5LCS

NMR structure of Chicken AvBD7 defensin

5LCS の概要

• エントリーDOI: 10.2210/pdb5lcs/pdb
• NMR情報: BMRB: 34014
• 分子名称: Gallinacin-7 (1 entity in total)
• 機能のキーワード: avian defensin, antimicrobial peptide, immune system
• 由来する生物種: Gallus gallus (Chicken)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5366.27

構造登録者

Landon, C.,Loth, K.,Meudal, H. (登録日: 2016-06-22, 公開日: 2016-09-07, 最終更新日: 2024-10-16)

主引用文献

Bailleul, G.,Kravtzoff, A.,Joulin-Giet, A.,Lecaille, F.,Labas, V.,Meudal, H.,Loth, K.,Teixeira-Gomes, A.P.,Gilbert, F.B.,Coquet, L.,Jouenne, T.,Bromme, D.,Schouler, C.,Landon, C.,Lalmanach, G.,Lalmanach, A.C.
The Unusual Resistance of Avian Defensin AvBD7 to Proteolytic Enzymes Preserves Its Antibacterial Activity.
Plos One, 11:e0161573-e0161573, 2016

PubMed Abstract: Defensins are frontline peptides of mucosal immunity in the animal kingdom, including birds. Their resistance to proteolysis and their ensuing ability to maintain antimicrobial potential remains questionable and was therefore investigated. We have shown by bottom-up mass spectrometry analysis of protein extracts that both avian beta-defensins AvBD2 and AvBD7 were ubiquitously distributed along the chicken gut. Cathepsin B was found by immunoblotting in jejunum, ileum, caecum, and caecal tonsils, while cathepsins K, L, and S were merely identified in caecal tonsils. Hydrolysis product of AvBD2 and AvBD7 incubated with a panel of proteases was analysed by RP-HPLC, mass spectrometry and antimicrobial assays. AvBD2 and AvBD7 were resistant to serine proteases and to cathepsins D and H. Conversely cysteine cathepsins B, K, L, and S degraded AvBD2 and abolished its antibacterial activity. Only cathepsin K cleaved AvBD7 and released Ile4-AvBD7, a N-terminal truncated natural peptidoform of AvBD7 that displayed antibacterial activity. Besides the 3-stranded antiparallel beta-sheet typical of beta-defensins, structural analysis of AvBD7 by two-dimensional NMR spectroscopy highlighted the restricted accessibility of the C-terminus embedded by the N-terminal region and gave a formal evidence of a salt bridge (Asp9-Arg12) that could account for proteolysis resistance. The differential susceptibility of avian defensins to proteolysis opens intriguing questions about a distinctive role in the mucosal immunity against pathogen invasion.

PubMed: 27561012
DOI: 10.1371/journal.pone.0161573

実験手法

SOLUTION NMR