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DNA Bacteriophages01:26

DNA Bacteriophages

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Bacteriophages, or phages, are viruses that specifically infect bacteria, utilizing their genetic material to hijack host cellular machinery for replication. DNA bacteriophages employ single-stranded DNA (ssDNA) or double-stranded DNA (dsDNA) genomes. These phages exhibit diverse replication strategies and host interactions, influencing their ecological roles and applications in biotechnology and medicine.ssDNA BacteriophagesssDNA phages, with their small genomes, utilize unique strategies to...
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Lytic Cycle of Bacteriophages01:30

Lytic Cycle of Bacteriophages

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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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Viral Replication: Lytic Cycle01:20

Viral Replication: Lytic Cycle

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Bacteriophages, or phages, are viruses that specifically infect bacteria. Among them, T-even bacteriophages, such as T4, exhibit a well-characterized lytic replication cycle in Escherichia coli (E. coli). This process ensures the rapid proliferation of the virus while ultimately leading to the destruction of the bacterial host.Attachment and DNA InjectionThe infection process begins with the recognition and binding of the T4 phage to the E. coli cell surface. Tail fibers of the phage...
1.0K
Translesion DNA Polymerases02:10

Translesion DNA Polymerases

10.9K
Translesion (TLS) polymerases rescue stalled DNA polymerases at sites of damaged bases by replacing the replicative polymerase and installing a nucleotide across the damaged site. Doing so, TLS allows additional time for the cell to repair the damage before resuming regular DNA replication.
TLS polymerases are found in all three domains of life - archaea, bacteria, and eukaryotes. Of the different classes of TLS polymerases, members of the Y family are fitted with specialized structures that...
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Proofreading01:31

Proofreading

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Synthesis of new DNA molecules is carried out by the enzyme DNA polymerase, which adds nucleotides on the daughter strand complementary to the template DNA strand. DNA polymerase has a higher affinity to add the correct base and ensures fidelity during DNA replication. Furthermore,  it exhibits proofreading activity during replication, using an exonuclease domain that cuts off incorrect nucleotides from the nascent DNA strand.
Errors During Replication are Corrected by the DNA Polymerase...
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Proofreading01:43

Proofreading

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Overview
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Updated: Dec 29, 2025

Phage Phenomics: Physiological Approaches to Characterize Novel Viral Proteins
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Phage Phenomics: Physiological Approaches to Characterize Novel Viral Proteins

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Diversity and Function of Phage Encoded Depolymerases.

Leandra E Knecht1, Marjan Veljkovic1, Lars Fieseler1

  • 1Institute of Food and Beverage Innovation, Zurich University of Applied Sciences, Wädenswil, Switzerland.

Frontiers in Microbiology
|January 31, 2020
PubMed
Summary

Bacteriophage depolymerases, often tail spike proteins (TSPs), degrade bacterial polysaccharides like CPS, EPS, and LPS. This review summarizes their diversity, function, and biotechnological applications.

Keywords:
bacteriophagecapsuledepolymeraselipopolysaccharidepolysaccharide

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Area of Science:

  • Microbiology
  • Biochemistry
  • Molecular Biology

Background:

  • Bacteriophages, viruses that infect bacteria, frequently possess depolymerase enzymes.
  • These enzymes, often tail spike proteins (TSPs), are crucial for phage infection by degrading bacterial surface polysaccharides.
  • Depolymerases are found in various phage families, including Podoviridae, Ackermannviridae, Myoviridae, and Siphoviridae.

Purpose of the Study:

  • To review the diversity and function of depolymerases encoded by bacteriophages.
  • To explore the substrate specificity of these enzymes against capsular polysaccharides (CPS), exopolysaccharides (EPS), and lipopolysaccharides (LPS).
  • To highlight potential applications of phage-encoded depolymerases in biotechnology.

Main Methods:

  • Literature review of scientific publications on bacteriophage depolymerases.
  • Analysis of enzyme structure-function relationships.
  • Summary of reported substrate specificities and biotechnological uses.

Main Results:

  • Phage depolymerases exhibit diverse structures and functions.
  • These enzymes specifically cleave polysaccharide-repeating units of bacterial CPS, EPS, and LPS.
  • Depolymerases play a vital role in enabling bacteriophages to reach and infect host cells.

Conclusions:

  • Bacteriophage depolymerases are versatile enzymes with significant biotechnological potential.
  • Understanding their substrate specificity is key to unlocking applications in areas like antimicrobial therapy and food safety.
  • Further research into these enzymes can lead to novel biotechnological tools.