Document Type
Article
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.
Disciplines
Animal Sciences | Bacteriology | Bioinformatics | Biology | Biotechnology | Dairy Science | Ecology and Evolutionary Biology | Environmental Health | Environmental Microbiology and Microbial Ecology | Food Biotechnology | Food Microbiology | Food Science | Genetics and Genomics | Immunology and Infectious Disease | Meat Science | Medical Microbiology | Medical Sciences | Medicine and Health Sciences | Microbiology | Nutrition | Organismal Biological Physiology | Organisms | Other Animal Sciences | Other Microbiology | Parasitology | Pathogenic Microbiology | Pharmacology, Toxicology and Environmental Health | Public Health | Virology
Abstract
The physical characteristics of bacteriophages establish them as viable candidates for downstream development of pathogen detection assays and biocontrol measures. To utilize phages for such purposes, a detailed knowledge of their host interaction mechanisms is a prerequisite. There is currently a wealth of knowledge available concerning Gram-negative phage-host interaction, but little by comparison for Gram-positive phages and Listeria phages in particular. In this research, the lytic spectrum of two recently isolated Listeria monocytogenes phages (vB_LmoS_188 and vB_LmoS_293) was determined, and the genomic basis for their observed serotype 4b/4e host-specificity was investigated using comparative genomics. The late tail genes of these phages were identified to be highly conserved when compared to other serovar 4-specific Listeria phages. Spontaneous mutants of each of these phages with broadened host specificities were generated. Their late tail gene sequences were compared with their wild-type counterparts resulting in the putative identification of the products of ORF 19 of vB_LmoS_188 and ORF 20 of vB_LmoS_293 as the receptor binding proteins of these phages. The research findings also indicate that conserved baseplate architectures and host interaction mechanisms exist for Listeria siphoviruses with differing host-specificities, and further contribute to the current knowledge of phage-host interactions with regard to Listeria phages.
Recommended Citation
Casey A, Jordan K, Neve H, Coffey A and McAuliffe O (2015) A tail of two phages: genomic and functional analysis of Listeria monocytogenes phages vB_LmoS_188 and vB_LmoS_293 reveal the receptor-binding proteins involved in host specificity. Front. Microbiol. 6:1107. doi: 10.3389/fmicb.2015.01107
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Bacteriology Commons, Bioinformatics Commons, Biology Commons, Biotechnology Commons, Dairy Science Commons, Ecology and Evolutionary Biology Commons, Environmental Health Commons, Environmental Microbiology and Microbial Ecology Commons, Food Biotechnology Commons, Food Microbiology Commons, Genetics and Genomics Commons, Meat Science Commons, Medical Microbiology Commons, Nutrition Commons, Organismal Biological Physiology Commons, Organisms Commons, Other Animal Sciences Commons, Other Microbiology Commons, Parasitology Commons, Pathogenic Microbiology Commons, Public Health Commons, Virology Commons
Publication Details
Frontiers in Microbiology / Food Microbiology
Received: 28 July 2015; Accepted: 25 September 2015;
Published: 09 October 2015.
Edited by:
Abd El-Latif Hesham, Assiut University, EgyptReviewed by:
Evelien M. Adriaenssens, University of Pretoria, South AfricaDavid Rodriguez-Lazaro, Instituto Tecnológico Agrario de Castilla y León, Spain
Copyright © 2015 Casey, Jordan, Neve, Coffey and McAuliffe. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
*Correspondence: Olivia McAuliffe, olivia.mcauliffe@teagasc.ie