Tailspike protein

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== Function ==
== Function ==
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'''Tailspike protein''' (TSP) of bacteriophage P22 is a trimeric protein which serves as the receptor-binding protein of the bacteriophage to its bacterial host<ref>PMID:29500571</ref>. O-antigen polysaccharides found on the outer surface of bacteria are the natural substrates for TSP<ref>PMID:20817910</ref>.
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The '''tailspike protein''' (TSP) of bacteriophage is a trimeric protein which serves as the receptor-binding protein of the bacteriophage to its bacterial host<ref>PMID:29500571</ref>. O-antigen polysaccharides found on the outer surface of bacteria are the natural substrates for TSP<ref>PMID:20817910</ref>.
== Relevance ==
== Relevance ==
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Bacteriophage research is becoming important due to antibiotics resistance. TSP binding to pathogenic bacteria can be used for their detection<ref>PMID:30111705</ref>.
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Bacteriophage research is becoming important due to the problem of antibiotics resistance. TSP binding to pathogenic bacteria can be used for their detection<ref>PMID:30111705</ref>.
== Structural highlights ==
== Structural highlights ==
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The C-terminal domain (CTD) (residues 109-end) of TSP is responsible for the attachment of the tailspike protein to the O-antigen moiety on bacterial cell surface. The 3D structure of an octasaccharide bound to CTP of TSP shows numerous hydrophobic interactions as well as well defined water molecules forming hydrogen bonds to the antigen<ref>PMID:30111705</ref>.
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The C-terminal domain (CTD) (residues 109-end) of TSP is responsible for the attachment of the tailspike protein to the O-antigen moiety on bacterial cell surface. The 3D structure of an octasaccharide bound to CTP of TSP shows numerous hydrophobic interactions as well as well defined water molecules forming hydrogen bonds to the antigen.
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Revision as of 09:18, 11 April 2020

Glycosylated tailspike protein from bacteriophage P222 complex with octasaccharide (PDB code 3th0)

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3D structures of tailspike protein

Updated on 11-April-2020

References

  1. Williams J, Venkatesan K, Ayariga JA, Jackson D, Wu H, Villafane R. A genetic analysis of an important hydrophobic interaction at the P22 tailspike protein N-terminal domain. Arch Virol. 2018 Jun;163(6):1623-1633. doi: 10.1007/s00705-018-3777-y. Epub 2018 , Mar 2. PMID:29500571 doi:http://dx.doi.org/10.1007/s00705-018-3777-y
  2. Andres D, Hanke C, Baxa U, Seul A, Barbirz S, Seckler R. Tailspike interactions with lipopolysaccharide effect DNA ejection from phage P22 particles in vitro. J Biol Chem. 2010 Nov 19;285(47):36768-75. doi: 10.1074/jbc.M110.169003. Epub, 2010 Sep 3. PMID:20817910 doi:http://dx.doi.org/10.1074/jbc.M110.169003
  3. Kunstmann S, Scheidt T, Buchwald S, Helm A, Mulard LA, Fruth A, Barbirz S. Bacteriophage Sf6 Tailspike Protein for Detection of Shigella flexneri Pathogens. Viruses. 2018 Aug 15;10(8). pii: v10080431. doi: 10.3390/v10080431. PMID:30111705 doi:http://dx.doi.org/10.3390/v10080431

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