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Journal articles
New insights into pb5, the receptor binding protein of bacteriophage T5, and its interaction with its Escherichia coli receptor FhuA
Abstract : The majority of bacterial viruses are bacteriophages bearing a tail that serves to recognise the bacterial surface and deliver the genome into the host cell. Infection is initiated by the irreversible interaction between the viral receptor binding protein (RBP) and a receptor at the surface of the bacterium. This interaction results ultimately in the phage DNA release in the host cytoplasm. Phage T5 infects Escher-ichia coli after binding of its RBP pb5 to the outer membrane ferrichrome transporter FhuA. Here, we have studied the complex formed by pb5 and FhuA by a variety of biophysical and biochemical techniques. We show that unlike RBPs of known structures, pb5 probably folds as a unique domain fulfilling both functions of binding to the host receptor and interaction with the rest of the phage. Pb5 likely binds to the domain occluding the b-barrel of FhuA as well as to external loops of the barrel. Furthermore, upon binding to FhuA, pb5 undergoes conformational changes, at the secondary and tertiary structure level that would be the key to the transmission of the signal through the tail to the capsid, triggering DNA release. This is the first structural information regarding the binding of a RBP to a proteic receptor. Ó 2012 Elsevier Masson SAS. All rights reserved.
Cited literature [43 references]
https://hal-cea.archives-ouvertes.fr/cea-01201918
Contributor : Magali Le Discorde <>
Submitted on : Friday, September 18, 2015 - 12:40:55 PM
Last modification on : Tuesday, October 6, 2020 - 4:12:08 PM
Long-term archiving on: : Tuesday, December 29, 2015 - 8:40:07 AM
Contributor : Magali Le Discorde <>
Submitted on : Friday, September 18, 2015 - 12:40:55 PM
Last modification on : Tuesday, October 6, 2020 - 4:12:08 PM
Long-term archiving on: : Tuesday, December 29, 2015 - 8:40:07 AM
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