This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by McPartland, J.
Right arrow Articles by Rothman-Denes, L. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by McPartland, J.
Right arrow Articles by Rothman-Denes, L. B.

 Previous Article  |  Next Article 

Journal of Bacteriology, January 2009, p. 525-532, Vol. 191, No. 2
0021-9193/09/$08.00+0     doi:10.1128/JB.01423-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

The Tail Sheath of Bacteriophage N4 Interacts with the Escherichia coli Receptor {triangledown}

Jennifer McPartland1 and Lucia B. Rothman-Denes1,2*

Committee on Microbiology,1 Department of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, Illinois 606372

Received 9 October 2008/ Accepted 3 November 2008

Unlike other characterized phages, the lytic coliphage N4 must inject the 360-kDa virion RNA polymerase (vRNAP), in addition to its 72-kbp genome, into the host 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 nonsuppressor strains, Escherichia coli W3350 supF and E. coli W3350, with a mutant N4 isolate (N4am229) harboring an amber mutation in Orf65 yielded virions containing (N4gp65+) and lacking (N4gp65) gp65, respectively. N4gp65+ but not N4gp65 phage was able to adsorb to the host. Recombinant gp65 with a hexahistidine tag at the N terminus or hexahistidine and c-myc tags 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.


* Corresponding author. Mailing address: Department of Molecular Genetics and Cell Biology, The University of Chicago, 920 East 58th Street, Chicago, IL 60637. Phone: (773) 702-1083. Fax: (773) 702-3172. E-mail: lbrd{at}uchicago.edu

{triangledown} Published ahead of print on 14 November 2008.


Journal of Bacteriology, January 2009, p. 525-532, Vol. 191, No. 2
0021-9193/09/$08.00+0     doi:10.1128/JB.01423-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.