Screening and Interaction Analysis of Shark-Derived Nanobodies against Crayfish Major Allergen Pro c 2.
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| Auteurs principaux: | , , , , , , , , , |
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| Format: | Artículo científico |
| Langue: | en |
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Journal of agricultural and food chemistry
2025
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| _version_ | 1868266214118129666 |
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| author | Yang, Yang He, Xin-Rong He, Si-Yang Lin, Jin-Jin Li, Fa-Jie Chen, Jin-Li Gu, Shi-Nong Jin, Tengchuan Chen, Gui-Xia Liu, Guang-Ming |
| author_facet | Yang, Yang He, Xin-Rong He, Si-Yang Lin, Jin-Jin Li, Fa-Jie Chen, Jin-Li Gu, Shi-Nong Jin, Tengchuan Chen, Gui-Xia Liu, Guang-Ming Yang, Yang He, Xin-Rong He, Si-Yang Lin, Jin-Jin Li, Fa-Jie Chen, Jin-Li Gu, Shi-Nong Jin, Tengchuan Chen, Gui-Xia Liu, Guang-Ming |
| collection | PubMed - marine biology |
| contents | Screening and Interaction Analysis of Shark-Derived Nanobodies against Crayfish Major Allergen Pro c 2. Yang, Yang He, Xin-Rong He, Si-Yang Lin, Jin-Jin Li, Fa-Jie Chen, Jin-Li Gu, Shi-Nong Jin, Tengchuan Chen, Gui-Xia Liu, Guang-Ming Animals Astacoidea Sharks Allergens Humans Single-Domain Antibodies Arginine Kinase Immunoglobulin E HEK293 Cells Arthropod Proteins Molecular Dynamics Simulation Amino Acid Sequence Pro c 2 (arginine kinase) is a major allergen in crayfish (). Shark-derived variable domains of new antigen receptors (VNARs) have advantages in developing allergen detection and immunotherapy. This study constructed a VNAR domain library from immunized with Pro c 2. Three VNARs (VNAR-11, VNAR-20, and VNAR-29) against Pro c 2 obtained by screening the library were expressed in the HEK293F cells, fusing with the immunoglobulin (Ig) G1 Fc fragment (VNAR-Fc-11, VNAR-Fc-29, and VNAR-Fc-20). The VNAR-Fc fusions bound to Pro c 2 with an affinity ranging from 0.2131 ∼ 465.3 μM, with the ability to inhibit patients' IgE binding to Pro c 2. VNAR-20 and VNAR-29 displayed more stable binding with Pro c 2 during molecular dynamics simulation. The binding sites of the VNARs are distributed in the conserved IgE epitopes of arginine kinase. These achievements indicate the application potential of VNARs in allergen detection and allergy therapeutics. |
| format | Artículo científico |
| id | pubmed_40256922 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Journal of agricultural and food chemistry |
| record_format | pubmed |
| spellingShingle | Screening and Interaction Analysis of Shark-Derived Nanobodies against Crayfish Major Allergen Pro c 2. Yang, Yang He, Xin-Rong He, Si-Yang Lin, Jin-Jin Li, Fa-Jie Chen, Jin-Li Gu, Shi-Nong Jin, Tengchuan Chen, Gui-Xia Liu, Guang-Ming Animals Astacoidea Sharks Allergens Humans Single-Domain Antibodies Arginine Kinase Immunoglobulin E HEK293 Cells Arthropod Proteins Molecular Dynamics Simulation Amino Acid Sequence Screening and Interaction Analysis of Shark-Derived Nanobodies against Crayfish Major Allergen Pro c 2. Yang, Yang He, Xin-Rong He, Si-Yang Lin, Jin-Jin Li, Fa-Jie Chen, Jin-Li Gu, Shi-Nong Jin, Tengchuan Chen, Gui-Xia Liu, Guang-Ming Animals Astacoidea Sharks Allergens Humans Single-Domain Antibodies Arginine Kinase Immunoglobulin E HEK293 Cells Arthropod Proteins Molecular Dynamics Simulation Amino Acid Sequence Pro c 2 (arginine kinase) is a major allergen in crayfish (). Shark-derived variable domains of new antigen receptors (VNARs) have advantages in developing allergen detection and immunotherapy. This study constructed a VNAR domain library from immunized with Pro c 2. Three VNARs (VNAR-11, VNAR-20, and VNAR-29) against Pro c 2 obtained by screening the library were expressed in the HEK293F cells, fusing with the immunoglobulin (Ig) G1 Fc fragment (VNAR-Fc-11, VNAR-Fc-29, and VNAR-Fc-20). The VNAR-Fc fusions bound to Pro c 2 with an affinity ranging from 0.2131 ∼ 465.3 μM, with the ability to inhibit patients' IgE binding to Pro c 2. VNAR-20 and VNAR-29 displayed more stable binding with Pro c 2 during molecular dynamics simulation. The binding sites of the VNARs are distributed in the conserved IgE epitopes of arginine kinase. These achievements indicate the application potential of VNARs in allergen detection and allergy therapeutics. |
| title | Screening and Interaction Analysis of Shark-Derived Nanobodies against Crayfish Major Allergen Pro c 2. |
| topic | Animals Astacoidea Sharks Allergens Humans Single-Domain Antibodies Arginine Kinase Immunoglobulin E HEK293 Cells Arthropod Proteins Molecular Dynamics Simulation Amino Acid Sequence |
| url | https://pubmed.ncbi.nlm.nih.gov/40256922/ |