
Antigenic Relationships between Pore Proteins of Escherichia coli K12
Author(s) -
OVERBEEKE Nico,
SCHARRENBURG Guus,
LUGTENBERG Ben
Publication year - 1980
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1980.tb04862.x
Subject(s) - antiserum , bacterial outer membrane , escherichia coli , proteus mirabilis , enterobacter aerogenes , porin , microbiology and biotechnology , biology , membrane protein , lipopolysaccharide , antigen , biochemistry , membrane , gene , endocrinology , genetics
Antisera were raised against the purified Escherichia coli K12 outer membrane proteins ompA‐, ompC‐ and ompF proteins and protein e. Several immunological methods were used to investigate the specificity of the antisera and the immunological relationship between the major outer membrane proteins. Although the antisera had been raised against highly purified proteins, several of them contained activity against lipopolysaccharide and lipoprotein due to minor impurities in the immunogens. The three general porins ompF protein, ompC protein and protein e were shown to be cross‐reactive. Anti‐( ompA protein) serum only reacted with the homologous protein. None of these antisera reacted with the phage lambda receptor protein or with protein III. Pore protein preparations isolated from Salmonella typhimurium, Klebsiella aerogenes, Enterobacter cloaceae and Proteus mirabilis were found to be structurally related to the E. coli K12 porins as they reacted with the antisera raised against E. coli K12 porins.