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Proteases influence colony aggregation behavior in Vibrio cholerae.

Tyler C Detomasi1, Allison E Batka2, Julie S Valastyan3

  • 1Department of Chemistry, University of California, Berkeley, Berkeley, California, USA; Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, California, USA.

The Journal of Biological Chemistry
|October 28, 2023
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Summary
This summary is machine-generated.

Two proteases, LapX and Lap, are crucial for Vibrio cholerae aggregation. LapX activates Lap, which then facilitates bacterial aggregation, enhancing survival in harsh environments.

Keywords:
Vibrio choleraeaggregationbiofilmproteolysis

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Area of Science:

  • Microbiology
  • Enzymology
  • Bacterial Physiology

Background:

  • Bacterial aggregation is a survival mechanism against environmental stress.
  • The proteases LapX and Lap play a role in Vibrio cholerae liquid-based aggregation.

Purpose of the Study:

  • To characterize the enzymatic activity and function of LapX and Lap in Vibrio cholerae.
  • To elucidate the sequential mechanism by which LapX and Lap regulate bacterial aggregation.

Main Methods:

  • Enzymatic assays to determine protease activity and substrate specificity.
  • Mass spectrometry-based substrate profiling.
  • Biochemical characterization of LapX and Lap.
  • Complementation assays in a V. cholerae mutant lacking lapX and lap genes.

Main Results:

  • LapX is identified as a serine protease with specific cleavage preferences.
  • Lap is characterized as an aminopeptidase whose activity is enhanced by LapX processing.
  • LapX sequentially processes Lap, amplifying its activity and restoring V. cholerae aggregation timing in a mutant.

Conclusions:

  • LapX and Lap function sequentially to regulate Vibrio cholerae aggregation.
  • This protease cascade is essential for the bacterial aggregation program and survival.
  • Understanding these proteases offers insights into bacterial social behavior and virulence.