Development of an immunoassay using recombinant maltose-binding protein-STa fusions for quantitating antibody responses against STa, the heat-stable enterotoxin of Escherichia coli

Author:

Aitken R1,Hirst T R1

Affiliation:

1. Department of Genetics, University of Leicester, United Kingdom.

Abstract

A set of fusion proteins containing heat-stable enterotoxin (STa) and maltose-binding protein were engineered. These molecules were readily purified and used as solid-phase antigens in an enzyme-linked immunosorbent assay to monitor anti-STa responses in mice immunized with a recombinant vaccine composed of STa and the B subunit of heat-labile enterotoxin.

Publisher

American Society for Microbiology

Subject

Microbiology (medical)

Reference18 articles.

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2. Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein;di Guan C.;Gene,1988

3. Export and processing analysis of a fusion between the extracellular heat-stable enterotoxin and the periplasmic B subunit of the heat-labile enterotoxin in Escherichia coli;Guzman-Verduzco L. M.;Mol. Microbiol.,1990

4. Coordinated assembly of multisubunit proteins: oligomerization of bacterial enterotoxins in vivo and in vitro;Hardy S. J. S.;Proc. Natl. Acad. Sci. USA,1988

5. Hirst T. R. 1991. Assembly and secretion of oligomeric toxins in Gram-negative bacteria p. 75-100. In J. E. Alouf and J. H. Freer (ed.) A source book of bacterial protein toxins. Academic Press London.

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