Processing of thePlasmodium falciparum major merozoite surface protein-1: identification of a 33-kilodalton secondary processing product which is shed prior to erythrocyte invasion

doi:10.1016/0166-6851(91)90128-S

Molecular and Biochemical Parasitology

Volume 49, Issue 1, November 1991, Pages 35-44

https://doi.org/10.1016/0166-6851(91)90128-S Get rights and content

Abstract

We have previously shown that only a single 19-kDa fragment of thePlasmodium falciparum major merozoite surface protein (MSP1) is carried with an invading merozoite into the infected red cell. This fragment (MSPI₁₉) is derived from the C-terminal, membrane-bound end of a major product, MSPI₄₂, of the primary stage of MSPI proteolytic processing. Using a monoclonal antibody mapped to an epitope within the N-terminal region of MSPI₄₂, we have shown that a soluble 33-kDa polypeptide (MSPI₃₃) corresponding to the N-terminal region of MSPI₄₂ is shed into culture supernatants during merozoite release and erythrocyte invasion. These observations provide further evidence that the secondary processing of MSPI₄₂ involves a highly site-specific proteolytic activity.

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Processing of thePlasmodium falciparum major merozoite surface protein-1: identification of a 33-kilodalton secondary processing product which is shed prior to erythrocyte invasion

Abstract

Mol. Biochem. Parasitol.

J. Biol. Chemistry

FEBS Lett.

Trans. R. Soc. Trop. Med. Hyg.

J. Mol. Biol.

Methods Enzymol.

The three major antigens on the surface ofPlasmodium falciparum merozoites are derived from a single high molecular weight precursor

J. Exp. Med.

Processing of the precursor to the major merozoite antigens ofPlasmodium falciparum

Parasitology

Epitope map and processing scheme for the 195,000-dalton surface glycoprotein ofPlasmodium falciparum merozoites deduced from cloned overlapping segments of the gene

Monoclonal antibody characterisation of the 195-kilodalton major surface glycoprotein ofPlasmodium falciparum malaria schizonts and merozoites: identification of additional processed products and a serotype-restricted repetitive epitope

J. Immunol.

A single fragment of a malaria merozoite surface protein remains on the parasite during red cell invasion and is the target of invasion-inhibiting antibodies

J. Exp. Med.

Inhibition ofPlasmodium falciparum growth by IgG antibody produced by human lymphocytes transformed with Epstein-Barr virus

Clin. Exp. Immunol.

Antigenic diversity in the human malaria parasitePlasmodium falciparum

Science