Characterization and Functional Analysis of Small Heat Shock Protein Genes (<i>Hsp22.2</i> and <i>Hsp26.7</i>) in <i>Sitodiplosis mosellana</i> Diapause
Small heat shock proteins (sHsps) play crucial roles in organismal adaptation to stress tolerance. <i>Sitodiplosis mosellana</i>, a devastating insect wheat pest, undergoes long obligatory larval diapause to survive temperature extremes during summer and winter. To elucidate the function...
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2025-06-01
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| author | Qitong Huang Qian Ma Xiaobin Liu Keyan Zhu-Salzman Weining Cheng |
| author_facet | Qitong Huang Qian Ma Xiaobin Liu Keyan Zhu-Salzman Weining Cheng |
| author_sort | Qitong Huang |
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| description | Small heat shock proteins (sHsps) play crucial roles in organismal adaptation to stress tolerance. <i>Sitodiplosis mosellana</i>, a devastating insect wheat pest, undergoes long obligatory larval diapause to survive temperature extremes during summer and winter. To elucidate the function of sHsps in this process, two sHsp-encoding genes (<i>SmHsp22.2</i> and <i>SmHsp26.7</i>) were characterized from <i>S. mosellana</i>, and their responsiveness to diapause and thermal stress, as well as their roles in cold stress, was analyzed. Both <i>SmHsp22.2</i> and <i>SmHsp26.7</i> possessed the canonical α-crystallin domain and lacked introns. Quantitative PCR indicated significant upregulation of <i>SmHsp22.2</i> and <i>SmHsp26.7</i> during diapause, especially in summer and winter. Notably, <i>SmHsp22.2</i> exhibited higher expression in summer relative to winter, whereas <i>SmHsp26.7</i> showed the opposite profile. Moreover, short-term heat shock (≥35 °C) in over-summering larvae or cold shock (≤−10 °C) in over-wintering larvae was found to trigger transcriptional upregulation of both genes, while prolonged temperature extremes (i.e., 45–50 °C or −15 °C) did not elicit a comparable response. RNA interference-mediated knockdown of both genes significantly increased the mortality of <i>S. mosellana</i> larvae under cold stress. These findings indicate the importance of both <i>SmHsps</i> in diapause and environmental adaptation in <i>S. mosellana</i>. |
| format | Article |
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| institution | Kabale University |
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| publishDate | 2025-06-01 |
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| spelling | doaj-art-fdab2cfbbfc54619bb0847b5e5defc802025-08-20T03:35:37ZengMDPI AGInsects2075-44502025-06-0116764910.3390/insects16070649Characterization and Functional Analysis of Small Heat Shock Protein Genes (<i>Hsp22.2</i> and <i>Hsp26.7</i>) in <i>Sitodiplosis mosellana</i> DiapauseQitong Huang0Qian Ma1Xiaobin Liu2Keyan Zhu-Salzman3Weining Cheng4Shandong Institute of Sericulture, Shandong Academy of Agricultural Sciences, Yantai 265503, ChinaKey Laboratory of Plant Protection Resources and Pest Management of Ministry of Education, College of Plant Protection, Northwest A&F University, Yangling 712100, ChinaShandong Institute of Sericulture, Shandong Academy of Agricultural Sciences, Yantai 265503, ChinaDepartment of Entomology, Texas A&M University, College Station, TX 77843, USAKey Laboratory of Plant Protection Resources and Pest Management of Ministry of Education, College of Plant Protection, Northwest A&F University, Yangling 712100, ChinaSmall heat shock proteins (sHsps) play crucial roles in organismal adaptation to stress tolerance. <i>Sitodiplosis mosellana</i>, a devastating insect wheat pest, undergoes long obligatory larval diapause to survive temperature extremes during summer and winter. To elucidate the function of sHsps in this process, two sHsp-encoding genes (<i>SmHsp22.2</i> and <i>SmHsp26.7</i>) were characterized from <i>S. mosellana</i>, and their responsiveness to diapause and thermal stress, as well as their roles in cold stress, was analyzed. Both <i>SmHsp22.2</i> and <i>SmHsp26.7</i> possessed the canonical α-crystallin domain and lacked introns. Quantitative PCR indicated significant upregulation of <i>SmHsp22.2</i> and <i>SmHsp26.7</i> during diapause, especially in summer and winter. Notably, <i>SmHsp22.2</i> exhibited higher expression in summer relative to winter, whereas <i>SmHsp26.7</i> showed the opposite profile. Moreover, short-term heat shock (≥35 °C) in over-summering larvae or cold shock (≤−10 °C) in over-wintering larvae was found to trigger transcriptional upregulation of both genes, while prolonged temperature extremes (i.e., 45–50 °C or −15 °C) did not elicit a comparable response. RNA interference-mediated knockdown of both genes significantly increased the mortality of <i>S. mosellana</i> larvae under cold stress. These findings indicate the importance of both <i>SmHsps</i> in diapause and environmental adaptation in <i>S. mosellana</i>.https://www.mdpi.com/2075-4450/16/7/649small heat shock proteindiapause<i>Sitodiplosis mosellana</i>temperature stresscold adaptation |
| spellingShingle | Qitong Huang Qian Ma Xiaobin Liu Keyan Zhu-Salzman Weining Cheng Characterization and Functional Analysis of Small Heat Shock Protein Genes (<i>Hsp22.2</i> and <i>Hsp26.7</i>) in <i>Sitodiplosis mosellana</i> Diapause Insects small heat shock protein diapause <i>Sitodiplosis mosellana</i> temperature stress cold adaptation |
| title | Characterization and Functional Analysis of Small Heat Shock Protein Genes (<i>Hsp22.2</i> and <i>Hsp26.7</i>) in <i>Sitodiplosis mosellana</i> Diapause |
| title_full | Characterization and Functional Analysis of Small Heat Shock Protein Genes (<i>Hsp22.2</i> and <i>Hsp26.7</i>) in <i>Sitodiplosis mosellana</i> Diapause |
| title_fullStr | Characterization and Functional Analysis of Small Heat Shock Protein Genes (<i>Hsp22.2</i> and <i>Hsp26.7</i>) in <i>Sitodiplosis mosellana</i> Diapause |
| title_full_unstemmed | Characterization and Functional Analysis of Small Heat Shock Protein Genes (<i>Hsp22.2</i> and <i>Hsp26.7</i>) in <i>Sitodiplosis mosellana</i> Diapause |
| title_short | Characterization and Functional Analysis of Small Heat Shock Protein Genes (<i>Hsp22.2</i> and <i>Hsp26.7</i>) in <i>Sitodiplosis mosellana</i> Diapause |
| title_sort | characterization and functional analysis of small heat shock protein genes i hsp22 2 i and i hsp26 7 i in i sitodiplosis mosellana i diapause |
| topic | small heat shock protein diapause <i>Sitodiplosis mosellana</i> temperature stress cold adaptation |
| url | https://www.mdpi.com/2075-4450/16/7/649 |
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