Abstract
The variant surface antigen VAR2CSA is a pregnancy malaria vaccine candidate, but its size and polymorphism are obstacles to development. We expressed 3D7-type VAR2CSA domains in Escherichia coli as insoluble His-tagged proteins (Duffy binding-like [DBL] domains DBL1, DBL3, DBL4, and DBL5) that were denatured and refolded or as soluble glutathione S-transferase-tagged protein (DBL6). Anti-DBL5 antiserum cross-reacted with surface proteins of chondroitin sulfate A (CSA)-binding laboratory strains (3D7-CSA and FCR3-CSA) and a clinical pregnancy malaria isolate, whereas anti-DBL6 antiserum reacted only to 3D7 surface protein. This is the first report that E. coli-expressed VAR2CSA domains induce antibody to native VAR2CSA.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Antibodies, Protozoan / biosynthesis
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Antibodies, Protozoan / immunology
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Antigens, Protozoan / biosynthesis
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Antigens, Protozoan / genetics
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Antigens, Protozoan / immunology*
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DNA, Protozoan / chemistry
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DNA, Protozoan / genetics
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Erythrocytes / parasitology
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Female
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Humans
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Malaria, Falciparum / parasitology
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Molecular Sequence Data
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Phylogeny
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Plasmodium falciparum / genetics
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Plasmodium falciparum / immunology*
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Polymerase Chain Reaction
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Pregnancy
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Pregnancy Complications, Parasitic / parasitology
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Protein Structure, Tertiary
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / genetics
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Recombinant Proteins / immunology
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Sequence Alignment
Substances
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Antibodies, Protozoan
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Antigens, Protozoan
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DNA, Protozoan
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Recombinant Proteins
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VAR2CSA protein, Plasmodium falciparum