The structural peptidoglycan hydrolase gp181 of bacteriophage φKZ

Briers, Yves; Miroshnikov, Konstantin A.; Chertkov, O. V.; Nekrasov, A. N.; Mesyanzhinov, Vadim V.; Volckaert, Guido; Lavigne, Rob

doi:10.1016/j.bbrc.2008.07.102

Cited by 42 publications

(42 citation statements)

References 21 publications

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“…A similar phenomenon was also observed in Pseudomonas syringae phage Φ13, which contains a thermosensitive lytic enzyme involved in PG penetration (Daugelavicius et al, 2005). Phages ΦKMV and ΦKZ infecting P. aeruginosa strains also displayed structural proteins with PG hydrolase domains (Briers et al, 2006(Briers et al, , 2008. Of note, the VAPGH gp36 from bacteriophage ΦKMV showed high thermoresistance.…”

Section: Virion-associated Muralytic Activities Are Present In Phagessupporting

confidence: 63%

Bacteriophage virion-associated peptidoglycan hydrolases: potential new enzybiotics

Rodríguez-Rubio

Martínez

Donovan³

et al. 2012

Critical Reviews in Microbiology

134

110

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Virion-associated peptidoglycan hydrolases (VAPGH) are phage-encoded lytic enzymes that locally degrade the peptidoglycan (PG) of the bacterial cell wall during infection. In contrast to endolysins, PGHs that mediate lysis of the host bacteria at the end of the lytic cycle to release of phage progeny, the action of VAPGHs generates a small hole through which the phage tail tube crosses the cell envelope to eject the phage genetic material at the beginning to the infection cycle. The antimicrobial activity of VAPGHs was first discovered through the observation of the phenomenon of 'lysis from without', in which the disruption of the bacterial cell wall occurs prior to phage production and is caused by a high number of phages adsorbed onto the cell surface. Based on a unique combination of properties of VAPGHs such as high specificity, remarkable thermostability, and a modular organization, these proteins are potential candidates as new antibacterial agents, e.g. against antibiotic-resistant bacteria in human therapy and veterinary as well as biopreservatives in food safety, and as biocontrol agents of harmful bacteria in agriculture. This review provides an overview of the different VAPGHs discovered to date and their potential as novel antimicrobials.

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Section: Virion-associated Muralytic Activities Are Present In Phagessupporting

confidence: 63%

Bacteriophage virion-associated peptidoglycan hydrolases: potential new enzybiotics

Rodríguez-Rubio

Martínez

Donovan³

et al. 2012

Critical Reviews in Microbiology

134

110

View full text Add to dashboard Cite

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“…This suggests that not disulfide bonds, but unfolding of the protein with increasing temperatures, followed by rapid reactivation due to instant refolding upon cooling may reconstitute enzyme activity after prolonged high temperature exposure. The latter assumption receives support from a study on thermoresistant lytic structural proteins of Pseudomonas aeruginosa phages (Lavigne et al 2004;Briers et al 2008). It was found that Gp36C, a part of the putative injection needle of phage ΦKMV, retained 50% and 21% of its activity after 1-h incubation at 100°C or 121°C, respectively (Lavigne et al 2004) and also lacks Cys residues.…”

Section: Discussionmentioning

confidence: 93%

Listeria bacteriophage peptidoglycan hydrolases feature high thermoresistance and reveal increased activity after divalent metal cation substitution

Schmelcher

Waldherr

Loessner

2011

Appl Microbiol Biotechnol

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The ability of the bacteriophage-encoded peptidoglycan hydrolases (endolysins) to destroy Gram-positive bacteria from without makes these enzymes promising antimicrobials. Recombinant endolysins from Listeria monocytogenes phages have been shown to rapidly lyse and kill the pathogen in all environments. To determine optimum conditions regarding application of recombinant Listeria phage endolysins in food or production equipments, properties of different Listeria endolysins were studied. Optimum NaCl concentration for the amidase HPL511 was 200 nM and 300 mM for the peptidases HPL118, HPL500, and HPLP35. Unlike most other peptidoglycan hydrolases, all four enzymes exhibited highest activity at elevated pH values at around pH 8-9. Lytic activity was abolished by EDTA and could be restored by supplementation with various divalent metal cations, indicating their role in catalytic function. While substitution of the native Zn 2+ by Ca 2+ or Mn 2+ was most effective in case of HPL118, HPL500, and HPLP35, supplementation with Co 2+ and Mn 2+ resulted in an approximately 5-fold increase in HPL511 activity. Interestingly, the glutamate peptidases feature a conserved SxHxxGxAxD zinc-binding motif, which is not present in the amidases, although they also require centrally located divalent metals for activity.The endolysins HPL118, HPL511, and HPLP35 revealed a surprisingly high thermostability, with up to 35% activity remaining after 30 min incubation at 90°C. The available data suggest that denaturation at elevated temperatures is reversible and may be followed by rapid refolding into a functional state.

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“…However, at the C-terminal distal end, OBP-Gp276 contains approximately 170 residues that do not align (by PSI-BLAST) with the ϳ300 residues of EL-Gp183. This extreme C-terminal portion (2043 to 2237) of the structural lysozyme of phage KZ, Gp181, was shown to enhance the specific catalytic activity 3-fold (10). Similarity to the KZ and 2012-1 homologs (Gp181 and Gp276, respectively), however, breaks off before the catalytic domain.…”

Section: Figmentioning

confidence: 99%

Complete Genome Sequence of the Giant Virus OBP and Comparative Genome Analysis of the Diverse ϕKZ-Related Phages

Cornelissen

Hardies

Shaburova

et al. 2012

J Virol

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The 283,757-bp double-stranded DNA genome of Pseudomonas fluorescens phage OBP shares a general genomic organization with Pseudomonas aeruginosa phage EL. Comparison of this genomic organization, assembled in syntenic genomic blocks interspersed with hyperplastic regions of the KZ-related phages, supports the proposed division in the "EL-like viruses," and the "phiKZ-like viruses" within a larger subfamily. Identification of putative early transcription promoters scattered throughout the hyperplastic regions explains several features of the KZ-related genome organization (existence of genomic islands) and evolution (multi-inversion in hyperplastic regions). When hidden Markov modeling was used, typical conserved core genes could be identified, including the portal protein, the injection needle, and two polypeptides with respective similarity to the 3=-5= exonuclease domain and the polymerase domain of the T4 DNA polymerase. While the N-terminal domains of the tail fiber module and peptidoglycan-degrading proteins are conserved, the observation of C-terminal catalytic domains typical for the different genera supports the further subdivision of the KZ-related phages. P seudomonas fluorescens phage OBP (vB_PflM_OBP) (30, 47) is member of a growing group of giant phages, isolated, to date, only from Pseudomonas species and represented by the completely sequenced and well-studied Pseudomonas aeruginosa myovirus KZ (9,18,19,[31][32][33]36,42). Three other phages encoding many proteins with similarity to KZ proteins have been completely sequenced: EL (23), 2012-1 (52), and PA3 (43). Krylov et al. (33) assigned 19 unsequenced Pseudomonas phages to this group. We refer to the group as KZ-related phages. Lavigne et al. (35) have argued that EL should be classified as a genus separate from KZ and 2012-1 based on its less extensive levels of similarity. By that criterion, PA3 belongs to the "phiKZ-like viruses" and the results reported here classify OBP as the second member of the possible genus EL-like viruses.OBP shares a number of definitive properties with the other KZ-related phages. Typically, KZ-related phages have a very large icosahedral head, ϳ122 nm in diameter, and a long (ϳ190-nm) contractile tail surrounded by fibers. A KZ-related phage head contains a proteinic inner body, which has been speculated to organize the packaged DNA (18, 32). The exceptionally large genomes of the KZ-related phages (between 211 and 317 kb of nonredundant sequence) are composed of circularly permuted and terminally redundant linear double-stranded DNAs as determined for KZ and 2012-1 (42, 52). The KZ-related genomes display a pronounced difference in GϩC content (between 36.8 and 48%) and all have markedly lower GϩC content than the chromosomes of their GC-rich Pseudomonas hosts (60 to 66% GϩC).This group of phages has numerous genes involved in nucleotide metabolism (e.g., thymidylate synthase, thymidylate kinase, ribonucleoside diphosphate reductase, subunit beta [NrdB], and dihydrofolate reductase) and at least six genes enco...

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The structural peptidoglycan hydrolase gp181 of bacteriophage φKZ

Cited by 42 publications

References 21 publications

Bacteriophage virion-associated peptidoglycan hydrolases: potential new enzybiotics

Bacteriophage virion-associated peptidoglycan hydrolases: potential new enzybiotics

Listeria bacteriophage peptidoglycan hydrolases feature high thermoresistance and reveal increased activity after divalent metal cation substitution

Complete Genome Sequence of the Giant Virus OBP and Comparative Genome Analysis of the Diverse ϕKZ-Related Phages

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