2flg
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Revision as of 08:29, 21 November 2007
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Solution structure of an EGF-LIKE domain from the Plasmodium falciparum merozoite surface protein 1
Overview
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.
About this Structure
2FLG is a Single protein structure of sequence from [1] with NH2 as ligand. Full crystallographic information is available from OCA.
Reference
Synthesis, solution structure and immune recognition of an epidermal growth factor-like domain from Plasmodium falciparum merozoite surface protein-1., James S, Moehle K, Renard A, Mueller MS, Vogel D, Zurbriggen R, Pluschke G, Robinson JA, Chembiochem. 2006 Dec;7(12):1943-50. PMID:17068840
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