2026-10-10T20:01:37Z https://api.figshare.com/v2/oai

oai:figshare.com:article/33968536 2026-09-22T18:00:57Z category_8 category_12 category_24 category_272 category_39 category_46 category_734 category_132 category_134 portal_5 item_type_3 month_year_09_2026

<p>Blocking ELISA inter-assay repeatability test.</p> Lijuan Zheng (3984380) Wenjing Zhi (6257582) Mengjie Chu (25091292) Xinyi Zhou (3594002) Yong Fu (699744) Chen Xin (704623) Baoping Li (19451408) Lingzhi Pengmao (25091295) Zhendong Xin (25091298) Yihui Wu (1707376) Xuejun Ji (25091301) Anni Zhang (9647964) Changjie Qian (25091304) Zhen Wang (72451) Chenye Jin (15251488) Yun Han (718961) Zhijun Zhang (315079) Fuyun Chen (25091307) Gongguan Liu (777048) Microbiology Cell Biology Evolutionary Biology Environmental Sciences not elsewhere classified Ecology Immunology Biological Sciences not elsewhere classified Infectious Diseases Virology two elisa methods structural modeling revealed highly abundant excretory div >< p α ‑ helix strictly conserved within mammalian host sequences surface ‑ exposed echinococcus multilocularis </ 193 </ sup 189 </ sup 178 </ sup 174 </ sup early infection stage exposed linear epitopes multilocularis </ echinococcus </ conserved surface intra ‑ linear range larval stage intermediate host thioredoxin peroxidase potential utility mouse feces monoclonal antibody monoclonal antibodies markedly divergent invasive diagnosis invasive detection intermediate hosts flexible loop fecal samples established using detection rate conformations favorable based approaches antibody recognition alveolar echinococcosis 10 %, <div><p>Alveolar echinococcosis (AE) is a severe zoonotic parasitic disease caused by the larval stage of <i>Echinococcus multilocularis</i>, for which early and accurate diagnosis remains challenging. In this study, we targeted <i>E. multilocularis</i> thioredoxin peroxidase (EmTPx), a highly abundant excretory/secretory protein conserved across the genus <i>Echinococcus</i>, for diagnostic development. Monoclonal antibodies (mAbs) against EmTPx were generated, and two linear B‑cell epitopes, ¹⁷⁴HPGSK¹⁷⁸ and ¹⁸⁹SFMSS¹⁹³, were identified. Both epitopes are strictly conserved within <i>Echinococcus</i> but markedly divergent from mammalian host sequences. Structural modeling revealed that the epitopes are surface‑exposed, with ¹⁷⁴HPGSK¹⁷⁸ located in a flexible loop and ¹⁸⁹SFMSS¹⁹³ adjacent to an α‑helix, conformations favorable for antibody recognition. Two ELISA methods were established using the epitope‑specific mAbs. The blocking ELISA showed moderate diagnostic performance. More importantly, the sandwich ELISA enabled direct detection of EmTPx antigen in fecal samples of intermediate hosts, revealing a detection rate of 85% in mouse feces at an early infection stage. With a linear range of 0–250 ng/mL, a cutoff of 0.1724, and intra‑ and inter‑assay precision below 10%, this sandwich ELISA demonstrated robust analytical performance. In conclusion, this proof-of-concept study identifies two evolutionarily conserved and structurally exposed EmTPx epitopes and demonstrates their potential utility for the development of monoclonal antibody-based approaches for non-invasive detection of echinococcosis.</p></div> 2026-09-22T18:00:20Z Dataset Dataset 10.1371/journal.pntd.0014755.t004 https://figshare.com/articles/dataset/_p_Blocking_ELISA_inter-assay_repeatability_test_p_/33968536 CC BY 4.0