Structural proteins of Enterococcus faecalis bacteriophage φEf11

Autor: Eduardo Muniz Barretto Tinoco, Chaiwing Hsiao, Roy H. Stevens, Derrick E. Fouts, Scott C. Kachlany, Jessica DePew, Hongming Zhang
Rok vydání: 2016
Předmět:
Zdroj: Bacteriophage. 6:e1251381
ISSN: 2159-7081
DOI: 10.1080/21597081.2016.1251381
Popis: 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 antir...
Databáze: OpenAIRE