Comparative analysis of the genomes of the temperate bacteriophages φ11, φ12 and φ13 of Staphylococcus aureus 8325

Iandolo, John J.; Worrell, Veronica; Groicher, Kajetan H.; Qian, Yu; Tian, Runying; Kenton, Steve; Dorman, Angela; Ji, Honggui; Lin, Shaoping; Loh, Phoebe; Qi, Sulan; Zhu, Hua; Roe, Bruce A.

doi:10.1016/s0378-1119(02)00481-x

Cited by 150 publications

(122 citation statements)

References 38 publications

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“…StauST398-5pro shares 75% identity with /MR11 (Rashel et al, 2007) and with /ETA (Yamaguchi et al, 2000) over more than half of its length. The remaining 15 Kb of the genome showed a highly mosaic structure with small segments (generally <3 Kb) sharing some similarity with /PVL, / ETA, /13 or /ROSA (Yamaguchi et al, 2000;Kaneko et al, 1998;Iandolo et al, 2002). PCR tests with specific primers detected StauST398-5pro only in isolates of subgroup E (Suppl.…”

Section: Characterization Of Phages and Prophages Of The Emerging Hummentioning

confidence: 99%

Analysis of prophages harbored by the human-adapted subpopulation of Staphylococcus aureus CC398

Mee-Marquet

Corvaglia

Valentin

et al. 2013

Infection, Genetics and Evolution

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a b s t r a c tStaphylococcus aureus clonal complex 398 is a livestock-associated pathogen that poses a worldwide threat because of its ability to colonize and infect both humans and animals. We used high-resolution whole-genome microarrays, prophage profiling, immune evasion cluster characterization and wholegenome sequencing to investigate the roles of prophages in the emerging human-adapted subpopulation of CC398 that has been associated with invasive infections in humans living in animal-free environments.We characterized one phage and two prophages specifically harbored by CC398 isolates belonging to the emerging subpopulation. We introduced the phage into permissive prophage-free isolates. We investigated the effects of lysogeny on the host ability to resist further phage infection and transformation, to acquire the capacity to invade human cells, and to express virulence factors encoded by prophages. We report evidence of a defective /MR11-like helper prophage, named StauST398-5pro, specifically associated with the emerging non-LA CC398 subpopulation. StauST398-5pro confers substantial protection against horizontal genetic transfer to its host. It interacts with a human-associated b-converting prophage encoding immune-modulating proteins such that virulence genes are expressed during stress situations.Our findings provide insight into the role of phages in the expression of virulence and in the spread of genetic information among new host-adapted S. aureus isolates. We demonstrate that functional prophage elements can condition host specificity and confer new virulence traits on emerging intra-species clones of bacteria.

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Section: Characterization Of Phages and Prophages Of The Emerging Hummentioning

confidence: 99%

Analysis of prophages harbored by the human-adapted subpopulation of Staphylococcus aureus CC398

Mee-Marquet

Corvaglia

Valentin

et al. 2013

Infection, Genetics and Evolution

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“…Both share the morphogenesis region in their genomes. 26,89) (ii) The N315 group: This group includes N315 and Mu50A, which share about half of the morphogenesis region with that of 13.…”

Section: )mentioning

confidence: 99%

“…(iii) The SLT group: SLT and prohages Sa2mw, 65,66) 12, 26,89) and COL 67) belong to this group. The PVL-carrying prophage Sa2mw was found in the genomic sequencing data from S. aureus strain 2MW, a typical community-acquired MRSA strain.…”

Section: -64)mentioning

confidence: 99%

Bacterial Two-component and Hetero-heptameric Pore-forming Cytolytic Toxins: Structures, Pore-forming Mechanism, and Organization of the Genes

Kaneko

Kamio

2004

Bioscience, Biotechnology, and Biochemistry

296

248

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“…Knowledge of the lytic activity of both endolysins is limited. Their nucleotide sequences have been published (16), and the 11 endolysin has been shown to possess a D-alanyl-glycyl endopeptidase and an N-acetylmuramyl-L-alanine amidase activity on crude cell walls of S. aureus OS2 (24).…”

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confidence: 99%

Lytic Activity of Recombinant Bacteriophage φ11 and φ12 Endolysins on Whole Cells and Biofilms of Staphylococcus aureus

Saß

Bierbaum

2007

Appl Environ Microbiol

204

156

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The recombinant 11 endolysin hydrolyzed heat-killed staphylococci as well as staphylococcal biofilms. Cell wall targeting appeared to be a prerequisite for lysis of whole cells, and the combined action of the endopeptidase and amidase domains was necessary for maximum activity. In contrast, the 12 endolysin was inactive and caused aggregation of the cells.Infections caused by Staphylococcus aureus and Staphylococcus epidermidis still play a major role in human and animal disease. In particular staphylococcal biofilms on indwelling devices are difficult to treat due to their inherent antibiotic resistance (5,7,26). In this context, it is important to develop alternative treatment strategies to combat staphylococcal infections, particularly in view of the ability of staphylococci to acquire resistance to commonly used antibiotics (10,23,29). Phage lysins, or endolysins, have received considerable attention as possible antimicrobial agents against gram-positive bacteria and have been applied to a variety of pathogens, such as Bacillus anthracis (21), Streptococcus pneumoniae (9), and S. aureus (25). Endolysins are active against dead cells and even living, planktonic cells (9, 25), but their ability to lyse the complex structure of staphylococcal biofilms has not yet been investigated. In this approach, we cloned and heterologously overexpressed the lysis genes of the bacteriophages 11 and 12 of S. aureus NCTC8325 in Escherichia coli for subsequent analysis of the lytic activity of the enzymes and their single subdomains on cell walls, whole cells, and biofilms. Knowledge of the lytic activity of both endolysins is limited. Their nucleotide sequences have been published (16), and the 11 endolysin has been shown to possess a D-alanyl-glycyl endopeptidase and an N-acetylmuramyl-L-alanine amidase activity on crude cell walls of S. aureus OS2 (24).Sequence comparison, cloning, and overexpression of 11 and 12 endolysins. The 11 and 12 endolysin sequences were BLAST searched against the NCBI protein database. Both endolysins are modular enzymes which consist of three distinct domains coding for an N-terminal CHAP (cysteine, histidine-dependent amidohydrolases/peptidases) domain with hydrolytic function, a central amidase domain (N-acetylmuramyl-L-alanine amidase), and a C-terminal SH3b domain, which is involved in cell wall recognition (1). In spite of their similar domain architecture, these endolysins show low sequence identity (26.9%).The endolysin genes of the bacteriophages 11 (open reading frame [ORF] 53; 1,473 bp; accession number NC_004615) and 12 (ORF 49; 1,455 bp; accession number NC_004616) were amplified by PCR from genomic DNA of S. aureus NCTC8325, using the primers listed in Table 1. In order to test the activity of the 11 endolysin subunits, the endopeptidase unit (11endo, amino acids [aa] 1 to 180) and the amidase unit (11ami, aa 180 to 371) as well as each unit plus the cell wall binding domain (11endo/CBD, aa 1 to 180/371 to 490, and 11ami/CBD, aa 180 to 490) were constructed separately (Fig. 1). In ad...

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Comparative analysis of the genomes of the temperate bacteriophages φ11, φ12 and φ13 of Staphylococcus aureus 8325

Cited by 150 publications

References 38 publications

Analysis of prophages harbored by the human-adapted subpopulation of Staphylococcus aureus CC398

Analysis of prophages harbored by the human-adapted subpopulation of Staphylococcus aureus CC398

Bacterial Two-component and Hetero-heptameric Pore-forming Cytolytic Toxins: Structures, Pore-forming Mechanism, and Organization of the Genes

Lytic Activity of Recombinant Bacteriophage φ11 and φ12 Endolysins on Whole Cells and Biofilms of Staphylococcus aureus

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