Antimicrobial, Insecticidal and Cytotoxic Activity of Linear Venom Peptides from the Pseudoscorpion Chelifer cancroides

Toxins (Basel). 2022 Jan 14;14(1):58. doi: 10.3390/toxins14010058.

Abstract

Linear cationic venom peptides are antimicrobial peptides (AMPs) that exert their effects by damaging cell membranes. These peptides can be highly specific, and for some, a significant therapeutic value was proposed, in particular for treatment of bacterial infections. A prolific source of novel AMPs are arthropod venoms, especially those of hitherto neglected groups such as pseudoscorpions. In this study, we describe for the first time pharmacological effects of AMPs discovered in pseudoscorpion venom. We examined the antimicrobial, cytotoxic, and insecticidal activity of full-length Checacin1, a major component of the Chelifer cancroides venom, and three truncated forms of this peptide. The antimicrobial tests revealed a potent inhibitory activity of Checacin1 against several bacteria and fungi, including methicillin resistant Staphylococcus aureus (MRSA) and even Gram-negative pathogens. All peptides reduced survival rates of aphids, with Checacin1 and the C-terminally truncated Checacin11-21 exhibiting effects comparable to Spinosad, a commercially used pesticide. Cytotoxic effects on mammalian cells were observed mainly for the full-length Checacin1. All tested peptides might be potential candidates for developing lead structures for aphid pest treatment. However, as these peptides were not yet tested on other insects, aphid specificity has not been proven. The N- and C-terminal fragments of Checacin1 are less potent against aphids but exhibit no cytotoxicity on mammalian cells at the tested concentration of 100 µM.

Keywords: antimicrobial activity; antimicrobial peptides; checacin; cytotoxic activity; insecticidal activity; megicin; pseudoscorpion venom.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anti-Infective Agents* / chemistry
  • Anti-Infective Agents* / pharmacology
  • Anti-Infective Agents* / toxicity
  • Aphids / drug effects
  • Arachnida
  • Arthropod Proteins* / chemistry
  • Arthropod Proteins* / pharmacology
  • Arthropod Proteins* / toxicity
  • Arthropod Venoms* / chemistry
  • Arthropod Venoms* / pharmacology
  • Arthropod Venoms* / toxicity
  • Cytotoxins* / chemistry
  • Cytotoxins* / pharmacology
  • Cytotoxins* / toxicity
  • Dogs
  • Insecticides* / chemistry
  • Insecticides* / pharmacology
  • Insecticides* / toxicity
  • Madin Darby Canine Kidney Cells
  • Sequence Alignment

Substances

  • Anti-Infective Agents
  • Arthropod Proteins
  • Arthropod Venoms
  • Cytotoxins
  • Insecticides