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Analysis of human antibodies to erythrocyte binding antigen 175 of Plasmodium falciparum.


ABSTRACT: Invasion of human erythrocytes by Plasmodium falciparum merozoites is a multistep process. For many strains of the parasite, part of this process requires that the erythrocyte binding antigen 175 (EBA-175) of the merozoite binds to sialic acid residues of glycophorin A on the erythrocyte surface, a receptor-ligand interaction which represents a potential target for inhibition by antibodies. This study characterizes the reactivity of naturally acquired human antibodies with four recombinant proteins representing parts of EBA-175 (region II, regions III to V, and the dimorphic C and F segment region) in populations in which the organism is endemic. Serum immunoglobulin G (IgG) recognizing the recombinant proteins is predominantly of the IgG1 and IgG3 subclasses, and its prevalence increases with age. In a large population study in The Gambia, serum positivity for IgG or IgG1 and IgG3 subclass antibodies to each of the EBA-175 recombinant antigens was not significantly associated with subsequent protection from clinical malaria. However, there was a trend indicating that individuals with high levels of IgG to region II may have some protection.

SUBMITTER: Okenu DM 

PROVIDER: S-EPMC101506 | biostudies-literature | 2000 Oct

REPOSITORIES: biostudies-literature

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Analysis of human antibodies to erythrocyte binding antigen 175 of Plasmodium falciparum.

Okenu D M DM   Riley E M EM   Bickle Q D QD   Agomo P U PU   Barbosa A A   Daugherty J R JR   Lanar D E DE   Conway D J DJ  

Infection and immunity 20001001 10


Invasion of human erythrocytes by Plasmodium falciparum merozoites is a multistep process. For many strains of the parasite, part of this process requires that the erythrocyte binding antigen 175 (EBA-175) of the merozoite binds to sialic acid residues of glycophorin A on the erythrocyte surface, a receptor-ligand interaction which represents a potential target for inhibition by antibodies. This study characterizes the reactivity of naturally acquired human antibodies with four recombinant prote  ...[more]

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