A lectin produced by a Streptomyces species targets mammalian pancreatic acinar cells in mice and humans
Abstract Lectins are produced in almost all life forms, can interact with targets (glycans) in a cross-kingdom manner and have served as valuable tools for studying glycobiology. Previously, a bacterial lectin, named Streptomyces hemagglutinin (SHA), was found to agglutinate human type B erythrocyte...
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Nature Portfolio
2025-01-01
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| author | Janine C. Quijano Honoka Natsuyama Alonso Tapia Karine Bagramyan Jose A. Ortiz Jacob Mares Markus Kalkum Yoko Fujita-Yamaguchi Hsun Teresa Ku |
| author_facet | Janine C. Quijano Honoka Natsuyama Alonso Tapia Karine Bagramyan Jose A. Ortiz Jacob Mares Markus Kalkum Yoko Fujita-Yamaguchi Hsun Teresa Ku |
| author_sort | Janine C. Quijano |
| collection | DOAJ |
| description | Abstract Lectins are produced in almost all life forms, can interact with targets (glycans) in a cross-kingdom manner and have served as valuable tools for studying glycobiology. Previously, a bacterial lectin, named Streptomyces hemagglutinin (SHA), was found to agglutinate human type B erythrocytes. However, the binding of SHA to mammalian cell types other than human erythrocytes has not been explored. To address this, we produced a recombinant fusion protein, with the mCherry reporter protein proceeding the SHA protein (referred to as mCherry-SHA), and performed co-immunofluorescence staining analysis. We focused on the normal pancreas in this study because glycans on pancreatic cells have been associated with initiation and progression of pancreatic cancer, a deadly disease. We found that only acinar, but not ductal or endocrine cells were stained positively with mCherry-SHA from embryonic day (E) 18.5 to 35 weeks old mice; in contrast, E12.5 and E15.5 pancreas display minimal mCherry-SHA binding. In adult humans, mCherry-SHA also targeted acinar cells specifically; however, only tissue from blood type B donors, but not type A or O donors, showed positivity. Together, these results demonstrate that SHA can bind to normal murine and human pancreatic acinar cells and that SHA-binding glycans are developmentally regulated. |
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| institution | Kabale University |
| issn | 2045-2322 |
| language | English |
| publishDate | 2025-01-01 |
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| spelling | doaj-art-b1b75bac6d9c47f29df26e0234613e1b2025-01-26T12:28:20ZengNature PortfolioScientific Reports2045-23222025-01-0115111410.1038/s41598-024-80889-yA lectin produced by a Streptomyces species targets mammalian pancreatic acinar cells in mice and humansJanine C. Quijano0Honoka Natsuyama1Alonso Tapia2Karine Bagramyan3Jose A. Ortiz4Jacob Mares5Markus Kalkum6Yoko Fujita-Yamaguchi7Hsun Teresa Ku8Department of Translational Research and Cellular Therapeutics, Arthur Riggs Diabetes and Metabolism Research InstituteDepartment of Translational Research and Cellular Therapeutics, Arthur Riggs Diabetes and Metabolism Research InstituteThe Irell and Manella Graduate School of Biological SciencesDepartment of Immunology and Theranostics, Arthur Riggs Diabetes and Metabolism Research InstituteDepartment of Translational Research and Cellular Therapeutics, Arthur Riggs Diabetes and Metabolism Research InstituteDepartment of Translational Research and Cellular Therapeutics, Arthur Riggs Diabetes and Metabolism Research InstituteDepartment of Immunology and Theranostics, Arthur Riggs Diabetes and Metabolism Research InstituteDepartment of Diabetes Complications and Metabolism, Beckman Research Institute, Arthur Riggs Diabetes and Metabolism Research Institute, City of HopeDepartment of Translational Research and Cellular Therapeutics, Arthur Riggs Diabetes and Metabolism Research InstituteAbstract Lectins are produced in almost all life forms, can interact with targets (glycans) in a cross-kingdom manner and have served as valuable tools for studying glycobiology. Previously, a bacterial lectin, named Streptomyces hemagglutinin (SHA), was found to agglutinate human type B erythrocytes. However, the binding of SHA to mammalian cell types other than human erythrocytes has not been explored. To address this, we produced a recombinant fusion protein, with the mCherry reporter protein proceeding the SHA protein (referred to as mCherry-SHA), and performed co-immunofluorescence staining analysis. We focused on the normal pancreas in this study because glycans on pancreatic cells have been associated with initiation and progression of pancreatic cancer, a deadly disease. We found that only acinar, but not ductal or endocrine cells were stained positively with mCherry-SHA from embryonic day (E) 18.5 to 35 weeks old mice; in contrast, E12.5 and E15.5 pancreas display minimal mCherry-SHA binding. In adult humans, mCherry-SHA also targeted acinar cells specifically; however, only tissue from blood type B donors, but not type A or O donors, showed positivity. Together, these results demonstrate that SHA can bind to normal murine and human pancreatic acinar cells and that SHA-binding glycans are developmentally regulated.https://doi.org/10.1038/s41598-024-80889-yBacterial lectinStreptomyces sp. 27S5PancreasAcinar cells |
| spellingShingle | Janine C. Quijano Honoka Natsuyama Alonso Tapia Karine Bagramyan Jose A. Ortiz Jacob Mares Markus Kalkum Yoko Fujita-Yamaguchi Hsun Teresa Ku A lectin produced by a Streptomyces species targets mammalian pancreatic acinar cells in mice and humans Scientific Reports Bacterial lectin Streptomyces sp. 27S5 Pancreas Acinar cells |
| title | A lectin produced by a Streptomyces species targets mammalian pancreatic acinar cells in mice and humans |
| title_full | A lectin produced by a Streptomyces species targets mammalian pancreatic acinar cells in mice and humans |
| title_fullStr | A lectin produced by a Streptomyces species targets mammalian pancreatic acinar cells in mice and humans |
| title_full_unstemmed | A lectin produced by a Streptomyces species targets mammalian pancreatic acinar cells in mice and humans |
| title_short | A lectin produced by a Streptomyces species targets mammalian pancreatic acinar cells in mice and humans |
| title_sort | lectin produced by a streptomyces species targets mammalian pancreatic acinar cells in mice and humans |
| topic | Bacterial lectin Streptomyces sp. 27S5 Pancreas Acinar cells |
| url | https://doi.org/10.1038/s41598-024-80889-y |
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