Evidence map›Paper›PMID 24608122›Full record

ArticlePloS one2014

EndoE from Enterococcus faecalis hydrolyzes the glycans of the biofilm inhibiting protein lactoferrin and mediates growth.

Julia Garbe, Jonathan Sjögren, Eoin F J Cosgrave, Weston B Struwe, Marta Bober, Anders I Olin, Pauline M Rudd, Mattias Collin

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. 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
1.4field-weighted citation impact, top 19% 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, 32 citations in OpenAlex.

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  13. Frontiers in immunology · 2018
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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 2 institutions in 2 countries.

Julia GarbeDepartment of Clinical Sciences, Division of Infection Medicine, Lund University, Lund, Sweden.
Jonathan SjögrenDepartment of Clinical Sciences, Division of Infection Medicine, Lund University, Lund, Sweden.
Eoin F J CosgraveDublin Oxford Glycobiology Group, National Institute for Bioprocessing Research & Training (NIBRT), Mount Merrion, Blackrock, Co. Dublin, Ireland.
Weston B StruweDublin Oxford Glycobiology Group, National Institute for Bioprocessing Research & Training (NIBRT), Mount Merrion, Blackrock, Co. Dublin, Ireland.
Marta BoberDepartment of Clinical Sciences, Division of Infection Medicine, Lund University, Lund, Sweden.
Anders I OlinDepartment of Clinical Sciences, Division of Infection Medicine, Lund University, Lund, Sweden.
Pauline M RuddDublin Oxford Glycobiology Group, National Institute for Bioprocessing Research & Training (NIBRT), Mount Merrion, Blackrock, Co. Dublin, Ireland.
Mattias CollinDepartment of Clinical Sciences, Division of Infection Medicine, Lund University, Lund, Sweden.
Lund University · SENational Institute for Bioprocessing Research and Training · IE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosidases are widespread among bacteria. The opportunistic human pathogen Enterococcus faecalis encodes several putative glycosidases but little is known about their functions. The identified endo-β-N-acetylglucosaminidase EndoE has activity on the N-linked glycans of the human immunoglobulin G (IgG). In this report we identified the human glycoprotein lactoferrin (hLF) as a new substrate for EndoE. Hydrolysis of the N-glycans from hLF was investigated using lectin blot, UHPLC and mass spectrometry, showing that EndoE releases major glycoforms from this protein. hLF was shown to inhibit biofilm formation of E. faecalis in vitro. Glycans of hLF influence the binding to E. faecalis, and EndoE-hydrolyzed hLF inhibits biofilm formation to lesser extent than intact hLF indicating that EndoE prevents the inhibition of biofilm. In addition, hLF binds to a surface-associated enolase of E. faecalis. Culture experiments showed that the activity of EndoE enables E. faecalis to use the glycans derived from lactoferrin as a carbon source indicating that they could be used as nutrients in vivo when no other preferred carbon source is available. This report adds important information about the enzymatic activity of EndoE from the commensal and opportunist E. faecalis. The activity on the human glycoprotein hLF, and the functional consequences with reduced inhibition of biofilm formation highlights both innate immunity functions of hLF and a bacterial mechanism to evade this innate immunity function. Taken together, our results underline the importance of glycans in the interplay between bacteria and the human host, with possible implications for both commensalism and opportunism.

Indexed as

Bacterial ProteinsBiofilmsCarbohydrate SequenceEnterococcus faecalisEscherichia coliHumansHydrolysisLactoferrinMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseMolecular Sequence DataPhosphopyruvate HydratasePolysaccharidesProtein BindingRecombinant ProteinsBacterial ProteinsLactoferrinMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidasePhosphopyruvate HydratasePolysaccharidesRecombinant Proteins

Identifiers

PMID24608122
PMCPMC3946673
OpenAlexW2095310851

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.