The Glycoproteome of Loxosceles Venom Reveals an Expanded Landscape of Animal Toxins

N-glycosylation is detected across multiple venom proteins in Loxosceles gaucho, Loxosceles intermedia, and Loxosceles laeta, with 88 N-glycosylated peptide sequences identified and species-specific glyco-profiles.

• Why it matters: Glycosylation and its effects on venom properties are understudied despite proteomic work on Loxosceles toxins, leaving a gap in understanding molecular heterogeneity linked to loxoscelism.
• What they did: The team used two-dimensional electrophoresis with glycoprotein staining plus LC-MS/MS, then performed bottom-up glycoproteomics of crude venoms with Byonic and a customized sequence database to map N-glycosylated peptides.
• The result: They found extensive microheterogeneity at individual N-glycosylation sites, mainly paucimannosidic structures, lectin assays indicating mannose, galactose, and N-acetylgalactosamine epitopes, and 2,6-sialic acid-reactive motifs in two species.

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