Biochemical and structural characterization of a recombinant fibrinogen-related lectin from Penaeus monodon
Abstract Fibrinogen-related lectins are carbohydrate-binding proteins of the innate immune system that recognize glycan structures on microbial surfaces. These innate immune lectins are crucial for invertebrates as they do not rely on adaptive immunity for pathogen clearance. Here, we characterize a...
| Main Authors: | , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2021-02-01
|
| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-021-82301-5 |
| _version_ | 1818571107923394560 |
|---|---|
| author | Nongnuch Singrang Sirasit Laophetsakunchai Bich Ngoc Tran Paul T. Matsudaira Anchalee Tassanakajon Kittikhun Wangkanont |
| author_facet | Nongnuch Singrang Sirasit Laophetsakunchai Bich Ngoc Tran Paul T. Matsudaira Anchalee Tassanakajon Kittikhun Wangkanont |
| author_sort | Nongnuch Singrang |
| collection | DOAJ |
| description | Abstract Fibrinogen-related lectins are carbohydrate-binding proteins of the innate immune system that recognize glycan structures on microbial surfaces. These innate immune lectins are crucial for invertebrates as they do not rely on adaptive immunity for pathogen clearance. Here, we characterize a recombinant fibrinogen-related lectin PmFREP from the black tiger shrimp Penaeus monodon expressed in the Trichoplusia ni insect cell. Electron microscopy and cross-linking experiments revealed that PmFREP is a disulfide-linked dimer of pentamers distinct from other fibrinogen-related lectins. The full-length protein binds N-acetyl sugars in a Ca2+ ion-independent manner. PmFREP recognized and agglutinated Pseudomonas aeruginosa. Weak binding was detected with other bacteria, including Vibrio parahaemolyticus, but no agglutination activity was observed. The biologically active PmFREP will not only be a crucial tool to elucidate the innate immune signaling in P. monodon and other economically important species, but will also aid in detection and prevention of shrimp bacterial infectious diseases. |
| first_indexed | 2024-12-14T13:51:12Z |
| format | Article |
| id | doaj.art-3daf8350777c4876a653a2c216ac7285 |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-12-14T13:51:12Z |
| publishDate | 2021-02-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-3daf8350777c4876a653a2c216ac72852022-12-21T22:59:04ZengNature PortfolioScientific Reports2045-23222021-02-0111111110.1038/s41598-021-82301-5Biochemical and structural characterization of a recombinant fibrinogen-related lectin from Penaeus monodonNongnuch Singrang0Sirasit Laophetsakunchai1Bich Ngoc Tran2Paul T. Matsudaira3Anchalee Tassanakajon4Kittikhun Wangkanont5Center of Excellence for Molecular Biology and Genomics of Shrimp, Department of Biochemistry, Faculty of Science, Chulalongkorn UniversityCenter of Excellence for Molecular Biology and Genomics of Shrimp, Department of Biochemistry, Faculty of Science, Chulalongkorn UniversityDepartment of Biological Sciences, Faculty of Science, Centre for BioImaging Sciences, National University of SingaporeDepartment of Biological Sciences, Faculty of Science, Centre for BioImaging Sciences, National University of SingaporeCenter of Excellence for Molecular Biology and Genomics of Shrimp, Department of Biochemistry, Faculty of Science, Chulalongkorn UniversityCenter of Excellence for Molecular Biology and Genomics of Shrimp, Department of Biochemistry, Faculty of Science, Chulalongkorn UniversityAbstract Fibrinogen-related lectins are carbohydrate-binding proteins of the innate immune system that recognize glycan structures on microbial surfaces. These innate immune lectins are crucial for invertebrates as they do not rely on adaptive immunity for pathogen clearance. Here, we characterize a recombinant fibrinogen-related lectin PmFREP from the black tiger shrimp Penaeus monodon expressed in the Trichoplusia ni insect cell. Electron microscopy and cross-linking experiments revealed that PmFREP is a disulfide-linked dimer of pentamers distinct from other fibrinogen-related lectins. The full-length protein binds N-acetyl sugars in a Ca2+ ion-independent manner. PmFREP recognized and agglutinated Pseudomonas aeruginosa. Weak binding was detected with other bacteria, including Vibrio parahaemolyticus, but no agglutination activity was observed. The biologically active PmFREP will not only be a crucial tool to elucidate the innate immune signaling in P. monodon and other economically important species, but will also aid in detection and prevention of shrimp bacterial infectious diseases.https://doi.org/10.1038/s41598-021-82301-5 |
| spellingShingle | Nongnuch Singrang Sirasit Laophetsakunchai Bich Ngoc Tran Paul T. Matsudaira Anchalee Tassanakajon Kittikhun Wangkanont Biochemical and structural characterization of a recombinant fibrinogen-related lectin from Penaeus monodon Scientific Reports |
| title | Biochemical and structural characterization of a recombinant fibrinogen-related lectin from Penaeus monodon |
| title_full | Biochemical and structural characterization of a recombinant fibrinogen-related lectin from Penaeus monodon |
| title_fullStr | Biochemical and structural characterization of a recombinant fibrinogen-related lectin from Penaeus monodon |
| title_full_unstemmed | Biochemical and structural characterization of a recombinant fibrinogen-related lectin from Penaeus monodon |
| title_short | Biochemical and structural characterization of a recombinant fibrinogen-related lectin from Penaeus monodon |
| title_sort | biochemical and structural characterization of a recombinant fibrinogen related lectin from penaeus monodon |
| url | https://doi.org/10.1038/s41598-021-82301-5 |
| work_keys_str_mv | AT nongnuchsingrang biochemicalandstructuralcharacterizationofarecombinantfibrinogenrelatedlectinfrompenaeusmonodon AT sirasitlaophetsakunchai biochemicalandstructuralcharacterizationofarecombinantfibrinogenrelatedlectinfrompenaeusmonodon AT bichngoctran biochemicalandstructuralcharacterizationofarecombinantfibrinogenrelatedlectinfrompenaeusmonodon AT paultmatsudaira biochemicalandstructuralcharacterizationofarecombinantfibrinogenrelatedlectinfrompenaeusmonodon AT anchaleetassanakajon biochemicalandstructuralcharacterizationofarecombinantfibrinogenrelatedlectinfrompenaeusmonodon AT kittikhunwangkanont biochemicalandstructuralcharacterizationofarecombinantfibrinogenrelatedlectinfrompenaeusmonodon |