Pyrrhocoricin

Pyrrhocoricin is a 20-residue long antimicrobial peptide of the firebug Pyrrhocoris apterus.[1]

Pyrrhocoricin
The firebug Pyrrhocoris apterus
Identifiers
Symbol?
CAS number224569-84-0
PDB5FDV
UniProtP37362

Structure and function

Pyrrhocoricin is primarily active against Gram-negative bacteria. The peptide is proline-rich with proline-arginine repeats, as well a critical threonine residue, which is required for activity through O-glycosylation. Like the antimicrobial peptides drosocin and abaecin, pyrrhocoricin binds to the bacterial protein DnaK, inhibiting cell machinery and replication.[2] Only the L-enantiomer of pyrrhocoricin is active against bacteria.[3] The action of pyrrhocoricin-like peptides is potentiated by the presence of pore-forming peptides, which facilitates the entry of pyrrhocoricin-like peptides into the bacterial cell.[4] Proline-rich peptides like Pyrrhocoricin can also bind to microbe ribosomes, preventing protein translation.[5] In the absence of pore-forming peptides, pyrrhocoricin is taken into the bacteria by the action of bacterial uptake permeases.[6]

References
  1. Rosengren KJ, Göransson U, Otvos L, Craik DJ (24 February 2019). "Cyclization of pyrrhocoricin retains structural elements crucial for the antimicrobial activity of the native peptide". Biopolymers. 76 (5): 446–58. doi:10.1002/bip.20159. PMID 15478127.
  2. Zahn M, Berthold N, Kieslich B, Knappe D, Hoffmann R, Sträter N (July 2013). "Structural studies on the forward and reverse binding modes of peptides to the chaperone DnaK". Journal of Molecular Biology. 425 (14): 2463–79. doi:10.1016/j.jmb.2013.03.041. PMID 23562829.
  3. Kragol G, Hoffmann R, Chattergoon MA, Lovas S, Cudic M, Bulet P, Condie BA, Rosengren KJ, Montaner LJ, Otvos L (September 2002). "Identification of crucial residues for the antibacterial activity of the proline-rich peptide, pyrrhocoricin". European Journal of Biochemistry. 269 (17): 4226–37. doi:10.1046/j.1432-1033.2002.03119.x. PMID 12199701.
  4. Rahnamaeian M, Cytryńska M, Zdybicka-Barabas A, Dobslaff K, Wiesner J, Twyman RM, Zuchner T, Sadd BM, Regoes RR, Schmid-Hempel P, Vilcinskas A (May 2015). "Insect antimicrobial peptides show potentiating functional interactions against Gram-negative bacteria". Proceedings. Biological Sciences. 282 (1806): 20150293. doi:10.1098/rspb.2015.0293. PMC 4426631. PMID 25833860.
  5. Florin T, Maracci C, Graf M, Karki P, Klepacki D, Berninghausen O, Beckmann R, Vázquez-Laslop N, Wilson DN, Rodnina MV, Mankin AS (September 2017). "An antimicrobial peptide that inhibits translation by trapping release factors on the ribosome". Nature Structural & Molecular Biology. 24 (9): 752–757. doi:10.1038/nsmb.3439. PMC 5589491. PMID 28741611.
  6. Narayanan S, Modak JK, Ryan CS, Garcia-Bustos J, Davies JK, Roujeinikova A (May 2014). "Mechanism of Escherichia coli resistance to Pyrrhocoricin". Antimicrobial Agents and Chemotherapy. 58 (5): 2754–62. doi:10.1128/AAC.02565-13. PMC 3993218. PMID 24590485.
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