Next Article in Journal
Aspersymmetide A, a New Centrosymmetric Cyclohexapeptide from the Marine-Derived Fungus Aspergillus versicolor
Next Article in Special Issue
Recent Advances in Antibacterial and Antiendotoxic Peptides or Proteins from Marine Resources
Previous Article in Journal
The Oxepane Motif in Marine Drugs
Previous Article in Special Issue
Diversity and Antimicrobial Potential of Predatory Bacteria from the Peruvian Coastline
Article Menu
Issue 11 (November) cover image

Export Article

Open AccessArticle
Mar. Drugs 2017, 15(11), 362;

Antimicrobial Peptide Epinecidin-1 Modulates MyD88 Protein Levels via the Proteasome Degradation Pathway

Marine Research Station, Institute of Cellular and Organismic Biology, Academia Sinica, 23-10 Dahuen Rd., Jiaushi, Ilan 262, Taiwan
Author to whom correspondence should be addressed.
Received: 27 October 2017 / Revised: 10 November 2017 / Accepted: 14 November 2017 / Published: 16 November 2017
(This article belongs to the Special Issue Marine Antimicrobial Agents)
Full-Text   |   PDF [2312 KB, uploaded 16 November 2017]   |  


The cationic antimicrobial peptide epinecidin-1 was identified from Epinephelus coioides and possesses multiple biological functions, including antibacterial, antifungal, anti-tumor, and immunomodulatory effects. In addition, epinecidin-1 suppresses lipopolysaccharide (LPS)-induced inflammation by neutralizing LPS and ameliorating LPS/Toll-like receptor (TLR)-4 internalization. However, it is unclear whether the actions of epinecidin-1 depend on the regulation of TLR adaptor protein MyD88 or endogenous TLR signaling antagonists, which include A20, interleukin-1 receptor associated kinase (IRAK)-M, and suppressor of cytokine signaling (SOCS)-1. Our results demonstrate that epinecidin-1 alone does not affect A20, IRAK-M, or SOCS-1 protein levels. However, pre-incubation of epinecidin-1 significantly inhibits LPS-induced upregulation of A20, IRAK-M, and SOCS-1. In addition, epinecidin-1 significantly reduces the abundance of MyD88 protein. Both MG132 (a specific proteasome inhibitor) and Heclin (a specific Smurf E3 ligase inhibitor) are able to abolish epinecidin-1-mediated MyD88 degradation. Thus, our data suggest that epinecidin-1 directly inhibits MyD88 via induction of the Smurf E3 ligase proteasome pathway. View Full-Text
Keywords: epinecidin-1; MyD88; A20; IRAK-M; SOCS-1; proteasome epinecidin-1; MyD88; A20; IRAK-M; SOCS-1; proteasome

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Share & Cite This Article

MDPI and ACS Style

Su, B.-C.; Chen, J.-Y. Antimicrobial Peptide Epinecidin-1 Modulates MyD88 Protein Levels via the Proteasome Degradation Pathway. Mar. Drugs 2017, 15, 362.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Mar. Drugs EISSN 1660-3397 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top