A Remarkable Discovery: Exploring a Rare Eresus and Spider Wasp Interaction

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  Photo Credit: © Antonino Rametta . All photographs are used with permission. No part of these images may be reproduced, distributed, or used in any form without the prior written permission of the photographer. A Remarkable Discovery: Exploring a Rare Eresus and Spider Wasp Interaction One of the most rewarding aspects of maintaining Arácnido Taxonomy is hearing from naturalists and photographers around the world who take the time to share their discoveries. Every so often, an email arrives that immediately captures your attention. Not because it claims to rewrite what we know about biodiversity, but because it documents something that very few people have the opportunity to witness. Recently, I was contacted by a naturalist in Sicily who shared a series of exceptionally high-quality photographs of a female ladybird spider ( Eresus ) during what appeared to be an interaction with a spider wasp. Along with the images came a simple question: "Could this be scientifically import...

Spider venom phospholipase D toxin structure: Interfacial binding site, mechanism, activation, and head group preference

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Spider venom phospholipase D toxin structure: Interfacial binding site, mechanism, activation, and head group preference

Abstract

Envenomation by sicariid spiders such as the brown recluse can cause loxoscelism, a syndrome involving localized dermonecrosis and/or systemic effects like hemolysis. The causative venom toxins are unusual interfacial phospholipase D enzymes that cyclize sphingolipid and lysophospholipid substrates when bound to membrane surfaces. Crystal structures of several of these toxins have been reported, but none of them directly illuminates how lipids bind in the active site and at the interfacial binding site (IBS); indeed, as a general rule the lipid interfaces of peripheral membrane proteins resist crystallographic determination. Here, however, we report X-ray crystal structures at 1.85 to 2.6 Å resolution of a venom toxin from the Chilean six-eyed sand spider Sicarius levii (terrosus) bound to a micelle-like agglomeration of product and substrate sphingolipids. Each enzyme subunit binds three sphingolipid molecules, one in the active site and two at adjacent noncatalytic sites, generating an interface that approximates the IBS predicted by molecular dynamics. The conformations of substrate and cyclic product in the active site definitively confirm our previously proposed catalytic mechanism. Comparisons with lipid-free structures show conformational changes in two loops that suggest a mechanism for allosteric/surface activation. Docking studies suggest that the variable preference of these toxins for phosphocholine and phosphoethanolamine head groups involves subtle changes in size and shape of the active-site pocket. The structures reveal key facets of the molecular basis of loxoscelism and show that in favorable cases crystallography can illuminate the IBS of peripheral membrane proteins.

Sundman, A. K., Binford, G. J., Montfort, W. R., & Cordes, M. H. (2026). Spider venom phospholipase D toxin structure: Interfacial binding site, mechanism, activation, and head group preference. Proceedings of the National Academy of Sciences, 123(15), e2513997123. https://doi.org/10.1073/pnas.2513997123