Biology:Pyrrhocoricin
| Pyrrhocoricin | |
|---|---|
 The firebug Pyrrhocoris apterus | |
| Identifiers | |
| Symbol | ? |
| CAS number | |
| PDB | 5FDV |
| UniProt | P37362 |
Pyrrhocoricin is a 20-residue long antimicrobial peptide of the firebug Pyrrhocoris apterus.[1]
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
- ↑ "Cyclization of pyrrhocoricin retains structural elements crucial for the antimicrobial activity of the native peptide". Biopolymers 76 (5): 446–58. 24 February 2019. doi:10.1002/bip.20159. PMID 15478127.
- ↑ "Structural studies on the forward and reverse binding modes of peptides to the chaperone DnaK". Journal of Molecular Biology 425 (14): 2463–79. July 2013. doi:10.1016/j.jmb.2013.03.041. PMID 23562829.
- ↑ "Identification of crucial residues for the antibacterial activity of the proline-rich peptide, pyrrhocoricin". European Journal of Biochemistry 269 (17): 4226–37. September 2002. doi:10.1046/j.1432-1033.2002.03119.x. PMID 12199701.
- ↑ "Insect antimicrobial peptides show potentiating functional interactions against Gram-negative bacteria". Proceedings. Biological Sciences 282 (1806): 20150293. May 2015. doi:10.1098/rspb.2015.0293. PMID 25833860.
- ↑ "An antimicrobial peptide that inhibits translation by trapping release factors on the ribosome". Nature Structural & Molecular Biology 24 (9): 752–757. September 2017. doi:10.1038/nsmb.3439. PMID 28741611.
- ↑ "Mechanism of Escherichia coli resistance to Pyrrhocoricin". Antimicrobial Agents and Chemotherapy 58 (5): 2754–62. May 2014. doi:10.1128/AAC.02565-13. PMID 24590485.
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