Latarcins, Antimicrobial and Cytolytic Peptides from the Venom of the Spider Lachesana tarabaevi (Zodariidae) That Exemplify Biomolecular Diversity

Seven novel short linear antimicrobial and cytolytic peptides named latarcins were purified from the venom of the spider Lachesana tarabaevi. These peptides were found to produce lytic effects on cells of diverse origin (Gram-positive and Gram-negative bacteria, erythrocytes, and yeast) at micromola...

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Veröffentlicht in:The Journal of biological chemistry 2006-07, Vol.281 (30), p.20983-20992
Hauptverfasser: Kozlov, Sergey A., Vassilevski, Alexander A., Feofanov, Alexei V., Surovoy, Andrey Y., Karpunin, Dmitry V., Grishin, Eugene V.
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container_end_page 20992
container_issue 30
container_start_page 20983
container_title The Journal of biological chemistry
container_volume 281
creator Kozlov, Sergey A.
Vassilevski, Alexander A.
Feofanov, Alexei V.
Surovoy, Andrey Y.
Karpunin, Dmitry V.
Grishin, Eugene V.
description Seven novel short linear antimicrobial and cytolytic peptides named latarcins were purified from the venom of the spider Lachesana tarabaevi. These peptides were found to produce lytic effects on cells of diverse origin (Gram-positive and Gram-negative bacteria, erythrocytes, and yeast) at micromolar concentrations. In addition, five novel peptides that share considerable structural similarity with the purified latarcins were predicted from the L. tarabaevi venom gland expressed sequence tag data base. Latarcins were shown to adopt amphipathic α-helical structure in membrane-mimicking environment by CD spectroscopy. Planar lipid bilayer studies indicated that the general mode of action was scaled membrane destabilization at the physiological membrane potential consistent with the “carpet-like” model. Latarcins represent seven new structural groups of lytic peptides and share little homology with other known peptide sequences. For every latarcin, a precursor protein sequence was identified. On the basis of structural features, latarcin precursors were split into three groups: simple precursors with a conventional prepropeptide structure; binary precursors with a typical modular organization; and complex precursors, which were suggested to be cleaved into mature chains of two different types.
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subjects Amino Acid Sequence
Animals
Antimicrobial Cationic Peptides - chemistry
Antimicrobial Cationic Peptides - pharmacology
Araneae
Circular Dichroism
Databases, Genetic
Expressed Sequence Tags
Houseflies
Lipid Bilayers - metabolism
Molecular Sequence Data
Peptides - chemistry
Protein Binding
Sequence Homology, Amino Acid
Spider Venoms - chemistry
Spider Venoms - metabolism
Spider Venoms - pharmacology
Spiders
Zodariidae
title Latarcins, Antimicrobial and Cytolytic Peptides from the Venom of the Spider Lachesana tarabaevi (Zodariidae) That Exemplify Biomolecular Diversity
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