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Biochemical and biophysical research communications2015; 459(4); 668-672; doi: 10.1016/j.bbrc.2015.02.168

Solution structure and functional studies of the highly potent equine antimicrobial peptide DEFA1.

Abstract: Defensins are small effector molecules of the innate immune system that are present in almost all organisms including plants and animals. These peptides possess antimicrobial activity against a broad range of microbes including bacteria, fungi and viruses and act as endogenous antibiotics. α-Defensins are a subfamily of the defensin family and their expression is limited to specific tissues. Equine DEFA1 is an enteric α-defensin exclusively secreted by Paneth cells and shows an activity against a broad spectrum of microbes, including typical pathogens of the horse such as Rhodococcus equi, various streptococci strains, Salmonella choleraesuis, and Pasteurella multocida. Here, we report the three-dimensional structure of DEFA1 solved by NMR-spectroscopy and demonstrate its specific function of aggregating various phospholipids.
Publication Date: 2015-03-11 PubMed ID: 25769951DOI: 10.1016/j.bbrc.2015.02.168Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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This research focuses on understanding the structure and function of an equine antimicrobial peptide, DEFA1, which is known for its potent activity against a broad range of horse pathogens.

Understanding DEFA1

  • The research revolves around the study of Defensins, which are small molecules responsible for the innate immune system in all organisms, including plants and animals.
  • Defensins are known to possess antimicrobial activity, and they have the ability to fight a wide variety of microbes, such as bacteria, fungi and viruses, essentially functioning as internal antibiotics.
  • A particular subfamily of the defensin family, known as α-Defensins, has its expression limited to specific tissues only.

Role of Equine DEFA1

  • The study specifically focuses on Equine DEFA1, an enteric α-defensin, which is secreted exclusively by a type of small intestinal cell called Paneth cells.
  • DEFA1 is known for its capability to act against a wide spectrum of microbes, particularly the pathogens known to affect horses such as Rhodococcus equi, various strains of streptococci, Salmonella choleraesuis, and Pasteurella multocida.

NMR-spectroscopy and Functional Studies

  • Through Nuclear Magnetic Resonance (NMR) spectroscopy, the researchers were able to solve the three-dimensional structure of DEFA1, providing crucial insight into its configuration and working mechanisms.
  • Further, the study successfully demonstrates DEFA1’s specific functionality of aggregating various phospholipids, adding to the understanding of this antimicrobial peptide’s action.

Cite This Article

APA
Michalek M, Jung S, Shomali MR, Cauchard S, Sönnichsen FD, Grötzinger J. (2015). Solution structure and functional studies of the highly potent equine antimicrobial peptide DEFA1. Biochem Biophys Res Commun, 459(4), 668-672. https://doi.org/10.1016/j.bbrc.2015.02.168

Publication

ISSN: 1090-2104
NlmUniqueID: 0372516
Country: United States
Language: English
Volume: 459
Issue: 4
Pages: 668-672
PII: S0006-291X(15)00424-6

Researcher Affiliations

Michalek, Matthias
  • Institute of Biochemistry, Christian-Albrechts-Universität zu Kiel, Olshausenstr. 40, 24098 Kiel, Germany.
Jung, Sascha
  • Institute of Biochemistry, Christian-Albrechts-Universität zu Kiel, Olshausenstr. 40, 24098 Kiel, Germany.
Shomali, Mohammad R
  • Institute of Biochemistry, Christian-Albrechts-Universität zu Kiel, Olshausenstr. 40, 24098 Kiel, Germany.
Cauchard, Severine
  • ANSES, Dozulé Laboratory for Equine Diseases, Bacteriology and Parasitology Unit, 14430 Goustranville, France.
Sönnichsen, Frank D
  • Otto Diels Institute of Organic Chemistry, Christian-Albrechts-Universität zu Kiel, Olshausenstr. 40, 24098 Kiel, Germany.
Grötzinger, Joachim
  • Institute of Biochemistry, Christian-Albrechts-Universität zu Kiel, Olshausenstr. 40, 24098 Kiel, Germany. Electronic address: jgroetzinger@biochem.uni-kiel.de.

MeSH Terms

  • Animals
  • Nuclear Magnetic Resonance, Biomolecular
  • Spectrometry, Fluorescence
  • Structure-Activity Relationship
  • alpha-Defensins / chemistry
  • alpha-Defensins / pharmacology

Citations

This article has been cited 2 times.
  1. Cui C, Li L, Wu L, Wang X, Zheng Y, Wang F, Wei H, Peng J. Paneth cells in farm animals: current status and future direction.. J Anim Sci Biotechnol 2023 Aug 15;14(1):118.
    doi: 10.1186/s40104-023-00905-5pubmed: 37582766google scholar: lookup
  2. Passarini I, Rossiter S, Malkinson J, Zloh M. In Silico Structural Evaluation of Short Cationic Antimicrobial Peptides.. Pharmaceutics 2018 Jun 21;10(3).
    doi: 10.3390/pharmaceutics10030072pubmed: 29933540google scholar: lookup