Anchorless surface associated glycolytic enzymes from Lactobacillus plantarum 299v bind to epithelial cells and extracellular matrix proteins
(2013) In Microbiological Research 168(5). p.245-253- Abstract
- An important criterion for the selection of a probiotic bacterial strain is its ability to adhere to the mucosal surface. Adhesion is usually mediated by proteins or other components located on the outer cell surface of the bacterium. In the present study we characterized the adhesive properties of two classical intracellular enzymes glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and enolase (ENO) isolated from the outer cell surface of the probiotic bacterium Lactobacillus plantarum 299v. None of the genes encoded signal peptides or cell surface anchoring motifs that could explain their extracellular location on the bacterial surface. The presence of the glycolytic enzymes on the outer surface was verified by western blotting using... (More)
- An important criterion for the selection of a probiotic bacterial strain is its ability to adhere to the mucosal surface. Adhesion is usually mediated by proteins or other components located on the outer cell surface of the bacterium. In the present study we characterized the adhesive properties of two classical intracellular enzymes glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and enolase (ENO) isolated from the outer cell surface of the probiotic bacterium Lactobacillus plantarum 299v. None of the genes encoded signal peptides or cell surface anchoring motifs that could explain their extracellular location on the bacterial surface. The presence of the glycolytic enzymes on the outer surface was verified by western blotting using polyclonal antibodies raised against the specific enzymes. GAPDH and ENO showed a highly specific binding to plasminogen and fibronectin whereas GAPDH but not ENO showed weak binding to mucin. Furthermore, a pH dependent and specific binding of GAPDH and ENO to intestinal epithelial Caco-2 cells at pH 5 but not at pH 7 was demonstrated. The results showed that these glycolytic enzymes could play a role in the adhesion of the probiotic bacterium L. plantarum 299v to the gastrointestinal tract of the host. Finally, a number of probiotic as well non-probiotic Lactobacillus strains were analyzed for the presence of GAPDH and ENO on the outer surface, but no correlation between the extracellular location of these enzymes and the probiotic status of the applied strains was demonstrated. (c) 2013 Elsevier GmbH. All rights reserved. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3930470
- author
- Glenting, Jacob ; Beck, Hans Christian ; Vrang, Astrid ; Riemann, Holger ; Ravn, Peter ; Hansen, Anne Maria ; Antonsson, Martin ; Ahrné, Siv LU ; Israelsen, Hans and Madsen, Soren
- organization
- publishing date
- 2013
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Lactobacillus plantarum strain 299v, Glyceraldehyde 3-phosphate, dehydrogenase, Enolase, Surface enzymes, Probiotics
- in
- Microbiological Research
- volume
- 168
- issue
- 5
- pages
- 245 - 253
- publisher
- Urban & Fischer Verlag
- external identifiers
-
- wos:000320074200001
- scopus:84876410923
- pmid:23395591
- ISSN
- 1618-0623
- DOI
- 10.1016/j.micres.2013.01.003
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Applied Nutrition and Food Chemistry (011001300)
- id
- 15f3391d-71d9-4e38-add0-93b7089fced0 (old id 3930470)
- date added to LUP
- 2016-04-01 14:50:19
- date last changed
- 2023-11-13 13:03:12
@article{15f3391d-71d9-4e38-add0-93b7089fced0,
abstract = {{An important criterion for the selection of a probiotic bacterial strain is its ability to adhere to the mucosal surface. Adhesion is usually mediated by proteins or other components located on the outer cell surface of the bacterium. In the present study we characterized the adhesive properties of two classical intracellular enzymes glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and enolase (ENO) isolated from the outer cell surface of the probiotic bacterium Lactobacillus plantarum 299v. None of the genes encoded signal peptides or cell surface anchoring motifs that could explain their extracellular location on the bacterial surface. The presence of the glycolytic enzymes on the outer surface was verified by western blotting using polyclonal antibodies raised against the specific enzymes. GAPDH and ENO showed a highly specific binding to plasminogen and fibronectin whereas GAPDH but not ENO showed weak binding to mucin. Furthermore, a pH dependent and specific binding of GAPDH and ENO to intestinal epithelial Caco-2 cells at pH 5 but not at pH 7 was demonstrated. The results showed that these glycolytic enzymes could play a role in the adhesion of the probiotic bacterium L. plantarum 299v to the gastrointestinal tract of the host. Finally, a number of probiotic as well non-probiotic Lactobacillus strains were analyzed for the presence of GAPDH and ENO on the outer surface, but no correlation between the extracellular location of these enzymes and the probiotic status of the applied strains was demonstrated. (c) 2013 Elsevier GmbH. All rights reserved.}},
author = {{Glenting, Jacob and Beck, Hans Christian and Vrang, Astrid and Riemann, Holger and Ravn, Peter and Hansen, Anne Maria and Antonsson, Martin and Ahrné, Siv and Israelsen, Hans and Madsen, Soren}},
issn = {{1618-0623}},
keywords = {{Lactobacillus plantarum strain 299v; Glyceraldehyde 3-phosphate; dehydrogenase; Enolase; Surface enzymes; Probiotics}},
language = {{eng}},
number = {{5}},
pages = {{245--253}},
publisher = {{Urban & Fischer Verlag}},
series = {{Microbiological Research}},
title = {{Anchorless surface associated glycolytic enzymes from Lactobacillus plantarum 299v bind to epithelial cells and extracellular matrix proteins}},
url = {{http://dx.doi.org/10.1016/j.micres.2013.01.003}},
doi = {{10.1016/j.micres.2013.01.003}},
volume = {{168}},
year = {{2013}},
}