Characterising four Sarconesiopsis magellanica (Diptera: Calliphoridae) larval fat body-derived antimicrobial peptides

Mem Inst Oswaldo Cruz. 2021 Jul 16:116:e200587. doi: 10.1590/0074-02760200587. eCollection 2021.

Abstract

Background: The inappropriate use of antibiotics has led to the accelerated growth of resistance to antibiotics. The search for new therapeutic strategies (i.e., antimicrobial peptides-AMPs) has thus become a pressing need.

Objective: Characterising and evaluating Sarconesiopsis magellanica larval fat body-derived AMPs.

Methods: Fat body extracts were analysed by reversed-phase high-performance liquid chromatography (RP-HPLC); mass spectrometry was used for characterising the primary structure of the AMPs so found. ProtParam (Expasy) was used for analysing the AMPs' physico-chemical properties. Synthetic AMPs' antibacterial activity was evaluated.

Findings: Four new AMPs were obtained and called sarconesin III, IV, V and VI. Sarconesin III had an α-helix structure and sarconesins IV, V and VI had linear formations. Oligomer prediction highlighted peptide-peptide interactions, suggesting that sarconesins III, V and VI could form self-aggregations when in contact with the microbial membrane. AMPs synthesised from their native molecules' sequences had potent activity against Gram-positive bacteria and, to a lesser extent, against Gram-negative and drug-resistant bacteria. Sarconesin VI was the most efficient AMP. None of the four synthetic AMPs had a cytotoxic effect.

Main conclusions: S. magellanica larval fat body-derived antimicrobial peptides are an important source of AMPs and could be used in different antimicrobial therapies and overcoming bacterial resistance.

MeSH terms

  • Animals
  • Anti-Bacterial Agents / pharmacology
  • Calliphoridae
  • Diptera*
  • Fat Body
  • Larva
  • Microbial Sensitivity Tests
  • Pore Forming Cytotoxic Proteins

Substances

  • Anti-Bacterial Agents
  • Pore Forming Cytotoxic Proteins