Evidence map›Paper›PMID 25100731›Full record

ArticleThe Journal of biological chemistry2014

Conformational analysis of the Streptococcus pneumoniae hyaluronate lyase and characterization of its hyaluronan-specific carbohydrate-binding module.

Michael D L Suits, Benjamin Pluvinage, Adrienne Law, Yan Liu, Angelina S Palma, Wengang Chai, Ten Feizi, Alisdair B Boraston

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.3field-weighted citation impact, top 43% 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

13 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Acoustic force spectroscopy reveals subtle differences in cellulose unbinding behavior of carbohydrate-binding modules.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Article
  12. Review
  13. Blood‒Brain Barrier Pathology and CNS Outcomes inInternational journal of molecular sciences · 2018
    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

8 authors at 3 institutions in 3 countries.

Michael D L SuitsDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8W 3P6, Canada.
Benjamin PluvinageDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8W 3P6, Canada.
Adrienne LawDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8W 3P6, Canada.
Yan LiuGlycosciences Laboratory, Imperial College London, Burlington Danes Building, Du Cane Road, London W12 0NN, United Kingdom, and.
Angelina S PalmaGlycosciences Laboratory, Imperial College London, Burlington Danes Building, Du Cane Road, London W12 0NN, United Kingdom, and; REQUIMTE, Department of Chemistry, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal.
Wengang ChaiGlycosciences Laboratory, Imperial College London, Burlington Danes Building, Du Cane Road, London W12 0NN, United Kingdom, and.
Ten FeiziGlycosciences Laboratory, Imperial College London, Burlington Danes Building, Du Cane Road, London W12 0NN, United Kingdom, and.
Alisdair B BorastonDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8W 3P6, Canada,. Electronic address: boraston@uvic.ca.
University of Victoria · CAImperial College London · GBUniversidade Nova de Lisboa · PT

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
CIHR FRN 86610NCRR NIH HHS P41 RR001209NCRR NIH HHS P41RR001209Wellcome TrustWellcome Trust WT093378MA/Z/10/ZWellcome Trust WT099197/Z/12/ZMA
6 · The paper itself

Abstract

For a subset of pathogenic microorganisms, including Streptococcus pneumoniae, the recognition and degradation of host hyaluronan contributes to bacterial spreading through the extracellular matrix and enhancing access to host cell surfaces. The hyaluronate lyase (Hyl) presented on the surface of S. pneumoniae performs this role. Using glycan microarray screening, affinity electrophoresis, and isothermal titration calorimetry we show that the N-terminal module of Hyl is a hyaluronan-specific carbohydrate-binding module (CBM) and the founding member of CBM family 70. The 1.2 Å resolution x-ray crystal structure of CBM70 revealed it to have a β-sandwich fold, similar to other CBMs. The electrostatic properties of the binding site, which was identified by site-directed mutagenesis, are distinct from other CBMs and complementary to its acidic ligand, hyaluronan. Dynamic light scattering and solution small angle x-ray scattering revealed the full-length Hyl protein to exist as a monomer/dimer mixture in solution. Through a detailed analysis of the small angle x-ray scattering data, we report the pseudoatomic solution structures of the monomer and dimer forms of the full-length multimodular Hyl.

Indexed as

Protein MultimerizationBacterial ProteinsCrystallography, X-RayMutagenesis, Site-DirectedPolysaccharide-LyasesProtein Structure, QuaternaryProtein Structure, TertiaryStreptococcus pneumoniaeBacterial Proteinshyaluronate lyasePolysaccharide-LyasesCarbohydrateCarbohydrate-binding ProteinCarbohydrate ProcessingCrystallographyGlycobiologyHyaluronanHyaluronate LyaseSmall Angle X-ray Scattering (SAXS)Streptococcus

Identifiers

PMID25100731
PMCPMC4175358
OpenAlexW1970291191

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.