Abstract:
:Siphoviridae is the most abundant viral family on earth which infects bacteria as well as archaea. All known siphophages infecting gram+ Lactococcus lactis possess a baseplate at the tip of their tail involved in host recognition and attachment. Here, we report analysis of the p2 phage baseplate structure by X-ray crystallography and electron microscopy and propose a mechanism for the baseplate activation during attachment to the host cell. This approximately 1 MDa, Escherichia coli-expressed baseplate is composed of three protein species, including six trimers of the receptor-binding protein (RBP). RBPs host-recognition domains point upwards, towards the capsid, in agreement with the electron-microscopy map of the free virion. In the presence of Ca(2+), a cation mandatory for infection, the RBPs rotated 200 degrees downwards, presenting their binding sites to the host, and a channel opens at the bottom of the baseplate for DNA passage. These conformational changes reveal a novel siphophage activation and host-recognition mechanism leading ultimately to DNA ejection.
journal_name
Proc Natl Acad Sci U S Aauthors
Sciara G,Bebeacua C,Bron P,Tremblay D,Ortiz-Lombardia M,Lichière J,van Heel M,Campanacci V,Moineau S,Cambillau Cdoi
10.1073/pnas.1000232107subject
Has Abstractpub_date
2010-04-13 00:00:00pages
6852-7issue
15eissn
0027-8424issn
1091-6490pii
1000232107journal_volume
107pub_type
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