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2MGP

Structure of Plasmodium Yoelii Merozoite Surface Protein 1 - C-terminal Domain

Summary for 2MGP
Entry DOI10.2210/pdb2mgp/pdb
Related2MGR
NMR InformationBMRB: 19233
DescriptorMerozoite surface protein 1 (1 entity in total)
Functional Keywordsmembrane protein
Biological sourcePlasmodium yoelii yoelii
Cellular locationCell membrane; Lipid-anchor, GPI-anchor (By similarity): P13828
Total number of polymer chains1
Total formula weight10729.72
Authors
Curd, R.D.,Birdsall, B.,Kadekoppala, M.,Ogun, S.,Kelly, G.,Holder, A.A. (deposition date: 2013-11-03, release date: 2014-02-12, Last modification date: 2024-11-13)
Primary citationCurd, R.D.,Birdsall, B.,Kadekoppala, M.,Ogun, S.A.,Kelly, G.,Holder, A.A.
The structure of Plasmodium yoelii merozoite surface protein 119, antibody specificity and implications for malaria vaccine design
OPEN BIOLOGY, 4:130091-130091, 2014
Cited by
PubMed Abstract: Merozoite surface protein 1 (MSP1) has been identified as a target antigen for protective immune responses against asexual blood stage malaria, but effective vaccines based on MSP1 have not been developed so far. We have modified the sequence of Plasmodium yoelii MSP119 (the C-terminal region of the molecule) and examined the ability of the variant proteins to bind protective monoclonal antibodies and to induce protection by immunization. In parallel, we examined the structure of the protein and the consequences of the amino acid changes. Naturally occurring sequence polymorphisms reduced the binding of individual protective antibodies, indicating that they contribute to immune evasion, but immunization with these variant proteins still provided protective immunity. One variant that resulted in the localized distortion of a loop close to the N-terminus of MSP119 almost completely ablated protection by immunization, indicating the importance of this region of MSP119 as a target for protective immunity and in vaccine development.
PubMed: 24403012
DOI: 10.1098/rsob.130091
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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数据于2025-06-25公开中

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