0119899
UT WoS 000350688100130
Keywords in English amino terminal sequence; animal experiment; animal model; antibody response; antibody specificity; antigenicity
Tags rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Eva Špillingová, učo 110713. Changed: 22/3/2016 15:24.
Abstract
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. We observe a strong relationship between the conformational dynamics and the antigenicity of MSP2, as assessed with antisera to recombinant MSP2. Regions of increased conformational order in MSP2, including those in the conserved regions, are more strongly antigenic, while the most flexible regions are minimally antigenic. This suggests that modifications that increase conformational order may offer a means to tune the antigenicity of MSP2 and other disordered antigens, with implications for vaccine design.
Links
ED1.1.00/02.0068, research and development projectName: CEITEC - central european institute of technology
PrintDisplayed: 25/4/2024 09:58