Evidence map›Paper›PMID 35377223›Full record

ArticleMicrobiology spectrum2022

Potential Role of the Host-Derived Cell-Wall Binding Domain of Endolysin CD16/50L as a Molecular Anchor in Preservation of Uninfected Clostridioides difficile for New Rounds of Phage Infection.

Wichuda Phothichaisri, Surang Chankhamhaengdecha, Tavan Janvilisri, Jirayu Nuadthaisong, Tanaporn Phetruen, Robert P Fagan, Sittinan Chanarat

Open access · goldAbstract read
In one paragraph

Article in Microbiology spectrum, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.1field-weighted citation impact, top 11% of its field
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

17 citing papers in PubMed, 23 citations in OpenAlex.

  1. A set of genetic tools for use inMicrobiology (Reading, England) · 2026
    Article
  2. Review
  3. Phage and endolysin-based inhibition ofFrontiers in cellular and infection microbiology · 2026
    Review
  4. Recent Advances in Endolysin Engineering.Antibiotics (Basel, Switzerland) · 2025
    Review
  5. Review
  6. Article
  7. Review
  8. Mechanisms ofFrontiers in cellular and infection microbiology · 2025
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Review
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 at 2 institutions in 2 countries.

Wichuda PhothichaisriDepartment of Biochemistry, Faculty of Science, Mahidol Universitygrid.10223.32, Bangkok, Thailand.
Surang ChankhamhaengdechaDepartment of Biology, Faculty of Science, Mahidol Universitygrid.10223.32, Bangkok, Thailand.
Tavan JanvilisriDepartment of Biochemistry, Faculty of Science, Mahidol Universitygrid.10223.32, Bangkok, Thailand.
Jirayu NuadthaisongDepartment of Biochemistry, Faculty of Science, Mahidol Universitygrid.10223.32, Bangkok, Thailand.
Tanaporn PhetruenDepartment of Biochemistry, Faculty of Science, Mahidol Universitygrid.10223.32, Bangkok, Thailand.
Robert P FaganSchool of Biosciences, Florey Institute, University of Sheffieldgrid.11835.3e, Sheffield, United Kingdom.
Sittinan ChanaratDepartment of Biochemistry, Faculty of Science, Mahidol Universitygrid.10223.32, Bangkok, Thailand.ORCID 0000-0001-6267-0040
Mahidol University · THUniversity of Sheffield · GB

Funding

Biotechnology and Biological Sciences Research Council BB/P02002X/1Medical Research Council MR/S009272/1Wellcome Trust 204877/Z/16/Z
6 · The paper itself

Abstract

Endolysin is a phage-encoded cell-wall hydrolase which degrades the peptidoglycan layer of the bacterial cell wall. The enzyme is often expressed at the late stage of the phage lytic cycle and is required for progeny escape. Endolysins of bacteriophage that infect Gram-positive bacteria often comprises two domains: a peptidoglycan hydrolase and a cell-wall binding domain (CBD). Although the catalytic domain of endolysin is relatively well-studied, the precise role of CBD is ambiguous and remains controversial. Here, we focus on the function of endolysin CBD from a recently isolated Clostridioides difficile phage. We found that the CBD is not required for lytic activity, which is strongly prevented by the surface layer of C. difficile. Intriguingly, hidden Markov model analysis suggested that the endolysin CBD is likely derived from the CWB2 motif of C. difficile cell-wall proteins but possesses a higher binding affinity to bacterial cell-wall polysaccharides. Moreover, the CBD forms a homodimer, formation of which is necessary for interaction with the surface saccharides. Importantly, endolysin diffusion and sequential cytolytic assays showed that CBD of endolysin is required for the enzyme to be anchored to post-lytic cell-wall remnants, suggesting its physiological roles in limiting diffusion of the enzyme, preserving neighboring host cells, and thereby enabling the phage progeny to initiate new rounds of infection. Taken together, this study provides an insight into regulation of endolysin through CBD and can potentially be applied for endolysin treatment against C. difficile infection.

Indexed as

BacteriophagesClostridioides difficileCell WallClostridioidesEndopeptidasesN-Acetylmuramoyl-L-alanine AmidasePolysaccharides, BacterialendolysinEndopeptidasesN-Acetylmuramoyl-L-alanine AmidasePolysaccharides, Bacterialbacteria-phage coevolutioncell-wall binding domainClostridioides difficileendolysinpeptidoglycansurface layer

Identifiers

PMID35377223
PMCPMC9045149
OpenAlexW4225087508

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.