2FLG
Solution structure of an EGF-LIKE domain from the Plasmodium falciparum merozoite surface protein 1
Summary for 2FLG
| Entry DOI | 10.2210/pdb2flg/pdb |
| Related | 1CEJ |
| NMR Information | BMRB: 7010 |
| Descriptor | Merozoite surface protein 1 (1 entity in total) |
| Functional Keywords | egf-like domain, extracellular, modular protein, surface antigen, malaria vaccine component, surface protein, surface active protein |
| Cellular location | Cell membrane; Lipid-anchor, GPI-anchor: P04933 |
| Total number of polymer chains | 1 |
| Total formula weight | 5600.31 |
| Authors | James, S.,Moehle, K.,Pluschke, G.,Robinson, J. (deposition date: 2006-01-06, release date: 2006-02-21, Last modification date: 2024-11-06) |
| Primary citation | James, S.,Moehle, K.,Renard, A.,Mueller, M.S.,Vogel, D.,Zurbriggen, R.,Pluschke, G.,Robinson, J.A. Synthesis, solution structure and immune recognition of an epidermal growth factor-like domain from Plasmodium falciparum merozoite surface protein-1. Chembiochem, 7:1943-1950, 2006 Cited by PubMed Abstract: The Plasmodium falciparum merozoite surface protein-1 19 kDa fragment (MSP-1(19)) comprises two closely packed EGF-like domains (EGF=epidermal growth factor), each stabilized by three disulfide bonds. The native conformation of this protein is important for eliciting P. falciparum growth inhibitory antibodies. Here we show that the N-terminal EGF domain alone can be chemically synthesized and efficiently refolded to a native-like state, as shown by its solution structure as determined by NMR spectroscopy. In order to study its immunogenicity, the domain was coupled through its N terminus to a phospholipid and incorporated into reconstituted influenza virus-like particles (virosomes). When used to immunize mice, the peptide-loaded virosomes elicited potent humoral immune responses that were shown by Western blots and immunofluorescence assays to cross-react with native MSP-1 on the surfaces of P. falciparum blood stage parasites. This opens the way for a medicinal chemistry-oriented approach to the study and optimization of the antigenicity of the protein as a potential malaria vaccine candidate, whilst exploiting the immunopotentiating properties of influenza virosomes as a delivery vehicle. PubMed: 17068840DOI: 10.1002/cbic.200600357 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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