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Refolding, purification, and crystallization of apical membrane antigen 1 from Plasmodium falciparum


Gupta, A; Bai, T; Murphy, V; Strike, P; Anders, RF; Batchelor, AH
2005-05
PROTEIN EXPRESSION AND PURIFICATION
Journal Article
41
1
186-198
Extracellular domains of malaria antigens almost invariably contain disulphide linkages but lack N- and O-linked glycosylation. The best practical approach to generating recombinant extracellular Plasmodium proteins is not established and the problems encountered when using a bacterial expression/refolding approach are discussed in detail. Limited proteolysis experiments were used to identify a relatively non-flexible core region of the Plasmodium falciparum protein apical membrane antigen 1 (AMA1), and refolding/purification was used to generate two fragments of AMA1 Several chromatographically distinct AMA1 variants were identified that are presumably differentially refolded proteins. One of these AMA1 preparations proved to be crystallizable and generated two crystal forms that diffracted X-rays to 2 angstrom resolution. (c) 2005 Elsevier Inc. All rights reserved.
ACADEMIC PRESS INC ELSEVIER SCIENCE
MALARIA VACCINE CANDIDATE; MEROZOITE SURFACE PROTEIN-1; HIGH-LEVEL EXPRESSION; ERYTHROCYTE INVASION; TOXOPLASMA-GONDII; CRYSTAL-STRUCTURE; BINDING PROTEIN; AMA-1; KNOWLESI; INHIBIT
10.1016/j.pep.2005.01.005
Refer to copyright notice on published article.

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Creation Date 2005-05-01 12:00:00