Sex Role–Dependent Behavioral and Architectural Divergence in a Jumping Spider

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  Sex Role–Dependent Behavioral and Architectural Divergence in a Jumping Spider ABSTRACT Sex differences in behavior and functional traits are often attributed to differences in mating effort intensity, but the role of sex-specific parental demands remains poorly understood. Using the jumping spider Toxeus maxillosus —where males engage in mate searching and courtship without providing parental care, while females provide extended maternal care from egg attendance to offspring maturity (around 3 months)—we conducted an exploratory investigation into whether these distinct selective pressures led to divergence in spatial behaviors and nest architecture. Results revealed that males and females showed equivalent accuracy, latency, and learning-related performance in both a route-planning test under water stress and a color-pattern associative memory task. In contrast, during nest-construction assays, females built complex, multi-entrance structures that closely matched the container'...

Molecular mechanism of α-latrotoxin action

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Molecular mechanism of α-latrotoxin action

Abstract


The potent neurotoxic venom of the black widow spider contains a cocktail of seven phylum-specific latrotoxins (LTXs), but only one, α-LTX, targets vertebrates. This 130 kDa toxin binds to receptors at presynaptic nerve terminals and triggers a massive release of neurotransmitters. It is widely accepted that LTXs tetramerize and insert into the presynaptic membrane, thereby forming Ca2+-conductive pores, but the underlying mechanism remains poorly understood. LTXs are homologous and consist of an N-terminal region with three distinct domains, along with a C-terminal domain containing up to 22 consecutive ankyrin repeats. Here we report the first high resolution structures of the vertebrate-specific α-LTX tetramer in its prepore and pore state. Our structures, in combination with AlphaFold2-based structural modeling and molecular dynamics simulations, reveal dramatic conformational changes in the N-terminal region of the complex. Four distinct helical bundles synchronously rearrange to progressively form a highly stable 15 nm cation-impermeable coiled-coil stalk. This stalk, in turn, positions an N-terminal pair of helices within the membrane, thereby enabling the assembly of a cation-permeable channel. Taken together, these data unveil a unique mechanism for membrane insertion and channel formation, characteristic of the LTX family, and provide the necessary framework for advancing novel therapeutics and biotechnological applications.


Molecular mechanism of α-latrotoxin action Bjoern Udo Klink, Azadeh Alavizargar, Kalyankumar Karthik Subramaniam, Minghao Chen, Andreas Heuer, Christos Gatsogiannis
bioRxiv 2024.03.06.583760; doi: https://doi.org/10.1101/2024.03.06.583760