EndoE from Enterococcus faecalis Hydrolyzes the Glycans of the Biofilm Inhibiting Protein Lactoferrin and Mediates Growth.
Garbe, Julia LU ; Sjögren, Jonathan LU ; Cosgrave, Eoin F J ; Struwe, Weston B ; Bober, Marta LU ; Olin, Anders LU ; Rudd, Pauline M and Collin, Mattias LU
(2014)
In PLoS ONE
9(3).
- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4383664
- author
- Garbe, Julia
LU
; Sjögren, Jonathan
LU
; Cosgrave, Eoin F J
; Struwe, Weston B
; Bober, Marta
LU
; Olin, Anders
LU
; Rudd, Pauline M
and Collin, Mattias
LU
- organization
- publishing date
- 2014
- type
- Contribution to journal
- publication status
- published
- subject
- in
- PLoS ONE
- volume
- 9
- issue
- 3
- article number
- e91035
- publisher
- Public Library of Science (PLoS)
- external identifiers
-
- pmid:24608122
- wos:000332485800085
- scopus:84897394119
- pmid:24608122
- ISSN
- 1932-6203
- DOI
- 10.1371/journal.pone.0091035
- language
- English
- LU publication?
- yes
- id
- 243c5285-47e8-4dce-9321-5656dcb2cbb9 (old id 4383664)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/24608122?dopt=Abstract
- date added to LUP
- 2016-04-01 13:44:09
- date last changed
- 2022-11-24 08:18:26
@article{243c5285-47e8-4dce-9321-5656dcb2cbb9,
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.}},
author = {{Garbe, Julia and Sjögren, Jonathan and Cosgrave, Eoin F J and Struwe, Weston B and Bober, Marta and Olin, Anders and Rudd, Pauline M and Collin, Mattias}},
issn = {{1932-6203}},
language = {{eng}},
number = {{3}},
publisher = {{Public Library of Science (PLoS)}},
series = {{PLoS ONE}},
title = {{EndoE from Enterococcus faecalis Hydrolyzes the Glycans of the Biofilm Inhibiting Protein Lactoferrin and Mediates Growth.}},
url = {{https://lup.lub.lu.se/search/files/3559469/4644688}},
doi = {{10.1371/journal.pone.0091035}},
volume = {{9}},
year = {{2014}},
}