Genre
Journal ArticleDate
2016-10Author
Stevens, Roy HZhang, Hongming
Hsiao, Chaiwing
Kachlany, Scott
Tinoco, Eduardo MB
DePew, Jessica
Fouts, Derrick E
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http://hdl.handle.net/20.500.12613/5011
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10.1080/21597081.2016.1251381Abstract
ϕEf11, a temperate Siphoviridae bacteriophage, was isolated by induction from a root canal isolate of Enterococcus faecalis. Sequence analysis suggested that the ϕEf11 genome included a contiguous 8 gene module whose function was related to head structure assembly and another module of 10 contiguous genes whose products were responsible for tail structure assembly. SDS-PAGE analysis of virions of a ϕEf11 derivative revealed 11 well-resolved protein bands. To unify the deduced functional gene assignments emanating from the DNA sequence data, with the structural protein analysis of the purified virus, 6 of the SDS-PAGE bands were subjected to mass spectrometry analysis. 5 of the 6 protein bands analyzed by mass spectrometry displayed identical amino acid sequences to those predicted to be specified by 4 of the ORFs identified in the ϕEf11 genome. These included: ORF8 (predicted scaffold protein), ORF10 (predicted major head protein), ORF15 (predicted major tail protein), and ORF23 (presumptive antireceptor).Citation to related work
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BacteriophageADA compliance
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http://dx.doi.org/10.34944/dspace/4993