New predatory interaction of Trichonephila clavipes (Araneae: Nephilidae) on Fidicinini (Hemiptera: Cicadidae) in a forest fragment of the Neotropical region

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  New predatory interaction of Trichonephila clavipes (Araneae: Nephilidae) on Fidicinini (Hemiptera: Cicadidae) in a forest fragment of the Neotropical region Abstract Trichonephila clavipes (Araneae: Nephilidae) is an orb web-building spider whose diet is primarily based on flying insects. This note aims to report the first predatory interaction of T. clavipes on a cicada of the genus Fidicina (Hemiptera: Cicadidae) in a fragment of the Atlantic Forest in Brazil. The predation event was observed (ad libitum) in the Benjamin Maranhão Botanical Garden situated in the Mata do Buraquinho Wildlife Refuge, northeastern Brazil. A specimen of Fidicina sp. was found freshly dead and trapped in the web of T. clavipes. The nephilid was observed moving slowly between the ventral and dorsal regions of the Fidicina sp. without weaving a web around the cicadid. Then, T. clavipes was observed perched on the left side of the Fidicina sp., with its pedipalps and chelicerae manipulating the thorax ...

Characterization of an antimicrobial peptide family from the venom gland of Heteropoda venatoria

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Characterization of an antimicrobial peptide family from the venom gland of Heteropoda venatoria

Abstract

Spider venom boasts extensive peptide diversity, constituting a natural biochemical arsenal for defense and predation. The new family HvAMPs, including 9 homologous members, were identified from the unnormalized cDNA library of Heteropoda venatoria venom gland by Sanger sequencing. The putative mature peptide is composed of 22 aliphatic amino acid residues. The mature peptides of HvAMP1 and HvAMP5, with 3 different amino acids, were synthesized and both were shown to adopt an amphipathic α-helical structure and amphipathicity in SDS buffer by CD spectroscopy. In comparison to HvAMP1, HvAMP5 exhibits higher antibacterial activity, particularly against Gram-positive bacteria, coupled with reduced hemolytic activity and cytotoxicity. Results from SYTO 9/PI staining indicate that HvAMP5 acts by disrupting bacterial cell membranes. Analysis of the relationships between structures and functions suggests that HvAMP5 enhances antibacterial activity and reduces mammalian cell toxicity by increasing positive charge and proline substitution. The three residues variation can augment the electrostatic attraction of antibacterial peptides to the bacterial phospholipid bilayer. The present study suggests that the HvAMPs may exert lytic action against cells of different origins to increase cellular and tissue barrier permeability to facilitate spider's defense or predation. Moreover, HvAMP5 holds promise as a novel antibacterial agent for treating Gram-positive bacterial infections. Simultaneously, the numerous diverse amino acid residue substitutions within the HvAMP family offer a template for future study.

Peng, Z., Wei, C., Cai, J., Zou, Z., & Chen, J. (2024). Characterization of an antimicrobial peptide family from the venom gland of Heteropoda venatoria. Toxicon, 107657. https://doi.org/10.1016/j.toxicon.2024.107657