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6ROW

Haemonchus galactose containing glycoprotein complex

Summary for 6ROW
Entry DOI10.2210/pdb6row/pdb
EMDB information4975
DescriptorPutative zinc metallopeptidase, Parasite pepsinogen, Cysteine Protease (3 entities in total)
Functional Keywordsmulti-protease complex, hydrolase
Biological sourceHaemonchus contortus (Barber pole worm)
More
Total number of polymer chains7
Total formula weight456215.68
Authors
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. (deposition date: 2019-05-13, release date: 2020-03-25, Last modification date: 2024-11-06)
Primary citationScarff, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.5 Å)
Structure validation

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