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Lysogenic Cycle of Bacteriophages00:43

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In contrast to the lytic cycle, phages infecting bacteria via the lysogenic cycle do not immediately kill their host cell. Instead, they combine their genome with the host genome, allowing the bacteria to replicate the phage DNA along with the bacterial genome. The incorporated copy of the phage genome is called the prophage. Some prophages can re-activate and enter the lytic cycle. This often occurs in response to a perturbation, such as DNA damage, but can also transpire in the absence of...
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Bacteriophages, also known as phages, are specialized viruses that infect bacteria. A key characteristic of phages is their distinctive “head-tail” morphology. A phage begins the infection process (i.e., lytic cycle) by attaching to the outside of a bacterial cell. Attachment is accomplished via proteins in the phage tail that bind to specific receptor proteins on the outer surface of the bacterium. The tail injects the phage’s DNA genome into the bacterial cytoplasm. In the...
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Updated: Jun 30, 2025

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
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Fermentation Practices Select for Thermostable Endolysins in Phages.

Frank Oechslin1,2,3, Xiaojun Zhu1,2, Carlee Morency1,2,3

  • 1Département de biochimie, de microbiologie, et de bio-informatique, Faculté des sciences et de génie, Université Laval, Québec City, Canada.

Molecular Biology and Evolution
|March 15, 2024
PubMed
Summary
This summary is machine-generated.

Bacteriophage endolysins targeting Streptococcus thermophilus show limited diversity. A novel calcium-binding motif enhances enzyme stability and activity, indicating positive selection in dairy fermentation environments.

Keywords:
Streptococcus thermophilusbacteriophagesdairy fermentationendolysinsexperimental evolutionhost adaptation

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Area of Science:

  • Microbiology
  • Enzymology
  • Evolutionary Biology

Background:

  • Bacteriophage endolysins are crucial for bacterial cell wall lysis and phage release.
  • Endolysins display diverse modular structures, but evolutionary drivers remain unclear.
  • Streptococcus thermophilus, a dairy fermenter, offers a focused ecological niche to study endolysin evolution.

Purpose of the Study:

  • Investigate the diversity and evolution of endolysins from phages infecting Streptococcus thermophilus.
  • Identify structural features of S. thermophilus endolysins and their functional significance.
  • Determine if endolysin evolution is influenced by the specific environmental conditions of dairy fermentation.

Main Methods:

  • Bioinformatic analysis of endolysins from S. thermophilus phages.
  • Structural and functional characterization of identified endolysins.
  • Enzyme activity assays at varying temperatures and calcium concentrations.
  • Analysis of positive selection pressures on endolysin motifs.

Main Results:

  • Observed limited endolysin diversity in S. thermophilus phages, with a dominant structural type.
  • Discovered a novel, conserved calcium-binding motif within the prevalent endolysin structure.
  • This motif significantly enhanced enzyme stability and activity at elevated temperatures.
  • Demonstrated positive selection for this motif under conditions mimicking dairy fermentation.

Conclusions:

  • Endolysin evolution in S. thermophilus is constrained, favoring a specific structural type adapted to dairy environments.
  • The identified calcium-binding motif is a key adaptation for endolysin function in high-temperature fermentation.
  • This finding highlights the role of ecological niche and environmental factors in shaping phage-encoded enzyme evolution.