Publication Name	World Journal of Virology
Manuscript ID	4472
Country	United States

Received	2013-07-01 11:47
Peer-Review Started	2013-07-02 10:47
To Make the First Decision	2013-07-26 18:35
Return for Revision	2013-07-29 14:30
Revised	2013-09-22 05:07
Second Decision	2013-10-15 14:38
Accepted by Journal Editor-in-Chief
Accepted by Company Editor-in-Chief	2013-10-16 10:21
Articles in Press
Publication Fee Transferred
Edit the Manuscript by Language Editor
Typeset the Manuscript	2013-11-08 17:01
Publish the Manuscript Online	2013-11-11 15:30

ISSN	2220-3249 (online)
Open Access
Copyright
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Category	Biochemistry & Molecular Biology
Manuscript Type	Autobiography
Article Title	Genetic analysis of structural proteins in the adsorption apparatus of bacteriophage epsilon 15
Manuscript Source	Invited Manuscript
All Author List	Jared A Guichard, Paula C Middleton and Michael R McConnell
Funding Agency and Grant Number	Funding Agency Grant Number NIH-AREA Grant 1R15GM52696-01 NSF-RUI Grant DMB-8608480 Howard Hughes Medical Research Institute (to the PLNU Biology Department) Research Associates of PLNU PLNU Administration
Corresponding Author	Michael R McConnell, PhD, Department of Biology, Point Loma Nazarene University, 3900 Lomaland Drive, San Diego, CA 92106, United States. mmcconne@pointloma.edu
Key Words	Epsilon15; Virion structure; Salmonella phages
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.
Publish Date	2013-11-11 15:30
Citation	Guichard JA, Middleton PC, McConnell MR. Genetic analysis of structural proteins in the adsorption apparatus of bacteriophage epsilon 15. World J Virol 2013; 2(4): 152-159
URL	http://www.wjgnet.com/2220-3249/full/v2/i4/152.htm
DOI	http://dx.doi.org/10.5501/wjv.v2.i4.152

Full Article (PDF)	WJV-2-152.pdf
Full Article (Word)	WJV-2-152.doc
Manuscript File	4472-Review.docx
Answering Reviewers	4472-Answering reviews.pdf
Copyright License Agreement	4472-Copyright assignment.pdf
Peer-review Report	4472-Peer review(s).pdf
Scientific Editor Work List	4472-Scientific editor work list.doc