Asset Details
Do you wish to reserve the book?
Structure, function, and evolution of Gga -AvBD11, the archetype of the structural avian-double-β-defensin family
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Structure, function, and evolution of Gga -AvBD11, the archetype of the structural avian-double-β-defensin family
Do you wish to request the book?
Structure, function, and evolution of Gga -AvBD11, the archetype of the structural avian-double-β-defensin family
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Structure, function, and evolution of Gga -AvBD11, the archetype of the structural avian-double-β-defensin family
2020
Overview
Out of the 14 avian β-defensins identified in the Gallus gallus genome, only 3 are present in the chicken egg, including the egg-specific avian β-defensin 11 (Gga-AvBD11). Given its specific localization and its established antibacterial activity, Gga-AvBD11 appears to play a protective role in embryonic development. Gga-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 Gga-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 AvBD11 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 Gga-AvBD11 displays antimicrobial activities against gram-positive and gram-negative bacterial pathogens, the avian protozoan Eimeria tenella, and avian influenza virus. Gga-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 Gga-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.
Publisher
National Academy of Sciences,CCSD
Subject
/ Animals
/ Avian Proteins - ultrastructure
/ Bacterial Infections - immunology
/ Bacterial Infections - microbiology
/ Bacterial Infections - veterinary
/ Chick Embryo - growth & development
/ Chickens
/ Domains
/ Eimeria tenella - immunology
/ Embryonic Development - immunology
/ Embryos
/ Genome
/ Genomes
/ Influenza A Virus, H1N1 Subtype - immunology
/ Influenza in Birds - immunology
/ Influenza in Birds - virology
/ NMR
/ Nuclear Magnetic Resonance, Biomolecular
/ Peptides
/ Protein Domains - immunology
/ Protozoa
/ Structure-function relationships
/ Toxicity
/ Viruses
ISBN
0005060012000
