Brief Article
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World J Virol. Nov 12, 2013; 2(4): 152-159
Published online Nov 12, 2013. doi: 10.5501/wjv.v2.i4.152
Genetic analysis of structural proteins in the adsorption apparatus of bacteriophage epsilon 15
Jared A Guichard, Paula C Middleton, Michael R McConnell
Jared A Guichard, Paula C Middleton, Michael R McConnell, Department of Biology, Point Loma Nazarene University, San Diego, CA 92106, United States
Author contributions: McConnell MR designed and performed the genetic mapping and DNA sequencing experiments and also directed undergraduate researchers; Guichard JA and Middleton PC, in performing compositional analyses of particles produced by nonsense mutant viruses and the wt parent strain under non-permissive growth conditions; McConnell MR interpreted the resulting data and wrote the manuscript.
Supported by The NIH-AREA Grant, No. 1R15GM52696-01; the NSF-RUI Grant, No. DMB-8608480; the Howard Hughes Medical Research Institute (two grants to the PLNU Biology Department); Research Associates of PLNU (a 300 member alumni support group); and the PLNU Administration
Correspondence to: Michael R McConnell, PhD, Department of Biology, Point Loma Nazarene University, 3900 Lomaland Drive, San Diego, CA 92106, United States. mmcconne@pointloma.edu
Telephone: +1-619-8492304 Fax: +1-619-8492598
Received: June 30, 2013
Revised: September 20, 2013
Accepted: October 15, 2013
Published online: November 12, 2013
Core Tip

Core tip: Epsilon 15 (E15) is a temperate, serotype-converting bacteriophage that specifically infects group E1 Salmonellae bacteria. This paper presents genetic and biochemical evidence regarding the identities and positional relationships of the proteins that comprise the tail tube structure of E15. As such, it makes a small contribution towards what may someday be a fuller understanding, not only of how E15 stabilizes its packaged DNA, but also, how it triggers release of its DNA when the phage encounters a susceptible Salmonella host cell.