The CS2 fimbrial antigen fromescherichia coli, purification, characterization and partial covalent structure

作者：Per Klemm, Wim Gaastra, Moyra M. McConnell, Henry R. Smith · 发表于：FEMS Microbiology Letters · 年份：1985 · DOI：10.1111/j.1574-6968.1985.tb01592.x · 被引用次数：26 · 研究领域：Bacteriophages and microbial interactions、Bacterial Genetics and Biotechnology、Protein purification and stability

The CS2 fimbrial antigen was isolated by salt and isoelectric precipitation and by column chromatography. The purified antigen was free of other fimbrial proteins present on the same bacterial strain. Analysis of the N-terminal amino acid sequence indicated extensive homology with the CFA1 fimbrial antigen, which was surprising since the two proteins do not show any immunological cross reactivity. It could therefore be concluded that the N-terminal parts of these fimbrial proteins are not located on the surfaces of the proteins and might be involved in conservation of the structural integrity of these proteins.