Evidence map›Paper›PMID 39668555›Full record

ReviewEssays in biochemistry2024

Specificity and diversity of Klebsiella pneumoniae phage-encoded capsule depolymerases.

Max J Cheetham, Yunlong Huo, Maria Stroyakovski, Li Cheng, Daniel Wan, Anne Dell, Joanne M Santini

Abstract readReview
In one paragraph

Review in Essays in biochemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed, 1 pooled it
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Article
  4. mBio · 2026
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  6. Article
  7. Article
  8. Article
  9. Article
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  11. Article
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  15. Phage and endolysin-based inhibition ofFrontiers in cellular and infection microbiology · 2026
    Review
  16. Article
  17. Article
  18. Article
  19. Isolation and characterization of a novel phage targeting Klebsiella pneumoniae K2 capsular type.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2025
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Max J Cheetham *Department of Structural and Molecular Biology, Division of Biosciences, University College London, London, WC1E 6AA, U.K.
Yunlong Huo *Department of Structural and Molecular Biology, Division of Biosciences, University College London, London, WC1E 6AA, U.K.
Maria Stroyakovski *Department of Structural and Molecular Biology, Division of Biosciences, University College London, London, WC1E 6AA, U.K.
Li ChengDepartment of Structural and Molecular Biology, Division of Biosciences, University College London, London, WC1E 6AA, U.K.
Daniel WanDepartment of Structural and Molecular Biology, Division of Biosciences, University College London, London, WC1E 6AA, U.K.
Anne DellDepartment of Life Sciences, Imperial College London, London, SW7 2AZ, U.K.
Joanne M SantiniDepartment of Structural and Molecular Biology, Division of Biosciences, University College London, London, WC1E 6AA, U.K.ORCID 0000-0003-1808-898X

Funding

Biotechnology and Biological Sciences Research Council (BBSRC) BB/X511079/1Engineering and Physical Sciences Research Council (EPSRC) EP/S022856/1
6 · The paper itself

Abstract

Klebsiella pneumoniae is an opportunistic pathogen with significant clinical relevance. K. pneumoniae-targeting bacteriophages encode specific polysaccharide depolymerases with the ability to selectively degrade the highly varied protective capsules, allowing for access to the bacterial cell wall. Bacteriophage depolymerases have been proposed as novel antimicrobials to combat the rise of multidrug-resistant K. pneumoniae strains. These enzymes display extraordinary diversity, and are key determinants of phage host range, however with limited data available our current knowledge of their mechanisms and ability to predict their efficacy is limited. Insight into the resolved structures of Klebsiella-specific capsule depolymerases reveals varied catalytic mechanisms, with the intra-chain cleavage mechanism providing opportunities for recombinant protein engineering. A detailed comparison of the 58 characterised depolymerases hints at structural and mechanistic patterns, such as the conservation of key domains for substrate recognition and phage tethering, as well as diversity within groups of depolymerases that target the same substrate. Another way to understand depolymerase specificity is by analyzing the targeted capsule structures, as these may share similarities recognizable by bacteriophage depolymerases, leading to broader substrate specificities. Although we have only begun to explore the complexity of Klebsiella capsule depolymerases, further research is essential to thoroughly characterise these enzymes. This will be crucial for understanding their mechanisms, predicting their efficacy, and engineering optimized enzymes for therapeutic applications.

Indexed as

Bacterial CapsulesBacteriophagesGlycoside HydrolasesKlebsiella pneumoniaeSubstrate Specificitycapsular-polysaccharide galactohydrolaseGlycoside Hydrolasescapsular polysaccharide depolymerasescapsuledepolymeraseKlebsiella pneumoniaephage

Identifiers

PMID39668555
PMCPMC11652154

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.