期刊
SCIENCE ADVANCES
卷 8, 期 48, 页码 -出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.ade0459
关键词
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资金
- National Institutes of Health (NIH) [R21 AI156636]
- NIH
- [U24 GM116789]
In this study, the structure of the complete virion of the Staphylococcus epidermidis-infecting phage Andhra was determined using high-resolution cryo-electron microscopy. The findings provide insights into critical features for virion assembly, host recognition, and penetration.
Staphylococcus epidermidis is an opportunistic pathogen of the human skin, often associated with infections of implanted medical devices. Staphylococcal picoviruses are a group of strictly lytic, short-tailed bacteriophages with compact genomes that are attractive candidates for therapeutic use. Here, we report the structure of the complete virion of S. epidermidis-infecting phage Andhra, determined using high-resolution cryo-electron micros-copy, allowing atomic modeling of 11 capsid and tail proteins. The capsid is a T = 4 icosahedron containing a unique stabilizing capsid lining protein. The tail includes 12 trimers of a unique receptor binding protein (RBP), a lytic protein that also serves to anchor the RBPs to the tail stem, and a hexameric tail knob that acts as a gate-keeper for DNA ejection. Using structure prediction with AlphaFold, we identified the two proteins that comprise the tail tip heterooctamer. Our findings elucidate critical features for virion assembly, host recognition, and penetration.
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