Interactions of the algicidal bacterium Kordia algicida with diatoms: regulated protease excretion for specific algal lysis

PLoS One. 2011;6(6):e21032. doi: 10.1371/journal.pone.0021032. Epub 2011 Jun 17.

Abstract

Interactions of planktonic bacteria with primary producers such as diatoms have great impact on plankton population dynamics. Several studies described the detrimental effect of certain bacteria on diatoms but the biochemical nature and the regulation mechanism involved in the production of the active compounds remained often elusive. Here, we investigated the interactions of the algicidal bacterium Kordia algicida with the marine diatoms Skeletonema costatum, Thalassiosira weissflogii, Phaeodactylum tricornutum, and Chaetoceros didymus. Algicidal activity was only observed towards the first three of the tested diatom species while C. didymus proved to be not susceptible. The cell free filtrate and the >30 kDa fraction of stationary K. algicida cultures is fully active, suggesting a secreted algicidal principle. The active supernatant from bacterial cultures exhibited high protease activity and inhibition experiments proved that these enzymes are involved in the observed algicidal action of the bacteria. Protease mediated interactions are not controlled by the presence of the alga but dependent on the cell density of the K. algicida culture. We show that protease release is triggered by cell free bacterial filtrates suggesting a quorum sensing dependent excretion mechanism of the algicidal protein. The K. algicida / algae interactions in the plankton are thus host specific and under the control of previously unidentified factors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Count
  • Cell-Free System
  • Coculture Techniques
  • Diatoms / growth & development
  • Diatoms / microbiology*
  • Diffusion
  • Filtration
  • Flavobacteriaceae / cytology
  • Flavobacteriaceae / enzymology*
  • Flavobacteriaceae / growth & development
  • Flavobacteriaceae / physiology*
  • Hot Temperature
  • Molecular Weight
  • Peptide Hydrolases / chemistry
  • Peptide Hydrolases / metabolism*
  • Species Specificity

Substances

  • Peptide Hydrolases