Phosphoproteomics analysis of hypopharyngeal glands of the newly emerged honey bees (Apis mellifera ligustica)
The most important honey bee queen food royal jelly is produced by the exocrine hypopharyngeal glands (HGs) of the worker honey bees. The HGs exhibits diverse gene and protein that create age-related physiological adaptations. However, limited knowledge is available on how the phosphorylation proces...
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| Format: | Article |
| Language: | English |
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Elsevier
2022-08-01
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| Series: | Journal of King Saud University: Science |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S1018364722003871 |
| _version_ | 1818118396066136064 |
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| author | Saboor Ahmad Khalid Ali Khan Hamed A. Ghramh Jianke Li |
| author_facet | Saboor Ahmad Khalid Ali Khan Hamed A. Ghramh Jianke Li |
| author_sort | Saboor Ahmad |
| collection | DOAJ |
| description | The most important honey bee queen food royal jelly is produced by the exocrine hypopharyngeal glands (HGs) of the worker honey bees. The HGs exhibits diverse gene and protein that create age-related physiological adaptations. However, limited knowledge is available on how the phosphorylation process is responsible for physiological alterations across the development of HGs in newly emerged bees. This study measured the acinus of HGs and characterized its phosphoproteomics analysis between the newly emerged bees of royal jelly bees (RJBs) and Italian bees (ITBs). Phosphopeptides of HGs were enriched by Ti4+-IMAC reagents, followed by protein identification via Q-Exactive LC-MS/MS. Our findings indicated that the mean acinus size of HGs of newly emerged bees of RJBs was significantly larger (56.18 ± 1.72 µm) than ITBs (45.98 ± 1.62 µm). A total of 1576 phosphopeptides with 1800 phosphosites containing 525 phosphoproteins were identified in RJBs, while 746 phosphopeptides, of which 846 phosphosites correspond to 317 phosphoproteins were identified in ITBs. Most proteins were phosphorylated on 1 residue followed by 2 and 3 residues in newly emerged bees of both bee stocks. In addition, serine phosphorylation was most observed, followed by threonine and tyrosine in both bee stocks. In newly emerged bees of RJBs, the protein metabolic process, glycolytic process, and formation of translation preinitiation were uniquely enriched, while protein translation, peptide metabolic process and elongation were enriched in ITBs. This research shows detailed phosphorylation of HGs and provides helpful information for understanding the biological activities of HGs development in newly emerged bees from both bee stocks. |
| first_indexed | 2024-12-11T04:53:38Z |
| format | Article |
| id | doaj.art-7f810f2408034c7eaaf8977bebe0e77c |
| institution | Directory Open Access Journal |
| issn | 1018-3647 |
| language | English |
| last_indexed | 2024-12-11T04:53:38Z |
| publishDate | 2022-08-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of King Saud University: Science |
| spelling | doaj.art-7f810f2408034c7eaaf8977bebe0e77c2022-12-22T01:20:20ZengElsevierJournal of King Saud University: Science1018-36472022-08-01346102206Phosphoproteomics analysis of hypopharyngeal glands of the newly emerged honey bees (Apis mellifera ligustica)Saboor Ahmad0Khalid Ali Khan1Hamed A. Ghramh2Jianke Li3Institute of Apicultural Research/Key Laboratory of Pollinating Insect Biology, Ministry of Agriculture, Chinese Academy of Agricultural Sciences, Beijing 100093, ChinaResearch Center for Advanced Materials Science (RCAMS), King Khalid University, P.O. Box 9004, Abha 61413, Saudi Arabia; Unit of Bee Research and Honey Production, Faculty of Science, King Khalid University, P. O. Box 9004, Abha 61413, Saudi ArabiaResearch Center for Advanced Materials Science (RCAMS), King Khalid University, P.O. Box 9004, Abha 61413, Saudi Arabia; Unit of Bee Research and Honey Production, Faculty of Science, King Khalid University, P. O. Box 9004, Abha 61413, Saudi Arabia; Biology Department, Faculty of Science, King Khalid University, P. O. Box 9004, Abha 61413, Saudi ArabiaInstitute of Apicultural Research/Key Laboratory of Pollinating Insect Biology, Ministry of Agriculture, Chinese Academy of Agricultural Sciences, Beijing 100093, China; Corresponding author.The most important honey bee queen food royal jelly is produced by the exocrine hypopharyngeal glands (HGs) of the worker honey bees. The HGs exhibits diverse gene and protein that create age-related physiological adaptations. However, limited knowledge is available on how the phosphorylation process is responsible for physiological alterations across the development of HGs in newly emerged bees. This study measured the acinus of HGs and characterized its phosphoproteomics analysis between the newly emerged bees of royal jelly bees (RJBs) and Italian bees (ITBs). Phosphopeptides of HGs were enriched by Ti4+-IMAC reagents, followed by protein identification via Q-Exactive LC-MS/MS. Our findings indicated that the mean acinus size of HGs of newly emerged bees of RJBs was significantly larger (56.18 ± 1.72 µm) than ITBs (45.98 ± 1.62 µm). A total of 1576 phosphopeptides with 1800 phosphosites containing 525 phosphoproteins were identified in RJBs, while 746 phosphopeptides, of which 846 phosphosites correspond to 317 phosphoproteins were identified in ITBs. Most proteins were phosphorylated on 1 residue followed by 2 and 3 residues in newly emerged bees of both bee stocks. In addition, serine phosphorylation was most observed, followed by threonine and tyrosine in both bee stocks. In newly emerged bees of RJBs, the protein metabolic process, glycolytic process, and formation of translation preinitiation were uniquely enriched, while protein translation, peptide metabolic process and elongation were enriched in ITBs. This research shows detailed phosphorylation of HGs and provides helpful information for understanding the biological activities of HGs development in newly emerged bees from both bee stocks.http://www.sciencedirect.com/science/article/pii/S1018364722003871Newly emerged beesHypopharyngeal glandsMass spectrometryPhosphoproteomicsPhosphopeptides |
| spellingShingle | Saboor Ahmad Khalid Ali Khan Hamed A. Ghramh Jianke Li Phosphoproteomics analysis of hypopharyngeal glands of the newly emerged honey bees (Apis mellifera ligustica) Journal of King Saud University: Science Newly emerged bees Hypopharyngeal glands Mass spectrometry Phosphoproteomics Phosphopeptides |
| title | Phosphoproteomics analysis of hypopharyngeal glands of the newly emerged honey bees (Apis mellifera ligustica) |
| title_full | Phosphoproteomics analysis of hypopharyngeal glands of the newly emerged honey bees (Apis mellifera ligustica) |
| title_fullStr | Phosphoproteomics analysis of hypopharyngeal glands of the newly emerged honey bees (Apis mellifera ligustica) |
| title_full_unstemmed | Phosphoproteomics analysis of hypopharyngeal glands of the newly emerged honey bees (Apis mellifera ligustica) |
| title_short | Phosphoproteomics analysis of hypopharyngeal glands of the newly emerged honey bees (Apis mellifera ligustica) |
| title_sort | phosphoproteomics analysis of hypopharyngeal glands of the newly emerged honey bees apis mellifera ligustica |
| topic | Newly emerged bees Hypopharyngeal glands Mass spectrometry Phosphoproteomics Phosphopeptides |
| url | http://www.sciencedirect.com/science/article/pii/S1018364722003871 |
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