Bacteriophage lysis: mechanism and regulation.

Young, Ry

doi:10.1128/mmbr.56.3.430-481.1992

Cited by 464 publications

(405 citation statements)

References 203 publications

(394 reference statements)

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“…2F). The majority of endolysins have a modular organization, composed of at least two distinctly separate functional domains: a C-terminal cell-wall binding domain (SH3b) which directs the enzyme to its target and an N-terminal catalytic domain (Young, 1992).…”

Section: Classification Of Phage Genomic Modules and Multiplex Pcr Asmentioning

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: Classification Of Phage Genomic Modules and Multiplex Pcr Asmentioning

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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“…In bacteriophages, newly synthesized virus particles are usually released from bacterial host cells following the synergistic action of a two-component lysis system. This system is composed of a hydrophobic membrane protein, holin and a cell-wall-hydrolyzing enzyme, endolysin [1,2]. Holins are small, bacteriophage-encoded, cytoplasmic membrane proteins that form nonspeci¢c pores promoting access of endolysin to the peptidoglycan substrate [1,2].…”

Section: Introductionmentioning

confidence: 99%

“…The mechanism of cell lysis by bacteriophages have been particularly well characterized in Gram-negative bacteria [1,2]. Regarding Gram-positive bacteria, several studies have been conducted in phages that infect such hosts as Staphylococcus aureus, Lactococcus lactis, Streptococcus thermophilus, Streptococcus pneumoniae, Listeria monocytogenes and Bacillus cereus [3^13].…”

Section: Introductionmentioning

confidence: 99%

“…Regarding Gram-positive bacteria, several studies have been conducted in phages that infect such hosts as Staphylococcus aureus, Lactococcus lactis, Streptococcus thermophilus, Streptococcus pneumoniae, Listeria monocytogenes and Bacillus cereus [3^13]. Holins share characteristics that have been used in the identi¢cation of putative family members: (i) the encoding gene is usually located immediately upstream of the endolysin gene; (ii) there are at least two hydrophobic transmembrane domains with no net charge; (iii) there is a highly charged, hydrophilic, Cterminal domain [1,2]. Some recent reports have described unusual lysis systems in S. aureus bacteriophages [9,10].…”

Section: Introductionmentioning

confidence: 99%

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Characterization of a holin (HolNU3-1) in methicillin-resistant Staphylococcus aureus host

Horii

2002

FEMS Immunology and Medical Microbiology

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The gene encoding holin protein HolNU3-1 from a clinical isolate of methicillin-resistant Staphylococcus aureus (MRSA) NU3-1 was cloned and expressed in S. aureus RN4220. HolNU3-1 encoded by the holNU3-1 gene, which is located upstream of the deleted endolysin gene, was functional. Expression of the holNU3-1 gene induced a decrease in culture turbidity and formation of translucent (empty ghost) cells in S. aureus. We found heterogeneity of the holin genes and diversity of the two-component lysis system, which consists of holin and endolysin, in MRSA hosts. We suggest that this diversity is important in the identification of the evolution of clinical isolates of S. aureus.

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“…The enzyme does not contain a signal sequence for transmembrane transport, therefore other lysis proteins are expected to facilitate its transport. The S 105 and S 107 proteins, called holins, have been implicated in this process [10], but the roles of Rz and Rz1 have not been clarified. These two proteins are the least understood.…”

mentioning

confidence: 99%

Membrane fusion by proline‐rich Rz1 lipoprotein, the bacteriophage λRz1 gene product

Bryl

Keôdzierska

Laskowska

et al. 2000

European Journal of Biochemistry

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The fusogenic properties of Rz1, the proline-rich lipoprotein that is the bacteriophage l Rz1 gene product, were studied. Light scattering was used to monitor Rz1-induced aggregation of artificial neutral (dipalmitoylphosphatidylcholine/cholesterol) and negatively charged (dipalmitoylphosphatidylcholine/ cholesterol/dioleoylphosphatidylserine) liposomes. Fluorescence assays [the resonance energy transfer between N-(7-nitro-2,1,3-benzoxadiazol-4-yl)phosphatidylethanolamine and N-(lissamine rhodamine B sulfonyl)dihexadecanol-sn-glycero-3-phosphoethanolamine lipid fluorescent probes, as well as fluorescent complex formation between terbium ions and dipicolinic acid encapsulated in two liposome populations and calcein fluorescence] were used to monitor Rz1-induced lipid mixing, contents mixing and leakage of neutral and negatively charged liposomes. The results demonstrated that Rz1 caused adhesion of neutral and negatively charged liposomes with concomitant lipid mixing; membrane distortion, leading to the fusion of liposomes and hence their internal content mixing; and local destruction of the membrane accompanied by leakage of the liposome contents. The use of artificial membranes showed that Rz1 induced the fusion of membranes devoid of any proteins. This might mean that the proline stretch of Rz1 allowed interaction with membrane lipids. It is suggested that Rz1-induced liposome fusion was mediated primarily by the generation of local perturbation in the bilayer lipid membrane and to a lesser extent by electrostatic forces.Keywords: fluorescence methods; lipid liposomes; membrane fusion; Rz1 lipoprotein. The Rz1 lipoprotein is interesting from at least two points of view: (a) as a proline-rich lipoprotein with possible membrane fusogenic properties, and (b) as one of the five products of bacteriophage l lysis genes whose function has yet to be elucidated.Recently, proline-rich proteins have attracted attention [1±3]. Several proline residues in succession form the extended helix (polyproline II helix). The proline stretches tend to be exposed on the surface of a protein molecule contributing to its hydrophobicity and facilitating protein±protein interactions. Such interactions lead to unspecific, firm, but reversible, noncovalent contacts [2]. Several proline-rich motifs of physiological importance have been established [4,5].Rz1, a 6.5-kDa prolipoprotein, is the Rz1 gene product of bacteriophage l [6±8]. The mature product contains the lipid (fatty acid-esterified glyceryl±cysteine) as its N-terminal part. The lipid corresponds to that of Braun's murein-lipoprotein (Lpp) of Escherichia coli [9], but the peptide part of Rz1, composed of 60 amino acids, shows no homology with that of the Lpp [7,8]: Lipid-1 CTSKQSVSQCVKPPPPPAWIMQP-PPDWQTPLNGIISPSERG 60 .A database search using fasta to identify homologies to the Rz1 protein part showed that the Rz1 lipoprotein had a unique sequence.The overlapping genes of bacteriophage l, namely S, R and Rz/Rz1 code for five lysis proteins [8,10,11] effecting the destruction of ...

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Bacteriophage lysis: mechanism and regulation.

Cited by 464 publications

References 203 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

Characterization of a holin (HolNU3-1) in methicillin-resistant Staphylococcus aureus host

Membrane fusion by proline‐rich Rz1 lipoprotein, the bacteriophage λRz1 gene product

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