Encrypted antimicrobial peptides from proteins present in the plasma of the millipede Rhinocricus sp

J Proteomics. 2021 Jun 30:242:104239. doi: 10.1016/j.jprot.2021.104239. Epub 2021 Apr 21.

Abstract

Millipedes are among the most diverse and abundant arthropods in terrestrial environments. However, little is known about their innate immune response against invading pathogenic microorganisms, which is very intriguing considering that the evolutionary success of millipedes is largely due to this complex and primitive defense system, since it allowed them to colonize a wide variety of microhabitats characterized by their high microbial proliferation. Accordingly, the aim of the present work was to determine the presence of antimicrobial peptides in the hemolymph of the millipede Rhinocricus sp. In total, four native peptides with potent antimicrobial activity against different microorganisms, lack of cytotoxicity against Vero cells and lack of hemolytic effects against human erythrocytes were isolated and named RP40-16, RP40-19, RP40-20/1 and RP40-20/2. The analysis with bioinformatics tools suggested that these peptides may be encrypted in large proteins present in the plasma: Hemocyanin and thioester-containing protein. Considering these results, it can be said that millipede hemolymph represents a promising source of molecules with potential for the development of non-conventional antibiotics. Therefore, in order to have a clearer notion of the biotechnological potential and the role of these peptides in the innate immune response of Rhinocricus sp., future studies should focus on elucidating their mechanisms of action, as well as additional biological properties.

Keywords: Antimicrobial peptide; Innate immunity; Millipede; Plasma; Rhinocricus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Anti-Bacterial Agents
  • Antimicrobial Cationic Peptides
  • Arthropods*
  • Chlorocebus aethiops
  • Humans
  • Pore Forming Cytotoxic Proteins
  • Vero Cells

Substances

  • Anti-Bacterial Agents
  • Antimicrobial Cationic Peptides
  • Pore Forming Cytotoxic Proteins