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Home / Equine Research Bank / Mol Microbiol / Function of bacteriophage G7C esterase tailspike in host cel...
Molecular microbiology2017; 105(3); 385-398; doi: 10.1111/mmi.13710

Function of bacteriophage G7C esterase tailspike in host cell adsorption.

Abstract: Bacteriophages recognize and bind to their hosts with the help of receptor-binding proteins (RBPs) that emanate from the phage particle in the form of fibers or tailspikes. RBPs show a great variability in their shapes, sizes, and location on the particle. Some RBPs are known to depolymerize surface polysaccharides of the host while others show no enzymatic activity. Here we report that both RBPs of podovirus G7C - tailspikes gp63.1 and gp66 - are essential for infection of its natural host bacterium E. coli 4s that populates the equine intestinal tract. We characterize the structure and function of gp63.1 and show that unlike any previously described RPB, gp63.1 deacetylates surface polysaccharides of E. coli 4s leaving the backbone of the polysaccharide intact. We demonstrate that gp63.1 and gp66 form a stable complex, in which the N-terminal part of gp66 serves as an attachment site for gp63.1 and anchors the gp63.1-gp66 complex to the G7C tail. The esterase domain of gp63.1 as well as domains mediating the gp63.1-gp66 interaction is widespread among all three families of tailed bacteriophages.
© 2017 John Wiley & Sons Ltd.
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Publication Date: 2017-06-19 PubMed ID: 28513100DOI: 10.1111/mmi.13710Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research explores how the bacteriophage G7C uses its receptor-binding proteins (RBPs) to bind to and infect its host bacterium E. coli 4s, a typical inhabitant of the equine intestinal tract. The study uncovers a previously unknown function of RBP gp63.1, which alters surface polysaccharides of E. coli 4s without destroying the backbone of the polysaccharide.

Receptor-Binding Proteins (RBPs) and Bacteriophage G7C

  • Bacteriophages are viruses that infect bacteria. They use receptor-binding proteins (RBPs) to recognize and bind to their host bacteria.
  • RBP structures can vary significantly in shape, size, and location on the bacteriophage.
  • The bacteriophage G7C, the focus of this research, uses two RBPs known as tailspikes gp63.1 and gp66 to bind to its host, the bacterium E. coli 4s.

New Role of RBP gp63.1

  • The study reveals that RBP gp63.1 has a unique function not previously observed in any other RBP. Instead of merely binding to the host bacterium, gp63.1 alters the composition of E. coli 4s surface polysaccharides.
  • Rather than depolymerizing, or breaking down, the polysaccharide, gp63.1 deacetylates it, a process which removes acetyl groups but leaves the polysaccharide backbone intact.

RBP Complex gp63.1-gp66

  • The gp63.1 RBP does not function in isolation. It forms a stable complex with the other RBP, gp66.
  • The complex is anchored to the G7C tail through the N-terminal part of gp66, which serves as the attachment site for gp63.1.

Broad Presence of Esterase Domain and RBP Interactions

  • The research also discovered that the esterase domain of gp63.1, associated with the deacetylation process, is widespread among all three families of tailed bacteriophages.
  • Similarly, the domains mediating the gp63.1-gp66 interaction, essential for the formation of the complex, are also prevalent among these bacteriophages.

Cite This Article

APA
Prokhorov NS, Riccio C, Zdorovenko EL, Shneider MM, Browning C, Knirel YA, Leiman PG, Letarov AV. (2017). Function of bacteriophage G7C esterase tailspike in host cell adsorption. Mol Microbiol, 105(3), 385-398. https://doi.org/10.1111/mmi.13710

Publication

Molecular microbiology
ISSN: 1365-2958
NlmUniqueID: 8712028
Country: England
Language: English
Volume: 105
Issue: 3
Pages: 385-398

Researcher Affiliations

Prokhorov, Nikolai S
  • Research Center of Biotechnology, Russian Academy of Sciences, Winogradsky Institute of Microbiology, 7b2 pr. 60-letiya Oktyabrya, Moscow, 117312, Russia.
Riccio, Cristian
  • École Polytechnique Fédérale de Lausanne (EPFL), BSP-415, Lausanne, 1015, Switzerland.
Zdorovenko, Evelina L
  • Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, 47 Leninsky pr, Moscow, 119991, Russia.
Shneider, Mikhail M
  • École Polytechnique Fédérale de Lausanne (EPFL), BSP-415, Lausanne, 1015, Switzerland.
  • Laboratory of Molecular Bioengineering, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, 16/10 Miklukho-Maklaya St, Moscow, 117997, Russia.
Browning, Christopher
  • École Polytechnique Fédérale de Lausanne (EPFL), BSP-415, Lausanne, 1015, Switzerland.
Knirel, Yuriy A
  • Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, 47 Leninsky pr, Moscow, 119991, Russia.
Leiman, Petr G
  • École Polytechnique Fédérale de Lausanne (EPFL), BSP-415, Lausanne, 1015, Switzerland.
Letarov, Andrey V
  • Research Center of Biotechnology, Russian Academy of Sciences, Winogradsky Institute of Microbiology, 7b2 pr. 60-letiya Oktyabrya, Moscow, 117312, Russia.
  • Faculty of Biology, Lomonosov Moscow State University, 1-12 Leninskie Gory, Moscow, 119991, Russia.

MeSH Terms

  • Adsorption / physiology
  • Animals
  • Bacteriophage P22 / chemistry
  • Bacteriophage P22 / physiology
  • Bacteriophages / physiology
  • Crystallography, X-Ray
  • Escherichia coli / metabolism
  • Esterases / genetics
  • Esterases / metabolism
  • Horses / microbiology
  • Models, Molecular
  • Polysaccharides, Bacterial / metabolism
  • Protein Binding
  • Protein Conformation
  • Viral Tail Proteins / metabolism

Citations

This article has been cited 40 times.
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