Peptide Toxin Diversity and a Novel Antimicrobial Peptide from the Spider Oxyopes forcipiformis

Spider venoms are emerging as a rich source of bioactive peptide toxins with therapeutic potential. Lynx spiders of the genus <i>Oxyopes</i> are small, cursorial hunters that employ complex venom to subdue arthropod prey. However, extracting crude venom from these diminutive arachnids poses significant challenges. This study presents a transcriptome analysis of venom glands from an undescribed <i>Oxyopes forcipiformis</i> species, revealing 339 putative protein and peptide toxin sequences categorized into seven functional groups. The venom composition was dominated by membrane-active peptides (40.71%), venom auxiliary proteins (22.71%), neurotoxins (15.63%), channel active peptides (7.08%) and uncharacterized components (13.87%). Additionally, phylogenetic analysis of 65 disulfide-bond-rich peptides yielded six distinct families based on sequence homology and cysteine framework. Finally, a novel antimicrobial peptide, GK37, was identified using in silico and homology analyses. Our data suggested that GK37 presented significant antibacterial activity against Gram-positive bacteria <i>Staphylococcus aureus</i> with a minimum inhibitory concentration (MIC) of 1.552 µM by disrupting bacterial membranes. At 4× MICs, GK37 almost showed no hemolytic activity on blood cells or toxicity against Hek293T cells. Our findings provided a basis for targeted studies of the diversity and pharmacological effects of lynx spider peptide. We elucidated a valuable high-throughput approach for obtaining proteins and peptides from small-group spiders.