Investigating the divergence of the major capsid protein within very closely related phage
EMSL Project ID
51282
Abstract
The objective is to begin to understand the evolution of the HK97-like major capsid protein in the closely related actinobacteriophage (viruses that infect the Actinobacteria phylum). It will have wider significance because the same capsid protein-fold is found in viruses that infect all three domains of life and is one of the most common protein folds found in nature.Using phage from the F1 sub-cluster (bacteriophage are grouped/clustered together based on genome nucleotide sequence similarity), I will test the hypothesis that within these very closely related phage there are three major capsid protein structural families, i.e. although their genomes are very similar, there are three distinct capsid morphologies. To test the hypothesis, I am requesting five days of cryo-EM time to obtain seven medium-resolution (4.5-7 angstrom) and three high-resolution (under 4.5 angstrom) structures of the phage capsids using multiplexed cryoEM grids and traditional single sample grids.
The structures will be of bacteriophage within the three F1 sub-cluster structural families, as well as phage capsids that have been identified to be related to the structural families but their genomes are distinct enough put them in other clusters. The medium-resolution maps will provide enough examples to show that the hypothesis is correct or not. Using the high-resolution maps, de novo amino acid sequence modelling will be carried out and the models used to build a phylogenetic tree using the Dali server to measure the major capsid protein divergence to obtain insight into the evolution of the major capsid protein.
Project Details
Start Date
2020-02-15
End Date
2021-03-17
Status
Closed
Released Data Link
Team
Principal Investigator
Team Members