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The role of the chaperone CooB in the folding of the CS1 pilus subunit CooA from enterotoxigenic Escherichia coli
Loh, Pui Yen
Loh, Pui Yen
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2024-07
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CS1 pili from enterotoxigenic Escherichia coli (ETEC) play an essential role in colonizing host intestinal tissue, leading to severe diarrheal disease. CS1 (coli surface antigen 1) pili are a representative class of pili formed using the alternate chaperone-usher pathway for pilus assembly. For CS1, the assembly of the subunits CooA and the tip CooD requires the chaperone CooB and the outer membrane usher CooC. Despite having little sequence homology, CooB is thought to assist in folding the subunits similarly to known chaperones, such as PapD (for P pili) and FimC (for type I pili), which have been shown to catalyze the folding of pilus subunits. To confirm that CooB functions as a chaperone or catalyst, we monitored the folding of CooA in the presence and absence of CooB. To do this, we generated a mutant of CooA (F84W) and a mutant of CooB (W71F) that allowed us to monitor solely the tryptophan fluorescence of F84WCooA, even in the presence of W71FCooB. The kinetic results indicated that the rate of F84WCooA folding did not increase with W71FCooB concentration, suggesting that W71FCooB acts as a classical chaperone by preventing nonspecific aggregation. Consequently, CooB does not function similarly to PapD and FimC in facilitating the folding of subunits and may represent a form of convergent evolution in how pilus subunits can be assembled.
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Thesis (M.S.)-- Wichita State University, College of Liberal Arts and Sciences, Dept. of Chemistry and Biochemistry
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Wichita State University
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