Structural characterization of nodule-specific cysteine-rich antifungal peptides and their phospholipid receptors for elucidation of their modes of action
EMSL Project ID
50739
Abstract
Antimicrobial peptides (AMPs) are a major component of innate immunity against infectious diseases in animals and plants [2]. A feature prominent in many families of AMPs, such as defensins (Figure 1), is disulfide covalent crosslinks between pairs of cysteine residues to give these peptides unique shapes important for their function and to make them extremely resistant to proteolysis. The properties afforded by the disulfide bonds in these "natural drugs" have been identified as a key component in the de novo design of a new generation of hyperstable peptide-based drugs [3]. In Medicago species of leguminous plants, AMPs have evolved to control nitrogen-fixing bacteria in a symbiosis within specialized root organs called nodules. We have discovered that a subset of these nodule-specific cysteine-rich (NCR) peptides (NCR1, NCR2, and NCR13) exhibit potent antifungal activity in vitro against a broad range of economically important plant pathogenic fungi. Critical issues which need to be addressed are the molecular modes of action (MOA) used by these peptides to kill fungi and to fine-tune commensal and symbiotic interactions with bacterial populations. The structure of these peptides and their interactions with phospholipids on the surface of fungi and bacteria are likely crucial features of their MOAs. We propose to decipher the MOAs of NCR1, NCR2, and NCR13 through structural analyses using NMR and mass spectrometry.
Project Details
Project type
Large-Scale EMSL Research
Start Date
2019-10-01
End Date
2021-09-30
Status
Closed
Released Data Link
Team
Principal Investigator
Team Members