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8UX6

Structure of Fab201 with a T. parva sporozoite neutralizing B cell epitope of p67

Summary for 8UX6
Entry DOI10.2210/pdb8ux6/pdb
DescriptorFab201 light chain, Fab201 heavy chain, p67 protein, ... (10 entities in total)
Functional Keywordsneutralizing antibody, protozoan, sporozoite, cell invasion, immunity, west coast fever, cattle, immune system
Biological sourceHomo sapiens (human)
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Total number of polymer chains6
Total formula weight103844.68
Authors
Singer, A.U.,Gopalsamy, A.,Fellouse, F.A.,Miersch, S.,Sidhu, S.S. (deposition date: 2023-11-08, release date: 2024-10-16, Last modification date: 2025-05-28)
Primary citationMiersch, S.,Singer, A.U.,Chen, C.,Fellouse, F.,Gopalsamy, A.,Costa, L.S.E.,Lacasta, A.,Chege, H.,Chege, N.,Nene, V.,Sidhu, S.S.
Molecular characterization of a synthetic neutralizing antibody targeting p67 of Theileria parva.
Protein Sci., 34:e70153-e70153, 2025
Cited by
PubMed Abstract: The Theileria parva sporozoite surface antigen p67 is a target of the bovine humoral immune response that generates antibodies capable of providing protection against subsequent infection. As a result, p67 has been the subject of efforts aimed at the development of an anti-sporozoite subunit vaccine. Previous studies have identified neutralizing epitopes in the N- and C-terminal regions of the full-length protein and shown that immunization with a C-terminal fragment of p67 (p67C) alone is capable of eliciting protection. To identify additional neutralizing epitopes in p67C, selections were conducted against it using a phage-displayed synthetic antibody library. An antibody that neutralized the sporozoite in vitro was identified, and the crystal structure of a Fab:peptide complex was elucidated. Mutagenesis studies aimed at validating and further characterizing the Fab:peptide interaction identified critical residues involved in binding and neutralization. This study also validates distinct epitopes for previously reported neutralizing antibodies.
PubMed: 40384600
DOI: 10.1002/pro.70153
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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数据于2025-07-23公开中

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