Antimicrobial activity of myotoxic phospholipases A2 from crotalid snake venoms and synthetic peptide variants derived from their C-terminal region.

@article{Santamaria2005AntimicrobialAO,
  title={Antimicrobial activity of myotoxic phospholipases A2 from crotalid snake venoms and synthetic peptide variants derived from their C-terminal region.},
  author={Carlos A. Santamaria and Silda Larios and Yamileth Angulo and Javier Pizarro-Cerd{\'a} and Jean Pierre Gorvel and Edgardo Moreno and Bruno Lomonte},
  journal={Toxicon : official journal of the International Society on Toxinology},
  year={2005},
  volume={45 7},
  pages={
          807-15
        }
}

Bactericidal and Antiendotoxic Properties of Short Cationic Peptides Derived from a Snake Venom Lys49 Phospholipase A2

TLDR
It is demonstrated that phospholipase A2-derived peptides may have the potential to counteract microbial infections and encourage further evaluations of their actions in vivo.

Fungicidal activity of a phospholipase-A2-derived synthetic peptide variant against Candida albicans.

TLDR
This peptide displays a broad-spectrum antimicrobial activity, in the absence of hemolytic activity, and the fungicidal action of pEM-2 against Candida can be partially inhibited by increasing concentrations of extracellular divalent cations, in agreement with its proposed membrane-permeabilizing mechanism of action.

An acidic phospholipase A₂ with antibacterial activity from Porthidium nasutum snake venom.

CoaTx-II, a new dimeric Lys49 phospholipase A2 from Crotalus oreganus abyssus snake venom with bactericidal potential: Insights into its structure and biological roles.

Antitumor effects of snake venom chemically modified Lys49 phospholipase A2-like BthTX-I and a synthetic peptide derived from its C-terminal region.

Membrane cholesterol modulates the cytolytic mechanism of myotoxin II, a Lys49 phospholipase A2 homologue from the venom of Bothrops asper

TLDR
Physicochemical properties that depend on membrane cholesterol content significantly influence the cytolytic mechanism of myotoxin II, reinforcing the concept that the primary site of action of Lys49 PLA2 myotoxins is the plasma membrane.
...

References

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Purification and characterization of myotoxin IV, a phospholipase A2 variant, from Bothrops asper snake venom.

TLDR
A basic myotoxic protein was purified from Bothrops asper venom and found that myotoxin IV induces acute muscle damage after intramuscular injection in mice and disrupts negatively charged liposomes but not positively charged ones, and is devoid of phospholipase A2 activity.

Structural and functional characterization of BnSP-7, a Lys49 myotoxic phospholipase A(2) homologue from Bothrops neuwiedi pauloensis venom.

TLDR
BnSP-7, a Lys49 myotoxic phospholipase A(2) homologue from Bothrops neuwiedi pauloensis venom, was structurally and functionally characterized and displayed bactericidal activity and promoted the blockage of the neuromuscular contraction of the chick biventer cervicis muscle.

Dissociation of enzymatic and pharmacological properties of piratoxins-I and -III, two myotoxic phospholipases A2 from Bothrops pirajai snake venom.

TLDR
Analysis of structural changes by circular dichroism spectroscopy demonstrated significant changes in the secondary structure only in the case of N-terminal octapeptide cleavage, which indicates that Pr TX-I and PrTX-III possess regions other than the catalytic site, which determine their toxic and pharmacological activities.

Isolation and characterization of a myotoxic phospholipase A2 from the venom of the arboreal snake Bothriechis (Bothrops) schlegelii from Costa Rica.

TLDR
A new myotoxic phospholipase A2 was isolated from the venom of the arboreal snake Bothriechis schlegelii from Costa Rica, by ion-exchange chromatography on CM-Sephadex.

Isolation of a myotoxin from Bothrops asper venom: partial characterization and action on skeletal muscle.

A common cytolytic region in myotoxins, hemolysins, cardiotoxins and antibacterial peptides.

  • R. KiniH. Evans
  • Biology, Chemistry
    International journal of peptide and protein research
  • 1989
TLDR
The concept of a cytolytic region is strongly supported by the existence of several natural and synthetic analogues of cy tolysins and by chemical modification studies of these cytolysins, and provides a new focus for cyto Lysin research.