Molecular analysis of lytic genes of bacteriophage 80α of<i>Staphylococcus aureus</i>

Bon, J.; Mani, Nagraj; Jayaswal, Radheshyam K.

doi:10.1139/m97-087

Cited by 17 publications

(7 citation statements)

References 23 publications

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“…Second, our φ80 variant carried dut2 gene type in contrast to dut1 in genome‐sequenced φ80 (DQ908929) and third, our φ80α variant carried ami1 endolysin type versus ami2 in genome‐sequenced φ80α (Tallent et al ., 2007). However, an older sequence of φ80α harbouring the amidase gene is of ami1 type (Bon et al ., 1997). Similar discrepancies have been reported recently for the S. aureus bacteriophage φ11 amidase gene (Donovan et al ., 2008).…”

Section: Resultsmentioning

confidence: 99%

Multilocus PCR typing strategy for differentiation of Staphylococcus aureus siphoviruses reflecting their modular genome structure

Kahánková¹,

Pantůček²,

Goerke

et al. 2010

Environmental Microbiology

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Given the great biological importance and high diversity of temperate Staphylococcus aureus bacteriophages, a method is needed for the description of their genomic structure. Here we have updated a multiplex PCR strategy for the complex characterization of S. aureus phages of the family Siphoviridae. Based on the comparative genomic analysis of the available phage sequences, a multilocus PCR strategy for typing the major modules of the phage genome was designed. The genomic modules were classified on the basis of the genes for integrase (10 types), anti-repressor (five types), replication proteins polA, dnaC and dnaD (four types), dUTPase (four types), portal protein (eight types), tail appendices (four types) and endolysin (four types) corresponding to the integrase locus, lysogeny control region, and modules for DNA replication, transcription regulation, packaging, tail appendices and lysis respectively. The nine PCR assays designed for the above sequences were shown to be capable to identify the bacteriophage gene pool present both in the phage and bacterial genomes and their extensive mosaic structure. The established multiplex PCR-based multilocus diagnostic scheme is convenient for rapid and reliable phage and prophage classification and for the study of bacteriophage evolution.

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Section: Resultsmentioning

confidence: 99%

Multilocus PCR typing strategy for differentiation of Staphylococcus aureus siphoviruses reflecting their modular genome structure

Kahánková¹,

Pantůček²,

Goerke

et al. 2010

Environmental Microbiology

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“…It is a virulent Myovirus of the A1 morphotype, belongs to serogroup D, and is the type phage of the designated phage species Twort [18,19]. It is completely di¡erent from P11 and the very closely related 80K [16,20] which are temperate siphoviruses (morphotype B1) of species P11-M15 and belong to serogroup B [18]. Both groups have di¡erent host ranges.…”

Section: Discussionmentioning

confidence: 99%

The two-component lysis system of Staphylococcus aureus bacteriophage Twort: a large TTG-start holin and an associated amidase endolysin

Loessner¹

1998

FEMS Microbiology Letters

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The lysis genes of the virulent Staphylococcus aureus bacteriophage Twort were cloned and their nucleotide sequences determined. The endolysin gene plyTW encodes a 53.3-kDa protein, whose catalytic site is located in the amino-terminal domain. An enzymatically active fragment (N-terminal 271 amino acids) was overexpressed in Escherichia coli and partially purified. The enzyme rapidly cleaves staphylococcal peptidoglycan, and was shown to act as N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28). Significant sequence homology to the specific cell wall targeting domain of lysostaphin was observed in a 101-amino acid C-terminal overlap. However, we found that the large C-terminal portion (63%, 295 aa) of PlyTW is not required for staphylolytic activity. Located upstream of and overlapping plyTW by 35 bp in a different reading frame (+1), we identified holTW, which starts with a single TTG triplet. The gene specifies a 185-amino acid (20.5 kDa) holin protein, which features two potential hydrophobic, antiparallel transmembrane domains, and a highly charged, acidic C-terminus. HolTW is the largest class II holin described to date. It can substitute for the defective allele in phage V S amber mutants, both in trans from an expression plasmid, and from within gt11: :holTW. The proposed function is the formation of unspecific membrane lesions to promote access of the endolysin to the bacterial peptidoglycan. z 1998 Federation of European Microbiological Societies. Published by Elsevier Science B.V.

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“…It is a virulent Myovirus of the A1 morphotype, belongs to serogroup D, and is the type phage of the designated phage species Twort [18, 19]. It is completely different from φ11 and the very closely related 80α[16, 20] which are temperate siphoviruses (morphotype B1) of species P11‐M15 and belong to serogroup B [18]. Both groups have different host ranges.…”

Section: Discussionmentioning

confidence: 99%

The two-component lysis system ofStaphylococcus aureusbacteriophage Twort: a large TTG-start holin and an associated amidase endolysin

Loessner

Gaeng

Wendlinger

et al. 1998

FEMS Microbiology Letters

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The lysis genes of the virulent Staphylococcus aureus bacteriophage Twort were cloned and their nucleotide sequences determined. The endolysin gene plyTW encodes a 53.3-kDa protein, whose catalytic site is located in the amino-terminal domain. An enzymatically active fragment (N-terminal 271 amino acids) was overexpressed in Escherichia coli and partially purified. The enzyme rapidly cleaves staphylococcal peptidoglycan, and was shown to act as N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28). Significant sequence homology to the specific cell wall targeting domain of lysostaphin was observed in a 101-amino acid C-terminal overlap. However, we found that the large C-terminal portion (63%, 295 aa) of PlyTW is not required for staphylolytic activity. Located upstream of and overlapping plyTW by 35 bp in a different reading frame (+1), we identified holTW, which starts with a single TTG triplet. The gene specifies a 185-amino acid (20.5 kDa) holin protein, which features two potential hydrophobic, antiparallel transmembrane domains, and a highly charged, acidic C-terminus. HolTW is the largest class II holin described to date. It can substitute for the defective allele in phase lambda S' amber mutants, both in trans from an expression plasmid, and from within gt11::holTW. The proposed function is the formation of unspecific membrane lesions to promote access of the endolysin to the bacterial peptidoglycan.

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Molecular analysis of lytic genes of bacteriophage 80α ofStaphylococcus aureus

Cited by 17 publications

References 23 publications

Multilocus PCR typing strategy for differentiation of Staphylococcus aureus siphoviruses reflecting their modular genome structure

Multilocus PCR typing strategy for differentiation of Staphylococcus aureus siphoviruses reflecting their modular genome structure

The two-component lysis system of Staphylococcus aureus bacteriophage Twort: a large TTG-start holin and an associated amidase endolysin

The two-component lysis system ofStaphylococcus aureusbacteriophage Twort: a large TTG-start holin and an associated amidase endolysin

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