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Infection and Immunity, July 2001, p. 4390-4397, Vol. 69, No. 7
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.7.4390-4397.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Naturally Acquired Antibody Responses to Plasmodium falciparum Merozoite Surface Protein 4 in a Population Living in an Area of Endemicity in Vietnam

Lina Wang,1 Thomas L. Richie,2 Anthony Stowers,3 Doan Hanh Nhan,4 and Ross L. Coppel1,*

Department of Microbiology, Monash University, Clayton, Victoria 3800, Australia1; Malaria Program, Naval Medical Research Center, Silver Spring, Maryland 209102; Malaria Vaccine Development Unit, NIAID, National Institutes of Health, Rockville, Maryland 208523; and Institute for Microbiology, Parasitology and Entomology, Hanoi, Vietnam4

Received 24 August 2000/Returned for modification 28 December 2000/Accepted 12 April 2001

Merozoite surface protein 4 (MSP4) of Plasmodium falciparum is a glycosylphosphatidylinositol-anchored integral membrane protein that is being developed as a component of a subunit vaccine against malaria. We report here the measurement of naturally acquired antibodies to MSP4 in a population of individuals living in the Khanh-Hoa region of Vietnam, an area where malaria is highly endemic. Antibodies to MSP4 were detected in 94% of the study population at titers of 1:5,000 or greater. Two forms of recombinant MSP4 produced in either Escherichia coli or Saccharomyces cerevisiae were compared as substrates in the enzyme-linked immunosorbent assay. There was an excellent correlation between reactivity measured to either, although the yeast substrate was recognized by a higher percentage of sera. Four different regions of MSP4 were recognized by human antibodies, demonstrating that there are at least four distinct epitopes in this protein. In the carboxyl terminus, where the single epidermal growth factor-like domain is located, the reactive epitope(s) was shown to be conformation dependent, as disruption of the disulfide bonds almost completely abolished reactivity with human antibodies. The anti-MSP4 antibodies were mainly of the immunoglobulin G1 (IgG1) and IgG3 subclasses, suggesting that such antibodies may play a role in opsonization and complement-mediated lysis of free merozoites. Individuals in the study population were drug-cured and followed up for 6 months; no significant correlation was observed between the anti-MSP4 antibodies and the absence of parasitemia during the surveillance period. As a comparison, antibodies to MSP119, a leading vaccine candidate, were measured, and no correlation with protection was observed in these individuals. The anti-MSP119 antibodies were predominantly of the IgG1 isotype, in contrast to the IgG3 predominance noted for MSP4.

* Corresponding author. Mailing address: Department of Microbiology, Monash University, Clayton, Victoria 3800, Australia. Phone: 61 3 9905 4822. Fax: 61 3 9905 4811. E-mail: ross.coppel{at}med.monash.edu.au.

Infection and Immunity, July 2001, p. 4390-4397, Vol. 69, No. 7
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.7.4390-4397.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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