Evidence map›Paper›PMID 31645552›Full record

ArticleNature communications2019

Inverting family GH156 sialidases define an unusual catalytic motif for glycosidase action.

Pedro Bule, Léa Chuzel, Elena Blagova, Liang Wu, Melissa A Gray, Bernard Henrissat, Erdmann Rapp, Carolyn R Bertozzi, Christopher H Taron, Gideon J Davies

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

14 citing papers in PubMed, 21 citations in OpenAlex.

  1. Phage RyR-domain proteins degrade ADPR-based immune signals and fuel NADbioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Human Gut Metagenomes Encode Diverse GH156 Sialidases.Applied and environmental microbiology · 2022
    Article
  12. Sialidase Inhibitors with Different Mechanisms.Journal of medicinal chemistry · 2022
    Review
  13. Article
  14. A glycan FRET assay for detection and characterization of catalytic antibodies to theProceedings of the National Academy of Sciences of the United States of America · 2021
    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

10 authors at 6 institutions in 4 countries.

Pedro BuleDepartment of Chemistry, University of York, York, YO10 5DD, UK.ORCID http://orcid.org/0000-0003-2531-9926
Léa ChuzelNew England Biolabs, 240 County Road, Ipswich, MA, 01938, USA.
Elena BlagovaDepartment of Chemistry, University of York, York, YO10 5DD, UK.
Liang WuDepartment of Chemistry, University of York, York, YO10 5DD, UK.ORCID http://orcid.org/0000-0003-0294-7065
Melissa A GrayDepartment of Chemistry, Stanford University, Stanford, CA, 94305-4404, USA.
Bernard HenrissatArchitecture et Fonction des Macromolécules Biologiques (AFMB), Centre National de la Recherche Scientifique (CNRS, UMR7257), Institut National Agronomique (INRA, USC 1408) and Aix-Marseille Université (AMU), 13288 Marseille cedex 9, Marseille, France.
Erdmann RappMax Planck Institute for Dynamics of Complex Technical Systems, Sandtorstrasse 1, 39106, Magdeburg, Germany.ORCID http://orcid.org/0000-0001-6618-2626
Carolyn R BertozziDepartment of Chemistry, Stanford University, Stanford, CA, 94305-4404, USA.
Christopher H TaronNew England Biolabs, 240 County Road, Ipswich, MA, 01938, USA. taron@neb.com.
Gideon J DaviesDepartment of Chemistry, University of York, York, YO10 5DD, UK. gideon.davies@york.ac.uk.ORCID http://orcid.org/0000-0002-7343-776X
University of York · GBNew England Biolabs (United States) · USCentre National de la Recherche Scientifique · FRHoward Hughes Medical Institute · USMax Planck Institute for Dynamics of Complex Technical Systems · DEStanford University · US

Funding

Overall Priority Score P41GM103694 · NIGMS · EMORY UNIVERSITY · PI CUMMINGS, RICHARD D · 2013 to 2018
$6.9M
Investigating the Surface GlycoproteomeR01CA200423 · NCI · STANFORD UNIVERSITY · PI Carolyn Bertozzi · 2015 to 2026
$3.8M
Protein-Glycan Interaction Resource of the CFGR24GM098791 · NIGMS · EMORY UNIVERSITY · PI CUMMINGS, RICHARD D, PAULSON, JAMES C · 2011 to 2013
$2.6M
NCI NIH HHS R01 CA200423NIGMS NIH HHS P41 GM103694NIGMS NIH HHS R24 GM098791
6 · The paper itself

Abstract

Sialic acids are a family of related sugars that play essential roles in many biological events intimately linked to cellular recognition in both health and disease. Sialidases are therefore orchestrators of cellular biology and important therapeutic targets for viral infection. Here, we sought to define if uncharacterized sialidases would provide distinct paradigms in sialic acid biochemistry. We show that a recently discovered sialidase family, whose first member EnvSia156 was isolated from hot spring metagenomes, defines an unusual structural fold and active centre constellation, not previously described in sialidases. Consistent with an inverting mechanism, EnvSia156 reveals a His/Asp active center in which the His acts as a Brønsted acid and Asp as a Brønsted base in a single-displacement mechanism. A predominantly hydrophobic aglycone site facilitates accommodation of a variety of 2-linked sialosides; a versatility that offers the potential for glycan hydrolysis across a range of biological and technological platforms.

Indexed as

Catalytic DomainCrystallography, X-RayGlycocalyxNeuraminidaseProtein Structure, TertiarySialic AcidsNeuraminidaseSialic Acids

Identifiers

PMID31645552
PMCPMC6811678
OpenAlexW2981992976

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.