
A Protein Factor Associated With Serum Resistance in Escherichia Coli
Author(s) -
Peter W. Taylor,
R. Parton
Publication year - 1977
Publication title -
journal of medical microbiology/journal of medical microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.91
H-Index - 117
eISSN - 1473-5644
pISSN - 0022-2615
DOI - 10.1099/00222615-10-2-225
Subject(s) - escherichia coli , strain (injury) , antigen , polyacrylamide gel electrophoresis , gel electrophoresis , sodium , biology , microbiology and biotechnology , sepharose , mutant , chemistry , biochemistry , gene , immunology , enzyme , organic chemistry , anatomy
Immunogel-diffusion studies showed that 60 degree C LiCl extracts of the smooth serum-resistant mutant Escherichia coli strain 17 contained greater amounts of a protein antigen than did extracts of the parent strain LP729. An extract of strain 17 was fractionated on Sepharose 4B and the protein antigen was found as the only detectable antigen in a number of fractions; sodium dodecyl sulphate-polyacrylamide gel electrophoresis indicated that these fractions contained one major polypeptide band with a molecular weight of 46 000 daltons. We suggest that this protein antigen may be partly responsible for the serum resistance of strain 17 though its presence in other serum-sensitive strains suggests that additional factors are essential for full serum resistance.