Frontiers in pharmacology · 2026
Exploratory proteomic characterization of Apis mellifera venom across an environmental gradient in central Chile.
СтатьяНазвание и аннотация: Перевод в очереди
Обработка статьи · этапы, ошибки и управление
Загрузка состояния…
Ошибки и ограничения
История · было → стало
Состояние обновляется каждые 5 секунд, пока блок открыт. Процент показывается только там, где известен объём работы. Пауза останавливает продолжение этапа; текущий запрос к источнику может завершиться.
Marcos José Luis, Campos-Soto Ricardo, Ortiz Rina, Olivares Yerko, Villena Joan, Párraga Mario, Sotomayor-Zárate Ramón, Constandil Luis, Müller Heine
Аннотация
BACKGROUND: Bee venom (Apis mellifera) is a complex biological secretion rich in peptides, enzymes, and bioactive molecules with recognized pharmacological potential. Environmental conditions may influence venom composition; however, geographic variation in the bee venom proteome remains insufficiently characterized, particularly in South American Mediterranean ecosystems, including central Chile.
METHODS: Venom from multiple A. mellifera colonies within each sampling area of the Valparaíso Region, Chile, was pooled to generate one composite sample per geographic zone: Sea Level, Inland Valley, and Andean Foothill. Two analytical aliquots from each pooled sample were independently processed by liquid chromatography tandem mass spectrometry (LC-MS/MS). Protein identification and label-free quantification were performed using MaxLFQ and iBAQ, and differential abundance was assessed using DEqMS.
RESULTS: Overall, 679 proteins were identified. Principal component analysis and hierarchical clustering showed reproducible grouping of analytical duplicates by geographic origin, indicating distinct proteomic profiles among zones. Differential abundance analysis identified proteins with significant abundance changes between regions, particularly between Sea Level and Inland Valley. Classical venom components, including melittin and phospholipase A2, predominated across samples, whereas proteins associated with stress response, redox regulation, metabolism, and secretion showed geographic variation.
CONCLUSION: Bee venom from geographically distinct areas of central Chile exhibited exploratory proteomic differences, primarily in protein abundance patterns. Although the absence of independent biological replicates limits population-level inference, these patterns suggest environmentally associated proteomic plasticity potentially relevant to biological activity and pharmacological standardization. Further studies incorporating biological replication, targeted validation, and functional assays are required to confirm these findings.
METHODS: Venom from multiple A. mellifera colonies within each sampling area of the Valparaíso Region, Chile, was pooled to generate one composite sample per geographic zone: Sea Level, Inland Valley, and Andean Foothill. Two analytical aliquots from each pooled sample were independently processed by liquid chromatography tandem mass spectrometry (LC-MS/MS). Protein identification and label-free quantification were performed using MaxLFQ and iBAQ, and differential abundance was assessed using DEqMS.
RESULTS: Overall, 679 proteins were identified. Principal component analysis and hierarchical clustering showed reproducible grouping of analytical duplicates by geographic origin, indicating distinct proteomic profiles among zones. Differential abundance analysis identified proteins with significant abundance changes between regions, particularly between Sea Level and Inland Valley. Classical venom components, including melittin and phospholipase A2, predominated across samples, whereas proteins associated with stress response, redox regulation, metabolism, and secretion showed geographic variation.
CONCLUSION: Bee venom from geographically distinct areas of central Chile exhibited exploratory proteomic differences, primarily in protein abundance patterns. Although the absence of independent biological replicates limits population-level inference, these patterns suggest environmentally associated proteomic plasticity potentially relevant to biological activity and pharmacological standardization. Further studies incorporating biological replication, targeted validation, and functional assays are required to confirm these findings.