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Species-specific and pathotype-specific binding of bacteria to zymogen granule membrane glycoprotein 2 (GP2)
Gut
  • Peter Schierack, Brandenburgische Technische Universität Cottbus-Senftenberg
  • Stefan Rödiger, Brandenburgische Technische Universität Cottbus-Senftenberg
  • Rafal Kolenda, Brandenburgische Technische Universität Cottbus-Senftenberg
  • Rico Hiemann, Brandenburgische Technische Universität Cottbus-Senftenberg
  • Enrico Berger, Brandenburgische Technische Universität Cottbus-Senftenberg
  • Krzysztof Grzymajło, Uniwersytet Przyrodniczy we Wrocławiu
  • Alexander Swidsinski, Charité Humboldt Universität
  • Thomas Juretzek, Carl-Thiem-Klinikum
  • Dirk Meissner, Labor Hameln Hildesheim
  • Karsten Mydlak, Gemeinschaftslabor Cottbus
  • Dirk Reinhold, Otto-von-Guericke-Universität Magdeburg
  • Lisa K. Nolan, Iowa State University
  • Dirk Roggenbuck, GA Generic Assays GmbH
Document Type
Letter to the Editor
Publication Version
Published Version
Publication Date
3-1-2015
DOI
10.1136/gutjnl-2014-307854
Abstract
With interest we read the paper by Juste et al 1 proposing the amount of zymogen-granule membrane glycoprotein 2 (GP2) on the surface of intestinal bacteria as a Crohn's disease (CD) marker. Indeed, a decreased GP2 level was found on microbes in patients with CD as compared to those of healthy controls. GP2 is a homologue to the urinary Tamm–Horsefall protein demonstrating an antimicrobial function by binding type 1-fimbriated uropathogenic Escherichia coli (UPEC). Likewise, GP2 seems to interact with intestinal bacteria as a specific receptor of bacterial type-1 fimbriae (FimH) on intestinal microfold cells that are partaking in immune responses against such microbes.2 GP2 is overexpressed in the inflamed intestine of patients with CD and has an immunomodulating role in innate and acquired immune responses.3 ,4Interestingly, GP2 was identified as autoantigen of pancreatic antibodies in CD.4 Altogether, these findings indicate two major GP2 sources (pancreatic/intestinal) and support a role for GP2 in the interaction between the immune system and intestinal microbiota.3 Thus, loss of tolerance to GP2 could play a role in CD's pathophysiology supposed to be exacerbated by preceding intestinal infections. In general, the findings by Juste et al 1 may be explained by a lower pancreatic GP2 secretion, an impaired GP2 binding to bacteria, or by a higher prevalence of bacteria with poor or no GP2 binding in patients with CD.
Comments

This article is from Gut 64 (2015): 517–519, doi:10.1136/gutjnl-2014-307854. Posted with permission.

Rights
s This is an Open Access article distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is noncommercial. See: http://creativecommons.org/licenses/ by-nc/4.0/
Copyright Owner
The authors
Language
en
Date Available
2015-05-26
File Format
application/pdf
Citation Information
Peter Schierack, Stefan Rödiger, Rafal Kolenda, Rico Hiemann, et al.. "Species-specific and pathotype-specific binding of bacteria to zymogen granule membrane glycoprotein 2 (GP2)" Gut Vol. 64 Iss. 3 (2015) p. 517 - 519
Available at: http://works.bepress.com/lisa_nolan/88/