Solution structure of a Plasmodium falciparum AMA-1/MSP 1 chimeric protein vaccine candidate (PfCP-2
- 影响因子：
0.0
- 发表刊物：
Malar. J
- 摘要：
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 15N-labeled and 13C/15N-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 (R2) 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 (R2) 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.
- 论文类型：
期刊论文
- 论文编号：
32
- 卷号：
9
- 页面范围：
76-84
- 是否译文：
否
- 发表时间：
2010-03-18
- 收录刊物：
SCI
- 发布期刊链接：
- 第一作者：
Peng Heng
- 通讯作者：
Hu Yunfei,Pan Weiqing
- 全部作者：
Zhou Aiguo,Jin Changwen
