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Viral Structure00:56

Viral Structure

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Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.
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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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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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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...
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Bacteria and archaea are susceptible to viral infections just like eukaryotes; therefore, they have developed a unique adaptive immune system to protect themselves. Clustered regularly interspaced short palindromic repeats and CRISPR-associated proteins (CRISPR-Cas) are present in more than 45% of known bacteria and 90% of known archaea.
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CRISPR stands for Clustered Regularly Interspaced Short Palindromic Repeats is a adaptive immune system found in bacteria and archaea that protects against viral infections. This system enables prokaryotic cells to identify, remember, and neutralize foreign genetic elements, primarily bacteriophages, by storing fragments of the invader’s DNA as a genetic memory.The CRISPR immune response begins during an initial infection. Cas (CRISPR-associated) proteins play a central role in this...
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Phage Phenomics: Physiological Approaches to Characterize Novel Viral Proteins
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Mapping Structural Constraints and Adaptive Potential in a Capsule-Degrading Phage Tailspike Protein.

Sarah Evert1,2, Phill Huss1, Dinesh Kumar Kuppa Baskaran3,4

  • 1Department of Biochemistry, University of Wisconsin-Madison, Madison, WI, USA.

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Deep mutational scanning of bacteriophage tailspike proteins (TSPs) reveals how mutations alter function and host range. This research provides a strategy for engineering phages to combat bacterial capsule defenses.

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Area of Science:

  • Microbiology
  • Structural Biology
  • Molecular Biology

Background:

  • Bacteriophage tailspike proteins (TSPs) are crucial for degrading bacterial capsules during infection.
  • Understanding the molecular basis of TSP function and host specificity is essential for phage therapy development.
  • The host range of bacteriophages is often limited by bacterial capsule structures.

Purpose of the Study:

  • To investigate the functional and adaptive landscape of a specific bacteriophage tailspike protein (TSP) from *Escherichia coli* K1 phage K1F.
  • To identify key residues and structural elements that determine TSP enzymatic activity, processivity, and host specificity.
  • To provide insights for designing bacteriophages capable of overcoming capsule-mediated bacterial resistance.

Main Methods:

  • Deep mutational scanning (DMS) was employed on the endosialidase TSP of *Escherichia coli* K1 phage K1F.
  • An enhanced ORACLE phage engineering platform was utilized to generate over 22,000 single-amino-acid variants.
  • Functional activity, processivity, and host specificity were assessed across engineered TSP variants through comparative selections.

Main Results:

  • The TSP was found to be structurally fragile but possessed adaptive flexibility, with specific mutations impacting function.
  • Mutations in the active site accommodated longer sialic acid chains, expanding substrate recognition.
  • The TSP stalk acted as a "tuning knob" for processivity and specificity, while other regions modulated host range by interacting with capsule modifications and O-antigens.

Conclusions:

  • Specific mutations in bacteriophage TSPs can significantly modulate their enzymatic activity, substrate specificity, and host range.
  • The study elucidates the structure-function relationships of TSPs, highlighting the stalk and distal regions as key modulators of host interaction.
  • These findings offer a framework for rationally designing bacteriophages to overcome bacterial capsule defenses and enhance therapeutic efficacy.