The Greater Celandine: Identification and characterization of a novel antimicrobial peptide sequence from Chelidonium majus

ABSTRACT: A highly abundant, cysteine-rich peptide, deemed CM-AMP1, is characterized through multiple mass spectrometric approaches. Complimentary CID and EAD fragmentation types are used to gain full sequence coverage of the full-length peptide. CM-AMP1 shares little sequence similarity to any proteins in publicly available databases, highlighting the novelty of its cysteine landscape and core motif. The presence of three disulfide bonds in the native peptide confers proteolytic stability, and antimicrobial activity is greatly decreased upon alkylation of the cysteine residues. Synthetic variants of CM-AMP1 are used to confirm activity of the full-length sequence and the core motif. To assess the biological impact, E. coli was grown in a sub-lethal concentration of CM-AMP1 and quantitative proteomics was used to identify proteins produced by the bacteria under stress, ultimately suggesting a membrane lytic antimicrobial mechanism of action. This study integrates multiple analytical methods for molecular and biological characterization of a unique antimicrobial peptide identified from C. majus.

INSTRUMENT(S): AB SCIEX instrument model

ORGANISM(S): Chelidonium Majus Escherichia Coli

TISSUE(S): Plant Cell, Cell Culture, Leaf

SUBMITTER: Leslie Hicks  

LAB HEAD: Leslie Hicks

PROVIDER: PXD045877 | Pride | 2024-01-27

REPOSITORIES: Pride