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Genome Sequence, Structural Proteins, and Capsid Organization of the Cyanophage Syn5: A "Horned" Bacteriophage of Marine Synechococcus

Pope, WH and Weigele, PR and Chang, J and Pedulla, ML and Ford, ME and Houtz, JM and Jiang, W and Chiu, W and Hatfull, GF and Hendrix, RW and King, J (2007) Genome Sequence, Structural Proteins, and Capsid Organization of the Cyanophage Syn5: A "Horned" Bacteriophage of Marine Synechococcus. Journal of Molecular Biology, 368 (4). 966 - 981. ISSN 0022-2836

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Abstract

Marine Synechococcus spp and marine Prochlorococcus spp are numerically dominant photoautotrophs in the open oceans and contributors to the global carbon cycle. Syn5 is a short-tailed cyanophage isolated from the Sargasso Sea on Synechococcus strain WH8109. Syn5 has been grown in WH8109 to high titer in the laboratory and purified and concentrated retaining infectivity. Genome sequencing and annotation of Syn5 revealed that the linear genome is 46,214 bp with a 237 bp terminal direct repeat. Sixty-one open reading frames (ORFs) were identified. Based on genomic organization and sequence similarity to known protein sequences within GenBank, Syn5 shares features with T7-like phages. The presence of a putative integrase suggests access to a temperate life cycle. Assignment of 11 ORFs to structural proteins found within the phage virion was confirmed by mass-spectrometry and N-terminal sequencing. Eight of these identified structural proteins exhibited amino acid sequence similarity to enteric phage proteins. The remaining three virion proteins did not resemble any known phage sequences in GenBank as of August 2006. Cryo-electron micrographs of purified Syn5 virions revealed that the capsid has a single "horn", a novel fibrous structure protruding from the opposing end of the capsid from the tail of the virion. The tail appendage displayed an apparent 3-fold rather than 6-fold symmetry. An 18 Å resolution icosahedral reconstruction of the capsid revealed a T = 7 lattice, but with an unusual pattern of surface knobs. This phage/host system should allow detailed investigation of the physiology and biochemistry of phage propagation in marine photosynthetic bacteria. © 2007 Elsevier Ltd. All rights reserved.


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Details

Item Type: Article
Status: Published
Creators/Authors:
CreatorsEmailPitt UsernameORCID
Pope, WHwelkin@pitt.eduWELKIN0000-0002-2012-2924
Weigele, PR
Chang, J
Pedulla, ML
Ford, ME
Houtz, JM
Jiang, W
Chiu, W
Hatfull, GFgfh@pitt.eduGFH
Hendrix, RWrhx@pitt.eduRHX
King, J
Date: 11 May 2007
Date Type: Publication
Journal or Publication Title: Journal of Molecular Biology
Volume: 368
Number: 4
Page Range: 966 - 981
DOI or Unique Handle: 10.1016/j.jmb.2007.02.046
Schools and Programs: Dietrich School of Arts and Sciences > Biological Sciences
Refereed: Yes
ISSN: 0022-2836
MeSH Headings: Bacteriophages--chemistry; Bacteriophages--ultrastructure; Capsid--chemistry; Capsid--ultrastructure; Capsid Proteins--chemistry; Capsid Proteins--genetics; Cryoelectron Microscopy; Genome, Viral; Molecular Sequence Data; Open Reading Frames; Synechococcus--virology
Other ID: NLM NIHMS22529, NLM PMC2971696
PubMed Central ID: PMC2971696
PubMed ID: 17383677
Date Deposited: 12 Dec 2012 20:17
Last Modified: 02 Feb 2019 16:58
URI: http://d-scholarship.pitt.edu/id/eprint/16708

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