Morintides: cargo-free chitin-binding peptides from Moringa oleifera

BMC Plant Biol. 2017 Mar 31;17(1):68. doi: 10.1186/s12870-017-1014-6.

Abstract

Background: Hevein-like peptides are a family of cysteine-rich and chitin-binding peptides consisting of 29-45 amino acids. Their chitin-binding property is essential for plant defense against fungi. Based on the number of cysteine residues in their sequences, they are divided into three sub-families: 6C-, 8C- and 10C-hevein-like peptides. All three subfamilies contain a three-domain precursor comprising a signal peptide, a mature hevein-like peptide and a C-terminal domain comprising a hinge region with protein cargo in 8C- and 10C-hevein-like peptides.

Results: Here we report the isolation and characterization of two novel 8C-hevein-like peptides, designated morintides (mO1 and mO2), from the drumstick tree Moringa oleifera, a drought-resistant tree belonging to the Moringaceae family. Proteomic analysis revealed that morintides comprise 44 amino acid residues and are rich in cysteine, glycine and hydrophilic amino acid residues such as asparagine and glutamine. Morintides are resistant to thermal and enzymatic degradation, able to bind to chitin and inhibit the growth of phyto-pathogenic fungi. Transcriptomic analysis showed that they contain a three-domain precursor comprising an endoplasmic reticulum (ER) signal sequence, a mature peptide domain and a C-terminal domain. A striking feature distinguishing morintides from other 8C-hevein-like peptides is a short and protein-cargo-free C-terminal domain. Previously, a similar protein-cargo-free C-terminal domain has been observed only in ginkgotides, the 8C-hevein-like peptides from a gymnosperm Ginkgo biloba. Thus, morintides, with a cargo-free C-terminal domain, are a stand-alone class of 8C-hevein-like peptides from angiosperms.

Conclusions: Our results expand the existing library of hevein-like peptides and shed light on molecular diversity within the hevein-like peptide family. Our work also sheds light on the anti-fungal activity and stability of 8C-hevein-like peptides.

Keywords: Anti-fungal; Chitin-binding; Cysteine-rich peptides; Hevein; Hevein-like peptides; Moringa oleifera.

MeSH terms

  • Animals
  • Antifungal Agents / chemistry
  • Antifungal Agents / pharmacology
  • Antimicrobial Cationic Peptides / chemistry
  • Chitin / metabolism*
  • Chlorocebus aethiops
  • Drug Evaluation, Preclinical / methods
  • Microbial Sensitivity Tests
  • Moringa oleifera / chemistry*
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptides / chemistry
  • Peptides / genetics
  • Peptides / metabolism*
  • Peptides / pharmacology*
  • Phylogeny
  • Plant Lectins / chemistry
  • Plant Proteins / chemistry
  • Plant Proteins / genetics
  • Plant Proteins / metabolism*
  • Protein Stability
  • Vero Cells

Substances

  • Antifungal Agents
  • Antimicrobial Cationic Peptides
  • Peptides
  • Plant Lectins
  • Plant Proteins
  • hevein
  • Chitin