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Assembly proteins of CS1 pili of enterotoxigenic Escherichia coli
Author(s) -
Sakellaris Harry,
Balding Donna P.,
Scott June R.
Publication year - 1996
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1996.tb02562.x
Subject(s) - pilus , pilin , periplasmic space , biology , protein subunit , bacterial outer membrane , fimbriae proteins , escherichia coli , microbiology and biotechnology , biochemistry , gene
Summary Some strains of enterotoxigenic Escherichia coli associated with human diarrhoeal disease produce a class of pili represented by those called CS1. For the assembly of the major‐pilin subunit, CooA, into pili, each of four linked genes, cooB,A,C , and D , is required. In this study, we have determined the subcellular localization of CooB, C and D, and investigated the molecular interactions of these proteins using specific antisera. CooD appears to be an integral pilus protein because it co‐purifies with, and is strongly associated with, CS1 pili. In keeping with its role as an assembly protein, the CooD minor pilin (when overexpressed in CS1‐piliated strains) was detected in periplasmic inter‐molecular complexes with the major‐pilin subunit CooA. CooB is an assembly protein found exclusively in the periplasm of CS1‐piliated strains. CooB also forms periplasmic intermolecular complexes with CooA, but does not constitute part of the final pilus structure. Immunoblot analysis of cell fractions showed that CooC is an outer membrane protein of CS1‐piliated E. coli. Based on this information, we have proposed a model for CS1 ‐pilus assembly which is very similar to the model for polymerization of the PapA pilin of uropathogenic E. coli. As the assembly proteins of Pap and CS1 pili are structurally unrelated, this may represent a case of convergent evolution.