Effect of Cold Acclimation on Selected Metabolic Enzymes During Diapause in The European Corn Borer Ostrinia nubilalis (Hbn.)

• Published in: Scientific reports 2020-06, Vol.10 (1), p.9085-9085, Article 9085
• Main Authors: Uzelac, Iva, Avramov, Miloš, Čelić, Tatjana, Vukašinović, Elvira, Gošić-Dondo, Snežana, Purać, Jelena, Kojić, Danijela, Blagojević, Duško, Popović, Željko D.
• Format: Article
• Language: English
• Subjects: 631/45/607; 631/601/1737; 82/29; Acclimation; Acclimatization; Acclimatization - physiology; Alanine - metabolism; Alanine transaminase; Animals; Aspartate aminotransferase; Aspartic Acid - metabolism; Citrate synthase; Citric Acid Cycle - physiology; Cold; Cold acclimation; Cold Temperature; Corn; Cryoprotectors; Diapause; Diapause, Insect - physiology; Enzymes; Humanities and Social Sciences; L-Alanine; L-Lactate dehydrogenase; Lactic acid; Larva - enzymology; Larva - metabolism; Larva - physiology; Larvae; Metabolism; Moths - enzymology; Moths - metabolism; Moths - physiology; multidisciplinary; Ostrinia nubilalis; Pupa - enzymology; Pupa - metabolism; Pupa - physiology; Pyruvic acid; Science; Science (multidisciplinary); Temperature; Transaminases - metabolism; Tricarboxylic acid cycle; Zea mays
• ISSN: 2045-2322; 2045-2322
• DOI: 10.1038/s41598-020-65926-w

The European corn borer, Ostrinia nubilalis Hbn., is a pest Lepidopteran species whose larvae overwinter by entering diapause, gradually becoming cold-hardy. To investigate metabolic changes during cold hardening, activities of four metabolic enzymes – citrate synthase (CS), lactate dehydrogenase (LDH), alanine aminotransferase (ALT) and aspartate aminotransferase (AST) were measured in whole-body homogenates of pupae, non-diapausing and diapausing larvae acclimated to 5 °C, −3 °C and −16 °C. The highest CS activity was detected in non-diapausing larvae, reflecting active development, while the highest in vitro LDH activity was recorded in diapausing larvae at temperatures close to 0 °C, evidencing a metabolic switch towards anaerobic metabolism. However, in-gel LDH activity showed that production of pyruvate from lactate is triggered by sub-zero temperatures. The activities of both aminotransferases were highest in non-diapausing larvae. Our findings suggest that during diapause and cold hardening the aminotransferases catalyse production of L-alanine, an important cryoprotectant, and L-aspartate, which is closely tied to both transamination reactions and Krebs cycle. The results of this study indicate that, during diapause, the activity of metabolic enzymes is synchronized with exogenous factors, such as temperatures close to 0 °C. These findings support the notion that diapause is metabolically plastic and vibrant, rather than simply a passive, resting state.