5XDI

Vaccatide: Antifungal Glutamine-rich 8C-Hevein-like Peptide, vH1

Summary for 5XDI

• Entry DOI: 10.2210/pdb5xdi/pdb
• NMR Information: BMRB: 36068
• Descriptor: Vaccatide, vH1 (1 entity in total)
• Functional Keywords: hevein-like peptide, cystein, antifungal, vaccaria hispanica, antifungal protein
• Biological source: Vaccaria hispanica
• Total number of polymer chains: 1
• Total formula weight: 4087.57

Authors

Xiao, T.,Tam, J.P. (deposition date: 2017-03-28, release date: 2017-07-19, Last modification date: 2024-10-30)

Primary citation

Wong, K.H.,Tan, W.L.,Kini, S.G.,Xiao, T.,Serra, A.,Sze, S.K.,Tam, J.P.
Vaccatides: Antifungal Glutamine-Rich Hevein-Like Peptides from Vaccaria hispanica
Front Plant Sci, 8:1100-1100, 2017

PubMed Abstract: Hevein and hevein-like peptides are disulfide-constrained chitin-binding cysteine-rich peptides. They are divided into three subfamilies, 6C-, 8C-, and 10C-hevein-like peptides, based on the number of cysteine residues. In addition, hevein-like peptides can exist in two forms, short and long. The long C-terminal form found in hevein and 10C-hevein-like peptides contain a C-terminal protein cargo. In contrast, the short form without a protein cargo is found in all three subfamilies. Here, we report the discovery and characterization of two novel glutamine-rich and protein cargo-free 8C-hevein-like peptides, vaccatides vH1 and vH2, from of the Caryophyllaceae family. Proteomic analyses showed that the vaccatides are 40-41 amino acids in length and contain a chitin-binding domain. NMR determination revealed that vaccatide vH2 displays a highly compact structure with a N-terminal cystine knot and an addition C-terminal disulfide bond. Stability studies showed that this compact structure renders vaccatide vH2 resistant to thermal, chemical and proteolytic degradation. The chitin-binding vH2 was shown to inhibit the mycelium growth of four phyto-pathogenic fungal strains with IC values in the micromolar range. Our findings show that vaccatides represent a new family of 8C-hevein-like peptides, which are protein cargo-free and glutamine-rich, characteristics that differentiate them from the prototypic hevein and the 10C-hevein-like peptides. In summary, this study enriches the existing library of hevein-like peptides and provides insight into their molecular diversity in sequence, structure and biosynthesis. Additionally, their highly disulfide-constrained structure could be used as a scaffold for developing metabolically and orally active peptidyl therapeutics.

PubMed: 28680440
DOI: 10.3389/fpls.2017.01100

Experimental method

SOLUTION NMR