Proline-Rich Peptide Complex of Calliphora vicina Larvae and Its Role in Suppressing Adaptive Bacterial Resistance.

Authors

Andrey Y Yakovlev, Nataliia A Kochergina, Alexey G Mittenberg

Published in

Biochemistry. Biokhimiia. Volume 91. Issue 10. Pages 2013-2018.

Abstract

Rapid rise of antibiotic resistance in Gram-negative pathogens dictates an urgent need to search for new natural factors capable of restoring efficacy of the "last-resort" drugs. In the present work, a complex of proline-rich peptides (PRPs) was isolated from the hemolymph of infected Calliphora vicina larvae and characterized using multistep chromatography, including reversed-phase HPLC and cation-exchange FPLC. Tandem mass spectrometry analysis revealed four peptides within the complex that exhibit structural similarity to PRPs from other dipteran species, particularly domesticin from Musca domestica. Although the isolated PRP complex exhibited no direct bactericidal activity against Escherichia coli, it effectively potentiated the effect of membrane-active peptide antibiotics, including polymyxin B. In the serial passage experiments, the PRP complex completely suppressed development of the adaptive resistance to polymyxin B in E. coli. The obtained data suggest that the primary function of these peptides within the co-adapted antimicrobial complexes could be inhibition of the intracellular protein synthesis and folding systems. Such mechanism likely prevents bacteria from mounting an effective stress response, thereby preventing fixation of the resistance mechanisms and ensuring evolutionary stability of the insect humoral immunity.

PMID:
42927758
Bibliographic data and abstract were imported from PubMed on 26 Oct 2026.

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