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Related Experiment Videos

Cell surface-associated enolase in Actinobacillus actinomycetemcomitans.

H Hara1, H Ohta, T Inoue

  • 1Department of Periodontology and Endontology, Okayama University Dental School, Japan.

Microbiology and Immunology
|July 11, 2000
PubMed
Summary

Actinobacillus actinomycetemcomitans releases enolase to its cell surface. This study identified enolase in extracellular extracts, suggesting its external localization in this bacterium.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Actinobacillus actinomycetemcomitans is a bacterium associated with periodontal disease.
  • The localization of bacterial enzymes can influence their function and interaction with the host.

Purpose of the Study:

  • To investigate the presence and localization of cell surface-associated proteins in Actinobacillus actinomycetemcomitans.
  • To determine if enolase, a glycolytic enzyme, is present on the bacterial cell surface or released extracellularly.

Main Methods:

  • Extraction of cell surface-associated materials using Tris-buffered saline with and without the restriction enzyme EcoRI.
  • Analysis of extracted proteins using N-terminal sequencing.
  • Enzyme activity assays for enolase and lactate dehydrogenase in the extracts.

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Main Results:

  • Four major proteins were identified in the extracts, including outer membrane proteins, a GroEL-like protein, and a protein homologous to Haemophilus influenzae enolase.
  • Enolase activity was detected in the extracts, with a significant relative amount in the EcoRI extract during the mid-exponential growth phase.
  • Lactate dehydrogenase, a cytosolic enzyme, showed very low activity in the extracts and supernatant.

Conclusions:

  • The findings suggest that enolase is localized on the external surface of Actinobacillus actinomycetemcomitans.
  • The extracellular presence of enolase may play a role in the bacterium's interaction with the host environment.