Latarcins: versatile spider venom peptides

Abstract

Arthropod venoms feature the presence of cytolytic peptides believed to act synergetically with neurotoxins to paralyze prey or deter aggressors. Many of them are linear, i.e., lack disulfide bonds. When isolated from the venom, or obtained by other means, these peptides exhibit common properties. They are cationic; being mostly disordered in aqueous solution, assume amphiphilic α-helical structure in contact with lipid membranes; and exhibit general cytotoxicity, including antifungal, antimicrobial, hemolytic, and anticancer activities. To suit the pharmacological needs, the activity spectrum of these peptides should be modified by rational engineering. As an example, we provide a detailed review on latarcins (Ltc), linear cytolytic peptides from Lachesana tarabaevi spider venom. Diverse experimental and computational techniques were used to investigate the spatial structure of Ltc in membrane-mimicking environments and their effects on model lipid bilayers. The antibacterial activity of Ltc was studied against a panel of Gram-negative and Gram-positive bacteria. In addition, the action of Ltc on erythrocytes and cancer cells was investigated in detail with confocal laser scanning microscopy. In the present review, we give a critical account of the progress in the research of Ltc. We explore the relationship between Ltc structure and their biological activity and derive molecular characteristics, which can be used for optimization of other linear peptides. Current applications of Ltc and prospective use of similar membrane-active peptides are outlined.

Antimicrobial Activity of Purified Toxins from <i>Crossopriza lyoni</i> (Spider) against Certain Bacteria and Fungi

“…Salmonella typhi and Vibrio cholerae 24.69 µg/ml, Pseudomonas aeruginosa 15 µg/ml Table 1). Similar activity was reported in the spider venom peptide Lycosin-II against clinically isolated bacterial pathogens [12] and Latarcins, the versatile spider venom peptides [13]. Spider venom possesses proteinaceous toxins which show remarkable insecticidal and antibacterial activities [14].…”

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“…[12,15,16] It is a cationic and amphiphilic peptide [17] which strongly acts on lipid membrane, and disintegrates its structure and cause lysis. [18,19] Similarly, LyeTx I was found active against bacteria E. coli and S. aureus when applied in dose-dependent manner. Most of the spider toxin peptides are alpha-helical amphipathic which directly interact with the cell membrane, perturb it and show bactericidal activity.…”

In vitro Delivery of HIV-1 Nef Antigen by Histidine-rich nona-arginine and Latarcin 1 peptide

“…The novel LDP-NLS cellpenetrating peptide was used to transfer the Nef protein into the HEK-293T cell. Spider venom peptides usually affect the permeability of the membrane [32]. LDP-NLS peptide was utilized for the effective delivery of the β-galactosidase enzyme into the HeLa cells [16].…”