@article{Hawkins:2021:10.1038/s41467-021-26759-x,
author = {Hawkins, NC and Kizziah, JL and Penades, JR and Dokland, T},
doi = {10.1038/s41467-021-26759-x},
journal = {Nature Communications},
title = {Shape shifter: redirection of prolate phage capsid assembly by staphylococcal pathogenicity islands},
url = {http://dx.doi.org/10.1038/s41467-021-26759-x},
volume = {12},
year = {2021}
}

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TY  - JOUR
AB  - Staphylococcus aureus pathogenicity islands (SaPIs) are molecular parasites that hijack helper phages for their transfer. SaPIbov5, the prototypical member of a family of cos type SaPIs, redirects the assembly of 12 helper capsids from prolate to isometric. This size and shape shift is dependent on the SaPIbov5-encoded protein Ccm, a homolog of the 12 capsid protein (CP). Using cryo-electron microscopy, we have determined structures of prolate 12 procapsids and isometric SaPIbov5 procapsids. 12 procapsids have icosahedral end caps with Tend = 4 architecture and a Tmid = 14 cylindrical midsection, whereas SaPIbov5 procapsids have T = 4 icosahedral architecture. We built atomic models for CP and Ccm, and show that Ccm occupies the pentameric capsomers in the isometric SaPIbov5 procapsids, suggesting that preferential incorporation of Ccm pentamers prevents the cylindrical midsection from forming. Our results highlight that pirate elements have evolved diverse mechanisms to suppress phage multiplication, including the acquisition of phage capsid protein homologs.
AU  - Hawkins,NC
AU  - Kizziah,JL
AU  - Penades,JR
AU  - Dokland,T
DO  - 10.1038/s41467-021-26759-x
PY  - 2021///
SN  - 2041-1723
TI  - Shape shifter: redirection of prolate phage capsid assembly by staphylococcal pathogenicity islands
T2  - Nature Communications
UR  - http://dx.doi.org/10.1038/s41467-021-26759-x
UR  - https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000714754400034&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=a2bf6146997ec60c407a63945d4e92bb
UR  - https://www.nature.com/articles/s41467-021-26759-x
UR  - http://hdl.handle.net/10044/1/112598
VL  - 12
ER  - 

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