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PMID:18567664
| Citation |
Klumpp, J, Dorscht, J, Lurz, R, Bielmann, R, Wieland, M, Zimmer, M, Calendar, R and Loessner, MJ (2008) The terminally redundant, nonpermuted genome of Listeria bacteriophage A511: a model for the SPO1-like myoviruses of gram-positive bacteria. J. Bacteriol. 190:5753-65 |
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| Abstract |
Only little information on a particular class of myoviruses, the SPO1-like bacteriophages infecting low-G+C-content, gram-positive host bacteria (Firmicutes), is available. We present the genome analysis and molecular characterization of the large, virulent, broad-host-range Listeria phage A511. A511 contains a unit (informational) genome of 134,494 bp, encompassing 190 putative open reading frames (ORFs) and 16 tRNA genes, organized in a modular fashion common among the Caudovirales. Electron microscopy, enzymatic fragmentation analyses, and sequencing revealed that the A511 DNA molecule contains linear terminal repeats of a total of 3,125 bp, encompassing nine small putative ORFs. This particular genome structure explains why A511 is unable to perform general transduction. A511 features significant sequence homologies to Listeria phage P100 and other morphologically related phages infecting Firmicutes such as Staphylococcus phage K and Lactobacillus phage LP65. Equivalent but more-extensive terminal repeats also exist in phages P100 (approximately 6 kb) and K (approximately 20 kb). High-resolution electron microscopy revealed, for the first time, the presence of long tail fibers organized in a sixfold symmetry in these viruses. Mass spectrometry-based peptide fingerprinting permitted assignment of individual proteins to A511 structural components. On the basis of the data available for A511 and relatives, we propose that SPO1-like myoviruses are characterized by (i) their infection of gram-positive, low-G+C-content bacteria; (ii) a wide host range within the host bacterial genus and a strictly virulent lifestyle; (iii) similar morphology, sequence relatedness, and collinearity of the phage genome organization; and (iv) large double-stranded DNA genomes featuring nonpermuted terminal repeats of various sizes. |
| Links |
PubMed PMC2519532 Online version:10.1128/JB.00461-08 |
| Keywords |
DNA, Viral/chemistry; DNA, Viral/genetics; Electrophoresis, Polyacrylamide Gel; Genome, Viral; Gram-Positive Bacteria/virology; Mass Spectrometry; Microscopy, Electron; Models, Genetic; Molecular Sequence Data; Myoviridae/genetics; Myoviridae/ultrastructure; Open Reading Frames/genetics; Sequence Analysis, DNA |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0046798: viral portal complex |
ECO:0000250: |
UniProtKB:A8ASR7
|
C |
Blastp of protein sequences from TsarBomba showed e value of 0 with protein gp83 [Listeria phage A511] |
complete | |||
| GO:0098025: virus tail, baseplate |
ECO:0000250: |
C |
Researchers sequenced A511 gene. Base on Blast analyses and amino acid sequence similarities, they assigned gp103 is baseplate protein, which shows in Table S1 in the supplemental material. |
Missing: with/from | ||||
| GO:0098025: virus tail, baseplate |
ECO:0000314: |
C |
Fig 1 For the first time, we are able to document the presence of long tail fibers with a sixfold symmetry attached to the base plate regions of A511, P100, and K (Fig. 1). These whiskers are distinct from the short tail spikes present on the lower side of the base plate structure, which are best visible in images of contracted phage tails (e.g., Fig. 1D), and also exhibit a sixfold symmetry. Interestingly, the base plates of all three phages seem to undergo quite dramatic conformational changes during tail contraction, allowing better visualization of its structure and components (Fig. 1A, C, D, and F). As a result of contraction triggering, the base plate moves upwards and the tail tube is exposed and extends beneath the base plate and tail sheath. Similar observations have been made for another SPO1-like phage, LP65 of Lactobacillus (9), which also appears to resembles A511 in morphology and approximate dimensions. Via the tips of exposed tail tubes in the contracted state, virions frequently adhere to some unstructured material, probably representing cell wall debris from lysed host cells (Fig. 1F). |
complete | ||||
Notes
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