The Crystal Structure of the Bacteriophage PSA Endolysin Reveals a Unique Fold Responsible for Specific Recognition of Listeria Cell Walls

Korndörfer, Ingo P.; Danzer, Joseph F.; Schmelcher, Mathias; Zimmer, Markus; Skerra, Arne; Loessner, Martin J.

doi:10.1016/j.jmb.2006.08.069

Cited by 108 publications

(142 citation statements)

References 46 publications

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“…An analogy comparison can be done for phage endolysins, in which the presence of a CBD does not often constitute a prerequisite for enzyme activity. Deletion of the CBD of the L. monocytogenes endolysin PlyPSA only reduces the lytic activity (84). Also, the C-terminal domain of the Lactobacillus delbrueckii subsp.…”

Section: Resultsmentioning

confidence: 99%

Molecular Aspects and Comparative Genomics of Bacteriophage Endolysins

Oliveira

Melo

Santos

et al. 2013

J Virol

243

247

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Phages are recognized as the most abundant and diverse entities on the planet. Their diversity is determined predominantly by their dynamic adaptation capacities when confronted with different selective pressures in an endless cycle of coevolution with a widespread group of bacterial hosts. At the end of the infection cycle, progeny virions are confronted with a rigid cell wall that hinders their release into the environment and the opportunity to start a new infection cycle. Consequently, phages encode hydrolytic enzymes, called endolysins, to digest the peptidoglycan. In this work, we bring to light all phage endolysins found in completely sequenced double-stranded nucleic acid phage genomes and uncover clues that explain the phage-endolysin-host ecology that led phages to recruit unique and specialized endolysins.

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Section: Resultsmentioning

confidence: 99%

Molecular Aspects and Comparative Genomics of Bacteriophage Endolysins

Oliveira

Melo

Santos

et al. 2013

J Virol

243

247

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“…Truncation of the endolysin to just the proposed catalytic domain produced an active lysin but did not affect the specificity. Other studies reported the maintenance of endolysin activity upon removal of C-terminal domains; in many cases, this truncation led to a notable increase in activity (9,14,28,32), while in others, activity remained similar to or was lower than that of the full-length endolysin (10,21). In several cases, endolysin catalytic domains retained the same or a similar host range upon removal of the C-terminal domain (9,18,28,32), despite the fact that their peptidoglycan target is usually shared with a number of other species.…”

Section: Discussionmentioning

confidence: 99%

Genomic Sequence of Bacteriophage ATCC 8074-B1 and Activity of Its Endolysin and Engineered Variants against Clostridium sporogenes

Mayer

Gasson

Narbad

2012

Appl Environ Microbiol

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ABSTRACTLytic bacteriophage ATCC 8074-B1 produces large plaques on its hostClostridium sporogenes. Sequencing of the 47,595-bp genome allowed the identification of 82 putative open reading frames, including those encoding proteins for head and tail morphogenesis and lysis. However, sequences commonly associated with lysogeny were absent. ORF 22 encodes an endolysin, CS74L, that shows homology toN-acetylmuramoyl-l-alanine amidases, and when expressed inEscherichia coli, the protein causes effective lysis ofC. sporogenescells when added externally. CS74L was also active onClostridium tyrobutyricumandClostridium acetobutylicum. The catalytic domain expressed alone (CS74L1–177) exhibited a similar activity and the same host range as the full-length endolysin. A chimeric endolysin consisting of the CS74L catalytic domain fused to the C-terminal domain of endolysin CD27L, derived fromClostridium difficilebacteriophage ΦCD27, was produced. This chimera (CSCD) lysedC. sporogenescells with an activity equivalent to that of the catalytic domain alone. In contrast, the CD27L C-terminal domain reduced the efficacy of the CS74L catalytic domain when tested againstC. tyrobutyricum. The addition of the CD27L C-terminal domain did not enable the lysin to targetC. difficileor other CD27L-sensitive bacteria.

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“…The specificities of the endolysins are conferred by their different cell wall binding domains, which are thought to recognize Listeria-specific surface carbohydrates (113). Supporting this idea, phage PSA endolysin has a cell wall binding domain closely related to that of Ply500 and targets the same serovars, while having different enzymatic activity than Ply500 (96).…”

Section: Cell Wall Metabolismmentioning

confidence: 98%

Listeria monocytogenesSurface Proteins: from Genome Predictions to Function

Bierne

Cossart

2007

Microbiol Mol Biol Rev

210

257

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SUMMARY The genome of the human food-borne pathogen Listeria monocytogenes is predicted to encode a high number of surface proteins. This abundance likely reflects the ability of this bacterium to survive in diverse environments, including soil, food, and the human host. This review focuses on the various mechanisms by which listerial proteins are attached at the bacterial surface and their many functions, including peptidoglycan metabolism, protein processing, adhesion to host cells, and invasion of host tissues. Extensive in silico analysis of the domains or motifs present in these mosaic proteins reveals that diverse structural features allow the surface proteome to interact with diverse bacterial or host components. This diversity offers new clues about the molecular bases of Listeria pathogenesis.

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The Crystal Structure of the Bacteriophage PSA Endolysin Reveals a Unique Fold Responsible for Specific Recognition of Listeria Cell Walls

Cited by 108 publications

References 46 publications

Molecular Aspects and Comparative Genomics of Bacteriophage Endolysins

Molecular Aspects and Comparative Genomics of Bacteriophage Endolysins

Genomic Sequence of Bacteriophage ATCC 8074-B1 and Activity of Its Endolysin and Engineered Variants against Clostridium sporogenes

Listeria monocytogenesSurface Proteins: from Genome Predictions to Function

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