Expression of an immunologically (MSP-1(42)) reactive merozoite surface protein in E-coli

文献类型： 外文期刊

第一作者： Leung, WH

作者： Leung, WH;Meng, ZQ;Hui, G;Ho, WK

作者机构：

关键词： malaria;vaccine;merozoite;surface protein;expression;immunity;PLASMODIUM-FALCIPARUM MEROZOITES;HUMORAL IMMUNE-RESPONSES;NON-DETERGENT SULFOBETAINES;CARBOXYL-TERMINAL FRAGMENT;MALARIA VACCINE CANDIDATE;INHIBIT PARASITE GROWTH;B-CELL EPITOPES;AOTUS MONKEYS;T-CELL;MONOCLONAL-ANTIBODY

期刊名称：BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS （ 影响因子：3.77； 五年影响因子：4.137 ）

ISSN：

年卷期：

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收录情况： SCI

摘要： The 42-kDa carboxyl-terminal processing fragment of Plasmodium falciparum merozoite surface protein-1 (PfMSP-1(42)) is one of the anti-malarial vaccine candidate antigens. In the present study, recombinant MSP-1(42) was expressed as a fusion protein in a novel E. coli host. The average yield of the recombinant protein was 48 mg/1 of bacterial culture. The antigenicity and immunogenicity of the purified protein were evaluated by comparing the results with those obtained from a well-characterized recombinant MSP-1(42) (Bmp42) expressed in the baculovirus expression system previously described from our laboratory. We observed that there is a high degree of similarities between the two recombinant proteins. Based on the results from T and B cell response, in vitro parasite growth inhibition, as well as cross-reactivities with several well-characterized MSP-1 specific Mabs, the bacterial expressed protein is apparently comparable to Bmp42 in terms of immunoreactivities. Our results suggest that the bacterial expression system could be employed to express immunologically active recombinant MSP-1(42) at elevated levels. This system may be an attractive alternative for producing a protective vaccine for human use at lower cost. (C) 2004 Elsevier B.V. All rights reserved.

分类号： Q5

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