6ROW

Haemonchus galactose containing glycoprotein complex

6ROW の概要

• エントリーDOI: 10.2210/pdb6row/pdb
• EMDBエントリー: 4975
• 分子名称: Putative zinc metallopeptidase, Parasite pepsinogen, Cysteine Protease (3 entities in total)
• 機能のキーワード: multi-protease complex, hydrolase
• 由来する生物種: Haemonchus contortus (Barber pole worm); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 456215.68

構造登録者

Scarff, C.A.,Thompson, R.F.,Newlands, G.F.J.,Jamson, H.,Kennaway, C.,da Silva, V.J.,Rabelo, E.M.,Song, C.F.,Trinick, J.,Smith, W.D.,Muench, S.P. (登録日: 2019-05-13, 公開日: 2020-03-25, 最終更新日: 2024-11-06)

主引用文献

Scarff, C.A.,Thompson, R.F.,Newlands, G.F.J.,Jamson, A.H.,Kennaway, C.,da Silva, V.J.,Rabelo, E.M.,Song, C.F.,Trinick, J.,Smith, W.D.,Muench, S.P.
Structure of the protective nematode protease complex H-gal-GP and its conservation across roundworm parasites.
Plos Pathog., 16:e1008465-e1008465, 2020

PubMed Abstract: Roundworm parasite infections are a major cause of human and livestock disease worldwide and a threat to global food security. Disease control currently relies on anthelmintic drugs to which roundworms are becoming increasingly resistant. An alternative approach is control by vaccination and 'hidden antigens', components of the worm gut not encountered by the infected host, have been exploited to produce Barbervax, the first commercial vaccine for a gut dwelling nematode of any host. Here we present the structure of H-gal-GP, a hidden antigen from Haemonchus contortus, the Barber's Pole worm, and a major component of Barbervax. We demonstrate its novel architecture, subunit composition and topology, flexibility and heterogeneity using cryo-electron microscopy, mass spectrometry, and modelling. Importantly, we demonstrate that complexes with the same architecture are present in other Strongylid roundworm parasites including human hookworm. This suggests a common ancestry and the potential for development of a unified hidden antigen vaccine.

PubMed: 32271834
DOI: 10.1371/journal.ppat.1008465

実験手法

ELECTRON MICROSCOPY (4.5 Å)