8UX6

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

8UX6 の概要

• エントリーDOI: 10.2210/pdb8ux6/pdb
• 分子名称: Fab201 light chain, Fab201 heavy chain, p67 protein, ... (10 entities in total)
• 機能のキーワード: neutralizing antibody, protozoan, sporozoite, cell invasion, immunity, west coast fever, cattle, immune system
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 103844.68

構造登録者

Singer, A.U.,Gopalsamy, A.,Fellouse, F.A.,Miersch, S.,Sidhu, S.S. (登録日: 2023-11-08, 公開日: 2024-10-16, 最終更新日: 2025-05-28)

主引用文献

Miersch, 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

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

実験手法

X-RAY DIFFRACTION (2 Å)