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J. Biol. Chem., Vol. 276, Issue 20, 17111-17116, May 18, 2001
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From the Malaria Research Group, International Centre for Genetic
Engineering and Biotechnology (ICGEB), Aruna Asaf Ali Marg, New
Delhi 110067, India
Invasion of erythrocytes by malaria parasites is
mediated by specific molecular interactions. Plasmodium
vivax is completely dependent on interaction with the Duffy blood
group antigen to invade human erythrocytes. The P. vivax
Duffy-binding protein, which binds the Duffy antigen during invasion,
belongs to a family of erythrocyte-binding proteins that also includes
Plasmodium falciparum sialic acid binding protein and
Plasmodium knowlesi Duffy binding protein. The receptor
binding domains of these proteins lie in a conserved, N-terminal,
cysteine-rich region, region II, found in each of these proteins. Here,
we have expressed P. vivax region II (PvRII), the P. vivax Duffy binding domain, in Escherichia coli.
Recombinant PvRII is incorrectly folded and accumulates in inclusion
bodies. We have developed methods to refold and purify recombinant
PvRII in its functional conformation. Biochemical, biophysical, and
functional characterization confirms that recombinant PvRII is pure,
homogeneous, and functionally active in that it binds Duffy-positive
human erythrocytes with specificity. Refolded PvRII is highly
immunogenic and elicits high titer antibodies that can inhibit binding
of P. vivax Duffy-binding protein to erythrocytes,
providing support for its development as a vaccine candidate for
P. vivax malaria. Development of methods to produce functionally active recombinant PvRII is an important step for structural studies as well as vaccine development.
Biochemical, Biophysical, and Functional Characterization of
Bacterially Expressed and Refolded Receptor Binding Domain of
Plasmodium vivax Duffy-binding Protein*
*
This investigation received support from the United Nations
Developmental Program/World Bank/ World Health Organization Special Program for Research and Training in Tropical Diseases (TDR) and International Research Scholar's Program of Howard Hughes Medical Institute.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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