| 词条 | Drosocin |
| 释义 |
| Symbol = Drosocin, Dro or Drc | Name = Drosocin | image = Drosophila melanogaster Proboscis.jpg | width = | caption = The fruit fly, Drosophila melanogaster | Pfam = DIM | Pfam_clan = | InterPro = | SMART = | PROSITE = | MEROPS = | SCOP = | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} Drosocin is a 19-residue long antimicrobial peptide of flies first isolated in the fruit fly Drosophila melanogaster, and later shown to be conserved throughout the genus Drosophila.[1][2] Drosocin is regulated by the NF-κB Imd signalling pathway in the fly. Structure and FunctionDrosocin is primarily active against Gram-negative bacteria. The peptide is Proline-rich with Proline-Arginine repeats, as well a critical threonine residue. This threonine is O-glycosylated, which is required for antimicrobial activity.[1] This O-glycosylation can be performed either by mono- or disaccharides, which have different activity spectra.[3] Like the antimicrobial peptides Pyrrhocoricin and Abaecin, Drosocin binds to bacterial DnaK, inhibiting cell machinery and replication.[4] The action of these Drosocin-like peptides is potentiated by the presence of pore-forming peptides, which facilitates the entry of Drosocin-like peptides into the baceterial cell.[5] Proline-rich peptides like Drosocin can also bind to microbe ribosomes, preventing protein translation.[6] In the absence of pore-forming peptides, the related AMP Pyrrhocoricin is taken into the bacteria by the action of uptake permeases.[7] References1. ^1 {{cite journal | vauthors = Bulet P, Dimarcq JL, Hetru C, Lagueux M, Charlet M, Hegy G, Van Dorsselaer A, Hoffmann JA | title = A novel inducible antibacterial peptide of Drosophila carries an O-glycosylated substitution | journal = The Journal of Biological Chemistry | volume = 268 | issue = 20 | pages = 14893–7 | date = July 1993 | pmid = 8325867 }} 2. ^{{cite journal | vauthors = Hanson MA, Hamilton PT, Perlman SJ | title = Immune genes and divergent antimicrobial peptides in flies of the subgenus Drosophila | journal = BMC Evolutionary Biology | volume = 16 | issue = 1 | pages = 228 | date = October 2016 | pmid = 27776480 | pmc = 5078906 | doi = 10.1186/s12862-016-0805-y }} 3. ^{{cite journal | vauthors = Uttenweiler-Joseph S, Moniatte M, Lagueux M, Van Dorsselaer A, Hoffmann JA, Bulet P | title = Differential display of peptides induced during the immune response of Drosophila: a matrix-assisted laser desorption ionization time-of-flight mass spectrometry study | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 95 | issue = 19 | pages = 11342–7 | date = September 1998 | pmid = 9736738 | pmc = 21644 | doi = 10.1073/pnas.95.19.11342 | bibcode = 1998PNAS...9511342U }} 4. ^{{cite journal | vauthors = Zahn M, Berthold N, Kieslich B, Knappe D, Hoffmann R, Sträter N | title = Structural studies on the forward and reverse binding modes of peptides to the chaperone DnaK | journal = Journal of Molecular Biology | volume = 425 | issue = 14 | pages = 2463–79 | date = July 2013 | pmid = 23562829 | doi = 10.1016/j.jmb.2013.03.041 }} 5. ^{{cite journal | vauthors = Rahnamaeian M, Cytryńska M, Zdybicka-Barabas A, Dobslaff K, Wiesner J, Twyman RM, Zuchner T, Sadd BM, Regoes RR, Schmid-Hempel P, Vilcinskas A | title = Insect antimicrobial peptides show potentiating functional interactions against Gram-negative bacteria | journal = Proceedings. Biological Sciences | volume = 282 | issue = 1806 | pages = 20150293 | date = May 2015 | pmid = 25833860 | pmc = 4426631 | doi = 10.1098/rspb.2015.0293 }} 6. ^{{cite journal | vauthors = Florin T, Maracci C, Graf M, Karki P, Klepacki D, Berninghausen O, Beckmann R, Vázquez-Laslop N, Wilson DN, Rodnina MV, Mankin AS | title = An antimicrobial peptide that inhibits translation by trapping release factors on the ribosome | journal = Nature Structural & Molecular Biology | volume = 24 | issue = 9 | pages = 752–757 | date = September 2017 | pmid = 28741611 | pmc = 5589491 | doi = 10.1038/nsmb.3439 }} 7. ^{{cite journal | vauthors = Narayanan S, Modak JK, Ryan CS, Garcia-Bustos J, Davies JK, Roujeinikova A | title = Mechanism of Escherichia coli resistance to Pyrrhocoricin | journal = Antimicrobial Agents and Chemotherapy | volume = 58 | issue = 5 | pages = 2754–62 | date = May 2014 | pmid = 24590485 | pmc = 3993218 | doi = 10.1128/AAC.02565-13 }} 2 : Drosophila|Insect immunity |
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