Fungal effector Ecp6 outcompetes host immune receptor for chitin binding through intrachain LysM dimerization

Andrea Sánchez-Vallet1, Raspudin Saleem-Batcha, Anja Kombrink

  • 1Centro de Biotecnología y Genómica de Plantas , Universidad Politécnica de Madrid , Madrid , Spain ; Laboratory of Phytopathology , Wageningen University , Wageningen , Netherlands.

Elife
|July 11, 2013
PubMed

Insights

Fungal LysM effectors, like Ecp6, bind chitin with ultra-high affinity using a unique dimerization mechanism. This prevents host immune detection, revealing a novel fungal immune evasion strategy.

Area of Science:

  • Plant-pathogen interactions
  • Molecular mechanisms of immunity
  • Fungal biology

Background:

  • Pathogens secrete effectors to evade host immunity.
  • Fungal LysM effectors bind chitin, a component of fungal cell walls.
  • The precise mechanism of LysM effector chitin binding and immune interference was unclear.

Purpose of the Study:

  • To elucidate the structural mechanism of chitin binding by the fungal LysM effector Ecp6.
  • To understand how Ecp6 competes with host immune receptors for chitin recognition.
  • To investigate the role of individual LysM domains in Ecp6 function.

Main Methods:

  • X-ray crystallography to determine the structure of Ecp6.
  • Biochemical assays to measure chitin-binding affinity.
  • Functional studies to assess Ecp6's impact on chitin-triggered immunity.

Main Results:

  • Ecp6 utilizes intrachain LysM dimerization to form a composite, deeply buried chitin-binding groove with ultra-high (pM) affinity.
  • Two LysM domains are involved in this high-affinity binding.
  • A separate LysM domain binds chitin with lower affinity (µM) but still perturbs host immunity, likely via non-sequestration mechanisms.

Conclusions:

  • Fungal LysM effectors have evolved sophisticated mechanisms for high-affinity chitin binding to evade host immunity.
  • Ecp6's composite binding site represents a novel mode of effector-mediated immune suppression.
  • The dual-affinity binding of Ecp6 suggests complex strategies for fungal pathogenesis and host immune interference.

Related Concept Videos

Antifungal Agents01:15

Antifungal Agents

Amphotericin B is a broad-spectrum antifungal agent that exploits structural differences between fungal and mammalian cell membranes. Its amphipathic structure—featuring a hydrophobic polyene-lactone ring and a hydrophilic region containing mycosamine and carboxylic acid groups—enables selective binding to ergosterol, a sterol predominantly found in fungal plasma membranes. This selective interaction underlies the drug’s antifungal activity, although weak binding to cholesterol contributes to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Yeast Signaling01:28

Yeast Signaling

Yeasts are single-celled organisms, but unlike bacteria, they are eukaryotes (cells with a nucleus). Cell signaling in yeast is similar to signaling in other eukaryotic cells. A ligand, such as a protein or a small molecule released from a yeast cell, attaches to a receptor on the cell surface. The binding stimulates second-messenger kinases to activate or inactivate transcription factors that further regulate gene expression. Many of the yeast intracellular signaling cascades have similar...
Chromatin Immunoprecipitation- ChIP02:36

Chromatin Immunoprecipitation- ChIP

Chromatin immunoprecipitation, or ChIP, is an antibody-based technique used to identify sites on DNA that bind to transcription factors of interest or histone proteins. It also helps determine the type of histone modifications such as acetylation, phosphorylation, or methylation.
Types of ChIP
ChIP can be divided into two types - X-ChIP and N-ChIP. X-ChIP involves in vivo cross-linking of histones and regulatory proteins to DNA, fragmenting the DNA by sonication, and isolating the protein-DNA...
Receptor-mediated Endocytosis01:38

Receptor-mediated Endocytosis

Overview