2N2R

NMR solution structure of RsAFP2

2N2R の概要

• エントリーDOI: 10.2210/pdb2n2r/pdb
• 関連するPDBエントリー: 2N2Q
• NMR情報: BMRB: 25609
• 分子名称: Defensin-like protein 2 (1 entity in total)
• 機能のキーワード: antifungal protein
• 由来する生物種: Raphanus sativus (Radish)
• 細胞内の位置: Secreted: P30230
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5744.69

構造登録者

Harvey, P.J.,Craik, D.J.,Vriens, K. (登録日: 2015-05-12, 公開日: 2016-05-25, 最終更新日: 2024-10-16)

主引用文献

Vriens, K.,Cools, T.L.,Harvey, P.J.,Craik, D.J.,Braem, A.,Vleugels, J.,De Coninck, B.,Cammue, B.P.,Thevissen, K.
The radish defensins RsAFP1 and RsAFP2 act synergistically with caspofungin against Candida albicans biofilms.
Peptides, 75:71-79, 2016

PubMed Abstract: The radish defensin RsAFP2 was previously characterized as a peptide with potent antifungal activity against several plant pathogenic fungi and human pathogens, including Candida albicans. RsAFP2 induces apoptosis and impairs the yeast-to-hypha transition in C. albicans. As the yeast-to-hypha transition is considered important for progression to mature biofilms, we analyzed the potential antibiofilm activity of recombinant (r)RsAFP2, heterologously expressed in Pichia pastoris, against C. albicans biofilms. We found that rRsAFP2 prevents C. albicans biofilm formation with a BIC-2 (i.e., the minimal rRsAFP2 concentration that inhibits biofilm formation by 50% as compared to control treatment) of 1.65 ± 0.40 mg/mL. Moreover, biofilm-specific synergistic effects were observed between rRsAFP2 doses as low as 2.5 μg/mL to 10 μg/mL and the antimycotics caspofungin and amphotericin B, pointing to the potential of RsAFP2 as a novel antibiofilm compound. In addition, we characterized the solution structure of rRsAFP2 and compared it to that of RsAFP1, another defensin present in radish seeds. These peptides have similar amino acid sequences, except for two amino acids, but rRsAFP2 is more potent than RsAFP1 against planktonic and biofilm cultures. Interestingly, as in case of rRsAFP2, also RsAFP1 acts synergistically with caspofungin against C. albicans biofilms in a comparable low dose range as rRsAFP2. A structural comparison of both defensins via NMR analysis revealed that also rRsAFP2 adopts the typical cysteine-stabilized αβ-motif of plant defensins, however, no structural differences were found between these peptides that might result in their differential antifungal/antibiofilm potency. This further suggests that the conserved structure of RsAFP1 and rRsAFP2 bears the potential to synergize with antimycotics against C. albicans biofilms.

PubMed: 26592804
DOI: 10.1016/j.peptides.2015.11.001

実験手法

SOLUTION NMR