6QEU

Gga-AvBD11 (Avian beta-defensin 11 from Gallus gallus)

Summary for 6QEU

• Entry DOI: 10.2210/pdb6qeu/pdb
• NMR Information: BMRB: 34350
• Descriptor: Gallinacin-11 (1 entity in total)
• Functional Keywords: new fold, double beta-defensin, defensin, avian egg, antimicrobial protein
• Biological source: Gallus gallus (Chicken)
• Total number of polymer chains: 1
• Total formula weight: 9304.90

Authors

Meudal, H.,Loth, K.,Delmas, A.F.,Landon, C. (deposition date: 2019-01-08, release date: 2019-12-18, Last modification date: 2024-11-06)

Primary citation

Guyot, N.,Meudal, H.,Trapp, S.,Iochmann, S.,Silvestre, A.,Jousset, G.,Labas, V.,Reverdiau, P.,Loth, K.,Herve, V.,Aucagne, V.,Delmas, A.F.,Rehault-Godbert, S.,Landon, C.
Structure, function, and evolution ofGga-AvBD11, the archetype of the structural avian-double-beta-defensin family.
Proc.Natl.Acad.Sci.USA, 117:337-345, 2020

PubMed Abstract: Out of the 14 avian β-defensins identified in the genome, only 3 are present in the chicken egg, including the egg-specific avian β-defensin 11 (-AvBD11). Given its specific localization and its established antibacterial activity, -AvBD11 appears to play a protective role in embryonic development. -AvBD11 is an atypical double-sized defensin, predicted to possess 2 motifs related to β-defensins and 6 disulfide bridges. The 3-dimensional NMR structure of the purified AvBD11 is a compact fold composed of 2 packed β-defensin domains. This fold is the archetype of a structural family, dubbed herein as avian-double-β-defensins (Av-DBD). We speculate that emanated from a monodomain gene ancestor and that similar events might have occurred in arthropods, leading to another structural family of less compact DBDs. We show that -AvBD11 displays antimicrobial activities against gram-positive and gram-negative bacterial pathogens, the avian protozoan , and avian influenza virus. -AvBD11 also shows cytotoxic and antiinvasive activities, suggesting that it may not only be involved in innate protection of the chicken embryo, but also in the (re)modeling of embryonic tissues. Finally, the contribution of either of the 2 -AvBD11 domains to these biological activities was assessed, using chemically synthesized peptides. Our results point to a critical importance of the cationic N-terminal domain in mediating antibacterial, antiparasitic, and antiinvasive activities, with the C-terminal domain potentiating the 2 latter activities. Strikingly, antiviral activity in infected chicken cells, accompanied by marked cytotoxicity, requires the full-length protein.

PubMed: 31871151
DOI: 10.1073/pnas.1912941117

Experimental method

SOLUTION NMR