Snake Venom Cathelicidins as Natural Antimicrobial Peptides

Abstract

Bioactive small molecules isolated from animals, plants, fungi and bacteria, including natural antimicrobial peptides, have shown great therapeutic potential worldwide. Among these peptides, snake venom cathelicidins are being widely exploited, because the variation in the composition of the venom reflects a range of biological activities that may be of biotechnological interest. Cathelicidins are short, cationic, and amphipathic molecules. They play an important role in host defense against microbial infections. We are currently facing a strong limitation on pharmacological interventions for infection control, which has become increasingly complex due to the lack of effective therapeutic options. In this review, we will focus on natural snake venom cathelicidins as promising candidates for the development of new antibacterial agents to fight antibiotic-resistant bacteria. We will highlight their antibacterial and antibiofilm activities, mechanism of action, and modulation of the innate immune response.

Pseudonajide peptide derived from snake venom alters cell envelope integrity interfering on biofilm formation in Staphylococcus epidermidis

“…Since AMPs can interact with a large variety of cell targets, they have an advantage in the ght against the production of bacterial resistance phenotypes (35). Currently only three natural cathelicidins have had their antibio lm activity reported (NA-CATH, CATHPb1, and SA-CATH) (7,36,37,38). Synthetic derivatives from these natural cathelicidins were tested and showed improved anti-bio lm activity in comparison with natural NA-CATH peptide (38).…”

“…Cathelicidin-related antimicrobial peptides (CRAMPs) from snake venoms (specially from Elapidae and Viperidae families) have been studied as models for the design of new antimicrobial pharmaceuticals against bacterial infections, facilitated by complete genome sequences available (7). These bioactive molecules are structurally characterized by an N-terminal segment with a gene-encoded signal peptide and a cathelin domain derived from the cathepsin L-inhibitor (pro-peptide), followed by a C-terminal antimicrobial domain with diverse structure (mature peptide) (8).…”

Pseudonajide peptide derived from snake venom alters cell envelope integrity interfering on biofilm formation in Staphylococcus epidermidis

“…Since AMPs can interact with a large variety of cell targets, they have an advantage in the fight against the production of bacterial resistance phenotypes (35). Nowadays, only three natural cathelicidins had their antibiofilm activity reported (NA-CATH, CATHPb1 and SA-CATH) (7,36,37,38). Synthetic derivatives from these natural cathelicidins were tested and showed improved anti-biofilm activity in comparison with natural NA-CATH peptide (38).…”

“…Cathelicidin-related antimicrobial peptides (CRAMPs) from snake venoms (specially from Elapidae and Viperidae families) have been studied, as a model for the design of new antimicrobial pharmaceuticals at bacterial infections setting, since sequencing of the complete genome techniques have been applied (7). These bioactive molecules are structurally characterized by a N-terminal segment with a gene-encoded signal peptide and a cathelin domain derived from the cathepsin Linhibitor (pro-peptide) followed by a C-terminal antimicrobial domain with diverse structure (mature peptide) (8).…”

Antimicrobial Properties of Apis mellifera’s Bee Venom

“…Venoms and their peptides from different animals or organisms such as bees, snakes, wasps, and scorpions, represent promising antimicrobial agents against various microbial pathogenesis [7][8][9][10][11][12]. BV is the venomous cocktail secreted by honeybee workers' poison glands as a protection mechanism [13].…”