CDNA CLONING AND FUNCTIONAL EXPRESSION OF THE SCHISTOSOMA-MANSONI PROTECTIVE ANTIGEN TRIOSE-PHOSPHATE ISOMERASE

被引：72

作者：

SHOEMAKER, C

GROSS, A

GEBREMICHAEL, A

HARN, D

机构：

[1] Tropical Public Health Dept., Harvard Sch. of Public Health, Boston, MA 02115

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1992年 / 89卷 / 05期

关键词：

RECOMBINANT DNA; GLYCOLYSIS; VACCINE; PROTECTIVE IMMUNITY;

D O I：

10.1073/pnas.89.5.1842

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

M.1 monoclonal antibody has previously been shown to passively transfer partial resistance to schistosome infection within mice and to recognize a 28-kDa antigen that has peptide sequence homology with triose-phosphate isomerase (TPI; D-glyceraldehyde-3-phosphate ketol-isomerase, EC 5.3.1.1). We have now isolated the complete coding DNA for Schistosoma mansoni TPI and confirmed that this cDNA encodes the 28-kDa antigen recognized by M.1. The predicted translation product has strong homology with other TPIs, particularly from higher eukaryotes, and the sequence homology is greatest in regions known to form the active site. The complete coding DNA has been expressed within an Escherichia coli host to produce high levels of soluble, recombinant S. mansoni TPI protein. The product is recognized and purified by the M.1 antibody and is a functional TPI with an intrinsic specific activity comparable to that of rabbit and yeast TPI.

引用

页码：1842 / 1846

页数：5

共 31 条

[1]

ALBER T, 1982, Journal of Molecular and Applied Genetics, V1, P419

[2] PRIMARY STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM BACILLUS-STEAROTHERMOPHILUS [J].