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Structural Insight into Fungal Cell Wall Recognition by a CVNH Protein with a Single LysM Domain

Leonardus M I Koharudin1, Karl T Debiec1, Angela M Gronenborn1

  • 1Department of Structural Biology, University of Pittsburgh School of Medicine, 3501 Fifth Avenue, Pittsburgh, PA 15260, USA.

Structure (London, England : 1993)
|October 13, 2015
PubMed

Insights

Magnaporthe oryzae lectin MGG_03307 uses its CVNH-LysM module to bind N-acetylglucosamine (GlcNAc) oligomers. This binding involves conformational changes and reveals a specific consensus mode for LysM domain recognition.

Area of Science:

  • Structural biology
  • Mycology
  • Plant pathology

Background:

  • MGG_03307 is a lectin from Magnaporthe oryzae, a fungus causing rice blast.
  • This lectin aids M. oryzae in evading plant immune responses.

Purpose of the Study:

  • To elucidate the structural basis of MGG_03307's protective function.
  • To understand how MGG_03307 interacts with N-acetylglucosamine (GlcNAc) containing chitin.

Main Methods:

  • X-ray crystallography was used to determine the structure of the CVNH-LysM module.
  • Solution nuclear magnetic resonance (NMR) studies investigated GlcNAc binding.

Main Results:

  • Crystal structures revealed conformational changes in the LysM domain upon GlcNAc binding.
  • GlcNAc3-6 were accommodated differently, with GlcNAc5 and GlcNAc6 showing multiple conformations.
  • Unlike other LysM proteins, MGG_03307 did not dimerize upon GlcNAc6 binding.
  • A consensus binding mode for GlcNAc oligomer recognition by single LysM domains was defined.

Conclusions:

  • MGG_03307 exhibits a unique GlcNAc binding mechanism.
  • The findings provide insights into fungal immune evasion strategies.
  • This study defines a specific binding mode for LysM domains recognizing chitin oligomers.
Keywords:
ChitinLysM domainNMRProtein-carbohydrate complexX-ray crystallography

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