Two calcium‐binding chaperones from the fat body of the Colorado potato beetle, Leptinotarsa decemlineata (Coleoptera: Chrysomelidae) involved in diapause

• Published in: Archives of insect biochemistry and physiology Vol. 106; no. 1; pp. e21755 - n/a
• Main Authors: Doğan, Cansu, Hänniger, Sabine, Heckel, David G., Coutu, Cathy, Hegedus, Dwayne D., Crubaugh, Linda, Groves, Russell L., Bayram, Şerife, Toprak, Umut
• Format: Journal Article
• Language: English
• Published: United States Wiley Subscription Services, Inc 01.01.2021
• Subjects: Animals; Binding; Calcium; Calcium - metabolism; Calnexin; Calnexin - chemistry; Calnexin - genetics; Calnexin - metabolism; Calreticulin; Calreticulin - chemistry; Calreticulin - genetics; Calreticulin - metabolism; chaperone; Chaperones; Chrysomelidae; Coleoptera; Coleoptera - genetics; Coleoptera - metabolism; Diapause; Diapause, Insect - physiology; Fat body; Fat Body - metabolism; Female; Females; Gene expression; Genes; Genes, Insect; Heat shock proteins; Leptinotarsa decemlineata; Male; Males; Molecular Chaperones - chemistry; Molecular Chaperones - genetics; Molecular Chaperones - metabolism; Phylogeny; Polypeptides; Potatoes; Sex Characteristics; Starvation; United States > US; Colorado; starvation; diapause; calreticulin; calnexin; chaperone
• ISSN: 0739-4462; 1520-6327
• DOI: 10.1002/arch.21755

Molecular chaperones are crucial for the correct folding of newly synthesized polypeptides, in particular, under stress conditions. Various studies have revealed the involvement of molecular chaperones, such as heat shock proteins, in diapause maintenance and starvation; however, the role of other chaperones in diapause and starvation relatively is unknown. In the current study, we identified two lectin‐type chaperones with calcium affinity, a calreticulin (LdCrT) and a calnexin (LdCnX), that were present in the fat body of the Colorado potato beetle, Leptinotarsa decemlineata (Coleoptera: Chrysomelidae) during diapause. Both proteins possessed an N‐globular domain, a P‐arm domain, and a highly charged C‐terminal domain, while an additional transmembrane domain was present in LdCnX. Phylogenetic analysis revealed distinction at the order level. Both genes were expressed in multiple tissues in larval and adult stages, and constitutively throughout development, though a starvation response was detected only for LdCrT. In females, diapause‐related expression analysis in the whole body revealed an upregulation of both genes by post‐diapause, but a downregulation by diapause only for LdCrT. By contrast, males revealed no alteration in their diapause‐related expression pattern in the entire body for both genes. Fat body‐specific expression analysis of both genes in relation to diapause revealed the same expression pattern with no alteration in females and downregulation in males by post‐diapause. This study suggests that calcium‐binding chaperones play similar and possibly gender‐specific roles during diapause. Two lectin‐type chaperones with calcium affinity, a calreticulin (LdCrT) and a calnexin (LdCnX), were identified in the fat body of Leptinotarsa decemlineata. The schematic diagram shows the domain organization of both proteins, and the site‐, starvation‐, and diapause‐related expression patterns of LdCrT and LdCnX. Highlights Chaperone calreticulin (LdCrT) and calnexin (LdCnX) were identified from Leptinotarsa decemlineata. Starvation response was detected only for LdCrT. In females, diapause‐related expression analysis in the whole body revealed an upregulation of both genes by post‐diapause.