A purified lectin with larvicidal activity from a woodland mushroom, Agaricus semotus Fr.

Abstract

This study investigated the larvicidal activity on Culex quinquefasciatus of lectin purified from fresh fruiting bodies of woodland mushroom, Agaricus semotus. A. semotus lectin (ASL) was purified via ion-exchange chromatography on DEAE-cellulose A-25 and size exclusion chromatography on Sephadex G-100 matrix. Molecular weight (16.6 kDa) was estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The effects of temperature, pH, metal chelation- and larvicidal activity of ASL were also investigated. The ASL indifferently agglutinated the erythrocytes of the human ABO blood system and was stable at acidic pH and below 50 °C whereas 66% of its activity was lost at 60 °C with complete inactivation at 70 °C. ASL is a metalloprotein requiring barium ion as chelation of metals by 50 mM EDTA rendered the lectin inactive, while the addition of BaCl2, among other metal salts, restored the activity. ASL showed larvicidal activity against C. quinquefasciatus larvae after 24 h with a mortality of 5 and 95% at 5 and 25 mg/mL respectively, and LC50 of 13.80 mg/mL. This study concluded that purified A. semotus lectin showed impressive larvicidal activity, which could be exploited in its development as an insecticidal agent.

Bioactivities of Calocybe indica Protein combined with Cell-Free Supernatant of Lactobacilli from a Fermented Cereal against Free Radicals and Microorganisms

“…indica mushroom is a rich source of protein. Supporting our findings, elevated protein yields have also been reported in the Basidiomycota Agaricus bisporus Agaricus semotus, and Pleurotus eryngii Yuan et al, 2017;Adedoyin et al, 2021). Although, mushroom protein content varies within species, these saprophytic organisms are however a unique reservoir of diverse Dummy short title Adewole et al…”

Antimicrobial Activities and Phylogenetic Study of Erythrina senegalensis DC (Fabaceae) Seed lectin

“…The MIC of ESL against susceptible bacteria ranged from 0.05 to 0.2 mg/ml (Table 1). Lectins have high specificity, enabling them to identify unique sugar structures (Adedoyin et al, 2021). This unique property allows them to mediate specific microbial binding, innate immune response, and cell-to-cell signaling, coupled with host-pathogen interactions (Paiva et al, 2010;Procópio et al, 2017).…”

“…Lectins are unique proteins or glycoproteins, having at least one domain devoid of catalytic activity and capable of binding specific glycan moieties reversibly (Alen’kina et al, 2014 ; Nubi et al, 2021 ). These proteins are heterogeneous in structures and proficient in agglutinating or precipitating cells and carbohydrate-relate structures via specific interactions (Singh et al, 2016 ; Adedoyin et al, 2021 ). Lectins mediate a wide range of biological and biochemical processes in many organisms, such as nitrogen fixation, cellular development, mitogenesis, symbiosis, immunomodulation, and defense (Smýkal et al, 2015 ; Osman and Konozy, 2017 ; Rambo et al, 2019 ; Van Holle and Van Damme, 2019 ; Fonseca et al, 2022a ).…”