期刊
MALARIA JOURNAL
卷 9, 期 -, 页码 -出版社
BMC
DOI: 10.1186/1475-2875-9-76
关键词
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资金
- National Natural Science Foundation of China [30430610]
- National Basic Research Programme ( 973 Programme) in China [2007CB513100]
- National 863 Programme in China [2006AA02A222]
- Shanghai Leading Academic Discipline [B901]
Background: The Plasmodium falciparum chimeric protein PfCP-2.9 is a promising asexual-stage malaria vaccine evaluated in clinical trials. This chimeric protein consists of two cysteine-rich domains: domain III of the apical membrane antigen 1 (AMA-1 [III]) and the C-terminal region of the merozoite surface protein 1 (MSP1-19). It has been reported that the fusion of these two antigens enhanced their immunogenicity and antibody-mediated inhibition of parasite growth in vitro. Methods: The N-15-labeled and C-13/N-15-labeled PfCP-2.9 was produced in Pichia pastoris for nuclear magnetic resonance (NMR) structure analysis. The chemical shift assignments of PfCP-2.9 were compared with those previously reported for the individual domains (i.e., PfAMA-1(III) or PfMSP 1-19). The two-dimensional spectra and transverse relaxation rates (R-2) of the PfMSP1-19 alone were compared with that of the PfCP-2.9. Results: Confident backbone assignments were obtained for 122 out of 241 residues of PfCP-2.9. The assigned residues in PfCP-2.9 were very similar to those previously reported for the individual domains. The conformation of the PfMSP1-19 in different constructs is essentially the same. Comparison of transverse relaxation rates (R-2) strongly suggests no weak interaction between the domains. Conclusions: These data indicate that the fusion of AMA-1(III) and MSP1-19 as chimeric protein did not change their structures, supporting the use of the chimeric protein as a potential malaria vaccine.
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