|Entry||Database: EMDB / ID: EMD-9676|
|Title||Vibrio phage M4 capsid|
|Method||single particle reconstruction / cryo EM / Resolution: 15.4 Å|
|Authors||Das S / Dutta M / Sen A / Ghosh AN|
|Funding support|| India, 1 items |
|Citation||Journal: Arch. Virol. / Year: 2019|
Title: Structural analysis and proteomics studies on the Myoviridae vibriophage M4.
Authors: Sayani Das / Moumita Dutta / Anindito Sen / Amar N Ghosh /
Abstract: Bacteriophages play a crucial role in tracking the spread of bacterial epidemics. The frequent emergence of antibiotic-resistant bacterial strains throughout the world has motivated studies on ...Bacteriophages play a crucial role in tracking the spread of bacterial epidemics. The frequent emergence of antibiotic-resistant bacterial strains throughout the world has motivated studies on bacteriophages that can potentially be used in phage therapy as an alternative to conventional antibiotic treatment. A recent outbreak of cholera in Haiti took many lives due to a rapid development of resistance to the available antibiotics. The properties of vibriophages, bacteriophages that infect Vibrio cholerae, are therefore of practical interest. A detailed understanding of the structure and assembly of a vibriophage is potentially useful in developing phage therapy against cholera as well as for fabricating artificial nanocontainers. Therefore, the aim of the present study was to determine the three-dimensional organization of vibriophage M4 at sub-nanometer resolution by electron microscopy and single-particle analysis techniques to facilitate its use as a therapeutic agent. We found that M4 has a large capsid with T = 13 icosahedral symmetry and a long contractile tail. This double-stranded DNA phage also contains a head-to-tail connector protein complex that joins the capsid to the tail and a prominent baseplate at the end of the tail. This study also provides information regarding the proteome of this phage, which is proteins similar to that of other Myoviridae phages, and most of the encoded proteins are structural proteins that form the exquisite architecture of this bacteriophage.
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_9676.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 2.5918 Å|
|Symmetry||Space group: 1|
CCP4 map header:
|Entire||Name: Viruses / Details: Vibrio phage M4, ATCC number-51354-B4 / Number of components: 1|
-Component #1: virus, Viruses
|Virus||Name: VirusesVirus / Class: VIRION / Details: Vibrio phage M4, ATCC number-51354-B4 / Empty: No / Enveloped: No / Isolate: OTHER|
|Species||Species: Viruses / Strain: M4|
|Source (natural)||Host Species: Vibrio cholerae MAK 757 (bacteria)|
|Shell #1||Name of element: Vibrio phage M4 capsid / Diameter: 800.0 Å / T number (triangulation number): 13|
|Specimen||Specimen state: Particle / Method: cryo EM|
|Sample solution||pH: 7.4|
|Vitrification||Instrument: LEICA EM CPC / Cryogen name: ETHANE|
-Electron microscopy imaging
|Imaging||Microscope: FEI TECNAI 12|
|Electron gun||Electron source: TUNGSTEN HAIRPIN / Accelerating voltage: 120 kV / Electron dose: 10 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: KODAK SO-163 FILM|
|Processing||Method: single particle reconstruction / Number of projections: 500|
|3D reconstruction||Resolution: 15.4 Å / Resolution method: FSC 0.143 CUT-OFF|
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