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A novel stabilization mechanism accommodating genome length variation in evolutionarily related viral capsids

biorxiv. 2023-11; 
Jennifer M Podgorski, Joshua Podgorski, Lawrence Abad, Deborah Jacobs-Sera, Krista G Freeman, Colin Brown, Graham Hatfull, Antoni Luque, Simon J White
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Proteins, Expression, Isolation and Analysis … coli protein expression and synthesized by GenScript, USA before being cloned into the pETDuet-1 vector. The protein was produced in NEBExpress Competent E. coli High Efficiency … Get A Quote

摘要

Tailed bacteriophages are one of the most numerous and diverse group of viruses. They store their genome at quasi-crystalline densities in capsids built from multiple copies of proteins adopting the HK97-fold. The high density of the genome exerts an internal pressure, requiring a maturation process that reinforces their capsids. However, it is unclear how capsid stabilization strategies have adapted to accommodate the evolution of larger genomes in this virus group. Here we characterized a novel capsid reinforcement mechanism in two evolutionary-related actinobacteriophages that modifies the length of a stabilization protein to accommodate a larger genome while maintaining the same capsid size. We used cryo-EM... More

關(guān)鍵詞

Accessory protein, Bacteriophage, Capsid stability, HK97-fold
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