Genomic and proteomic characterization of SuMu, a Mu-like bacteriophage infecting Haemophilus parasuisReport as inadecuate

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BMC Genomics

, 13:331

First Online: 23 July 2012Received: 11 January 2012Accepted: 28 June 2012DOI: 10.1186-1471-2164-13-331

Cite this article as: Zehr, E.S., Tabatabai, L.B. & Bayles, D.O. BMC Genomics 2012 13: 331. doi:10.1186-1471-2164-13-331


BackgroundHaemophilus parasuis, the causative agent of Glässer’s disease, is prevalent in swine herds and clinical signs associated with this disease are meningitis, polyserositis, polyarthritis, and bacterial pneumonia. Six to eight week old pigs in segregated early weaning herds are particularly susceptible to the disease. Insufficient colostral antibody at weaning or the mixing of pigs with heterologous virulent H. parasuis strains from other farm sources in the nursery or grower-finisher stage are considered to be factors for the outbreak of Glässer’s disease. Previously, a Mu-like bacteriophage portal gene was detected in a virulent swine isolate of H. parasuis by nested polymerase chain reaction. Mu-like bacteriophages are related phyologenetically to enterobacteriophage Mu and are thought to carry virulence genes or to induce host expression of virulence genes. This study characterizes the Mu-like bacteriophage, named SuMu, isolated from a virulent H. parasuis isolate.

ResultsCharacterization was done by genomic comparison to enterobacteriophage Mu and proteomic identification of various homologs by mass spectrometry. This is the first report of isolation and characterization of this bacteriophage from the Myoviridae family, a double-stranded DNA bacteriophage with a contractile tail, from a virulent field isolate of H. parasuis. The genome size of bacteriophage SuMu was 37,151 bp. DNA sequencing revealed fifty five open reading frames, including twenty five homologs to Mu-like bacteriophage proteins: Nlp, phage transposase-C-terminal, COG2842, Gam-like protein, gp16, Mor, peptidoglycan recognition protein, gp29, gp30, gpG, gp32, gp34, gp36, gp37, gpL, phage tail tube protein, DNA circulation protein, gpP, gp45, gp46, gp47, COG3778, tail fiber protein gp37-C terminal, tail fiber assembly protein, and Com. The last open reading frame was homologous to IS1414. The G + C content of bacteriophage SuMu was 41.87% while its H. parasuis host genome’s G + C content was 39.93%. Twenty protein homologs to bacteriophage proteins, including 15 structural proteins, one lysogeny-related and one lysis-related protein, and three DNA replication proteins were identified by mass spectrometry. One of the tail proteins, gp36, may be a virulence-related protein.

ConclusionsBacteriophage SuMu was characterized by genomic and proteomic methods and compared to enterobacteriophage Mu.

KeywordsHaemophilus parasuis Bacteriophage Virulence Abbreviations1-D and 2-D1- and 2- dimensional

ACTArtemis Comparison Tool

BpBase pair

β-NADβ-Nicotinamide adenine dinucleotide

CDSCoding sequence

EDTAEthylenediaminetetraacetic acid

HClHydrodrochloric acid

IPGImmobilized pH gradient

IEFIsoelectric focusing

MALDI-TOFMatrix-assisted laser desorption-ionization-time of flight

MWCOMolecular Weight Cut Off

NAHMSNational Animal Health Monitoring System

NCBINational Center for Biotechnology Information


ORFOpen reading frame

PCRPolymerase chain reaction

PRIDEProteomics identifications database

SDS-PAGESodium dodecyl sulfate polyacrylamide gel electrophoresis

SEWSegregated Early Weaning

TCATricholoroacetic acid

TFATrifluoroacetic acid.

Electronic supplementary materialThe online version of this article doi:10.1186-1471-2164-13-331 contains supplementary material, which is available to authorized users.

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Author: Emilie S Zehr - Louisa B Tabatabai - Darrell O Bayles


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