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TitleStructure and Function of Hoc-A Novel Environment Sensing Device Encoded by T4 and Other Bacteriophages.
Journal, issue, pagesViruses, Vol. 15, Issue 7, Year 2023
Publish dateJul 7, 2023
AuthorsAndrei Fokine / Mohammad Zahidul Islam / Qianglin Fang / Zhenguo Chen / Lei Sun / Venigalla B Rao /
PubMed AbstractBacteriophage T4 is decorated with 155 180 Å-long fibers of the highly antigenic outer capsid protein (Hoc). In this study, we describe a near-atomic structural model of Hoc by combining cryo- ...Bacteriophage T4 is decorated with 155 180 Å-long fibers of the highly antigenic outer capsid protein (Hoc). In this study, we describe a near-atomic structural model of Hoc by combining cryo-electron microscopy and AlphaFold structure predictions. It consists of a conserved C-terminal capsid-binding domain attached to a string of three variable immunoglobulin (Ig)-like domains, an architecture well-preserved in hundreds of Hoc molecules found in phage genomes. Each T4-Hoc fiber attaches randomly to the center of gp23* hexameric capsomers in one of the six possible orientations, though at the vertex-proximal hexamers that deviate from 6-fold symmetry, Hoc binds in two preferred orientations related by 180° rotation. Remarkably, each Hoc fiber binds to all six subunits of the capsomer, though the interactions are greatest with three of the subunits, resulting in the off-centered attachment of the C-domain. Biochemical analyses suggest that the acidic Hoc fiber (pI, ~4-5) allows for the clustering of virions in acidic pH and dispersion in neutral/alkaline pH. Hoc appears to have evolved as a sensing device that allows the phage to navigate its movements through reversible clustering-dispersion transitions so that it reaches its destination, the host bacterium, and persists in various ecological niches such as the human/mammalian gut.
External linksViruses / PubMed:37515203 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 3.4 Å
Structure data

PDB-8t1x:
T4 highly immunogenic outer capsid protein C-terminal domain bound to the vertex-proximal gp23* capsomer of the isometric head in two preferred orientations
Method: ELECTRON MICROSCOPY / Resolution: 3.3 Å

PDB-8t9r:
T4 highly immunogenic outer capsid protein C-terminal domain bound to a vertex-proximal gp23* capsomer of the prolate capsid in two preferred orientations.
Method: ELECTRON MICROSCOPY / Resolution: 3.4 Å

Source
  • escherichia phage t4 (virus)
KeywordsVIRAL PROTEIN / bacteriophage / capsid / T4 head / Hoc / highly immunogenic outer capsid protein / virus decoration protein / immunoglobulin-like domains / antigen display / vaccine

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