Cryo-EM structure of phage Goslar: 2888 protein chains from 28 structural proteins resolved
Researchers built a composite model of the E. coli phage Goslar, a Chimalliviridae member, and found filaments with carbohydrate-binding domains at the baseplate.
A research team determined the structure of Goslar, a bacteriophage of the family Chimalliviridae that infects Escherichia coli, using cryo–electron microscopy, according to a paper in Science Advances. Phages of this family build compartments inside infected bacterial cells that broadly protect their genomes from host defenses science.org
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The authors manually modeled 25 structural proteins and added predicted structures for three more. The composite model contains 2888 protein chains from 28 different structural proteins, with more than 1.4 million amino acid residues in total. It shows the architecture of the capsid, portal, tail and baseplate, with similarities and differences relative to other tailed phages.
The authors combined the structure with quantitative mass spectrometry of virions and identified several high-copy virion-associated proteins that likely play key roles when injected into host cells during infection. They also found a Chimalliviridae-specific protein family that forms long, flexible filaments anchored at the baseplate. These filaments incorporate carbohydrate-binding domains, which, according to the authors, suggests a key role in host recognition.
