Plasmodium falciparum anti-MSP1-19 antibodies induced by MSP1-42 and MSP1-19 based vaccines differed in specificity and parasite growth inhibition in terms of recognition of conserved versus variant epitopes.

Plasmodium falciparum anti-MSP1-19 antibodies induced by MSP1-42 and MSP1-19 based vaccines differed in specificity and parasite growth inhibition in terms of recognition of conserved versus variant epitopes. Research Abstract Details 

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Plasmodium falciparum anti-MSP1-19 antibodies induced by MSP1-42 and MSP1-19 based vaccines differed in specificity and parasite growth inhibition in terms of recognition of conserved versus variant epitopes. Abstract Text:

George Hui,Caryn Hashimoto,

The C-terminal 42 kDa fragment (MSP1-42) and its smaller 19 kDa subfragment (MSP1-19) of the Plasmodium falciparum merozoite surface protein, MSP1, are leading candidate malaria vaccines. Since the targets of protective immunity lie within the MSP1-19, we compared the anti-MSP1-19 antibodies induced by vaccination with recombinant MSP1-42 and MSP1-19. The specificities of the antibody responses were analyzed using five recombinant MSP1-19s expressing different naturally occurring variant amino acid residues. We observed dramatic differences in the specificities of the anti-MSP1-19 antibodies induced by the two vaccines. MSP1-42 consistently induced crossreactive antibodies; whereas the antibodies induced by recombinant MSP1-19 were highly variable among animals in terms of recognition of conserved versus variant epitopes. Of the variant residues examined, only a subset significantly contributed as part of immunogenic B epitopes. MSP1-42 consistently induced potent growth inhibitory antibodies that recognized conserved epitopes, leading to efficient inhibition of heterologous parasites. In contrast, MSP1-19 induced strong inhibitory antibody responses in only a subset of animals studied. In some of the MSP1-19 immunized animals, inhibition of homologous parasites may be due to recognition of inhibitory epitopes associated with the homologous variant residues, and the induction of antibodies to conserved inhibitory epitopes may not be efficiently achieved. These data suggest an advantage of using MSP1-42 over MSP1-19 based vaccines.

Plasmodium falciparum anti-MSP1-19 antibodies induced by MSP1-42 and MSP1-19 based vaccines differed in specificity and parasite growth inhibition in terms of recognition of conserved versus variant epitopes. Publishing Authors By Initials

G Hui,C Hashimoto,

For similar proteins: recombinant proteins: vaccines, synthetic research abstracts see: proteins: recombinant proteins: vaccines, synthetic research

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Plasmodium falciparum anti-MSP1-19 antibodies induced by MSP1-42 and MSP1-19 based vaccines differed in specificity and parasite growth inhibition in terms of recognition of conserved versus variant epitopes. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Vaccine

VOLUME: 25

Page Numbers: 948-56

Journal Abbreviation: Vaccine

ISSN: 0264-410X

DAY: 18

MONTH: 09

YEAR: 2006

Plasmodium falciparum anti-MSP1-19 antibodies induced by MSP1-42 and MSP1-19 based vaccines differed in specificity and parasite growth inhibition in terms of recognition of conserved versus variant epitopes. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 8406899

Plasmodium falciparum anti-MSP1-19 antibodies induced by MSP1-42 and MSP1-19 based vaccines differed in specificity and parasite growth inhibition in terms of recognition of conserved versus variant epitopes. Keywords Mesh Terms:

KEYWORDS: Vaccines, Synthetic

MESH TERMS: immunology

Chemical & Substance for Abstract: Plasmodium falciparum anti-MSP1-19 antibodies induced by MSP1-42 and MSP1-19 based vaccines differed in specificity and parasite growth inhibition in terms of recognition of conserved versus variant epitopes. Information

Substance Name: Vaccines, Synthetic

Registry Number: 0

Grant and Affiliation Information for Plasmodium falciparum anti-MSP1-19 antibodies induced by MSP1-42 and MSP1-19 based vaccines differed in specificity and parasite growth inhibition in terms of recognition of conserved versus variant epitopes.

AFFILIATION: Department of Tropical Medicine and Pharmacology, John A. Burns School of Medicine, University of Hawaii at Manoa, United States. ghui@hawaii.edu

Country: Netherlands

AGENCY: United States NIAID

GRANT: R01AI457680

ACRONYM: AI

MEDLINETA: Vaccine

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