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Published on: March 11, 2022
Distantly related Alteromonas bacteriophages share tail fibers exhibiting properties of transient chaperone caps
Rafael Gonzalez-Serrano1,2, Riccardo Rosselli3,4, Juan J Roda-Garcia1
1Evolutionary Genomics Group, Universidad Miguel Hernández, San Juan de Alicante, Spain.
Abstract:
The host recognition modules encoding the injection machinery and receptor binding proteins (RBPs) of bacteriophages are predisposed to mutation and recombination to maintain infectivity towards co-evolving bacterial hosts. In this study, we reveal how Alteromonas mediterranea schitovirus A5 shares its host recognition module, including tail fiber and cognate chaperone, with phages from distantly related families including Alteromonas myovirus V22. While the V22 chaperone is essential for producing active tail fibers, here we demonstrate production of functional A5 tail fibers regardless of chaperone co-expression. AlphaFold-generated models of tail fiber and chaperone pairs from phages A5, V22, and other Alteromonas phages reveal how amino acid insertions within both A5-like proteins results in a knob domain duplication in the tail fiber and a chaperone β-hairpin "tentacle" extension. These structural modifications are linked to differences in chaperone dependency between the A5 and V22 tail fibers. Structural similarity between the chaperones and intramolecular chaperone domains of other phage RBPs suggests an additional function of these chaperones as transient fiber "caps". Finally, our identification of homologous host recognition modules from morphologically distinct phages implies that horizontal gene transfer and recombination events between unrelated phages may be a more common process than previously thought among Caudoviricetes phages.
Insights
Bacteriophages share host recognition modules, like tail fibers, even between distant relatives. Structural changes explain differences in chaperone dependency and suggest broader horizontal gene transfer among phages.
Area of Science:
- Microbiology
- Virology
- Structural Biology
Background:
- Bacteriophage host recognition modules, including receptor binding proteins (RBPs), evolve rapidly through mutation and recombination to overcome bacterial host defenses.
- These modules are crucial for phage infectivity and are often shared among related phages.
Purpose of the Study:
- To investigate the structural basis and evolutionary implications of host recognition module sharing between distantly related bacteriophages.
- To understand the role of chaperones in the assembly and function of bacteriophage tail fibers.
Main Methods:
- Comparative analysis of host recognition modules from Alteromonas mediterranea schitovirus A5 and Alteromonas myovirus V22.
- AlphaFold modeling to predict the structures of tail fiber and chaperone pairs.
- Functional assays to assess tail fiber production and activity.
Main Results:
- Alteromonas mediterranea schitovirus A5 shares its host recognition module with distantly related phages like Alteromonas myovirus V22.
- Functional A5 tail fibers can be produced independently of chaperone co-expression, unlike V22 tail fibers.
- AlphaFold models reveal structural modifications, including knob domain duplication and chaperone β-hairpin extensions, linked to differential chaperone dependency.
- Chaperones may also function as transient tail fiber caps.
Conclusions:
- Horizontal gene transfer and recombination are likely more prevalent among Caudoviricetes phages than previously assumed.
- Structural variations in host recognition modules contribute to diverse phage-host interactions and evolutionary strategies.
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