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JB Accepts, published online ahead of print on 14 November 2008
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J. Bacteriol. doi:10.1128/JB.01423-08
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

The tail sheath of bacteriophage N4 interacts with the E. coli receptor

Jennifer McPartland and Lucia B. Rothman-Denes*

Committee on Microbiology, and Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, Illinois, 60637

* To whom correspondence should be addressed. Email: lbrd{at}uchicago.edu.


  Abstract

Unlike other characterized phages, lytic coliphage N4 must inject into the host the 360 kDa virion RNA polymerase (vRNAP) in addition to its 72 kbp genome, for successful infection. The process of adsorption to the host sets-up and elicits the necessary conformational changes in the virion to allow genome and vRNAP injection. Infection of suppressor and non-suppressor strains, E. coli W3350supF and E. coli W3350, with mutant N4 isolate (N4am229) harboring an amber mutation in ORF65 yielded virions containing (N4gp65+) and lacking gp65 (N4gp65-), respectively. N4gp65+ but not N4gp65- phage was able to adsorb to the host. Recombinant gp65 hexahistidine-tagged at the N-terminus or hexahistidine and c-myc tagged at the C-terminus was able to complement N4gp65- virions in vivo and in vitro. Immunogold detection of gp65 in vivo complemented virions revealed its localization at the N4 tail. Finally, we show both in vitro and in vivo that gp65 interacts with the previously determined N4 outer membrane receptor, NfrA.






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