
Conformation of Escherichia coli outer membrane protein OmpA produced in Bacillus subtilis : Influence of lipopolysaccharide
Author(s) -
Puohiniemi Ritvaleena,
Muotiala Anna,
Hilander Ikka M.,
Sarvas Matti
Publication year - 1993
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1993.tb05942.x
Subject(s) - bacterial outer membrane , bacillus subtilis , escherichia coli , lipopolysaccharide , bacteria , inner membrane , chemistry , bacillus (shape) , biochemistry , membrane protein , microbiology and biotechnology , biology , membrane , gene , genetics , endocrinology
The conformation of the outer membrane protein OmpA of Escherichia coli produced in Bacillus subtilis and solubilized in Sarkosyl was studied by measuring its ability to bind OmpA‐specific phage K3 and to inhibit F‐mediated conjugation. The partially purified protein was inactive in both these assays. Refolding of the protein in the presence of lipopolysaccharide resulted in preparations with full phage‐binding and conjugation‐inhibiting capacity, indicating the formation of surface‐exposed loops of OmpA of native conformation. The finding is of importance for the potential use of outer membrane proteins of Gram‐negative bacteria as vaccines.