Cleavage of hemoglobin by hookworm cathepsin D aspartic proteases and its potential contribution to host specificity.

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dc.contributor.author Williamson, AL
dc.contributor.author Brindley, PJ
dc.contributor.author Abbenante, G
dc.contributor.author Prociv, P
dc.contributor.author Berry, C
dc.contributor.author Girdwood, K
dc.contributor.author Pritchard, DI
dc.contributor.author Fairlie, DP
dc.contributor.author Hotez, PJ
dc.contributor.author Dalton, JP
dc.contributor.author Loukas, A
dc.date.accessioned 2010-05-28T09:44:52Z
dc.date.issued 2002-09
dc.identifier.citation FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2002, 16 (11), pp. 1458 - 1460
dc.identifier.issn 0892-6638
dc.identifier.other C1UNSUBMIT en_US
dc.identifier.uri http://hdl.handle.net/10453/8693
dc.description.abstract Hookworms routinely reach the gut of nonpermissive hosts but fail to successfully feed, develop, and reproduce. To investigate the effects of host-parasite coevolution on the ability of hookworms to feed in nonpermissive hosts, we cloned and expressed aspartic proteases from canine and human hookworms. We show here that a cathepsin D-like protease from the canine hookworm Ancylosotoma caninum (Ac-APR-1) and the orthologous protease from the human hookworm Necator americanus (Na-APR-1) are expressed in the gut and probably exert their proteolytic activity extracellularly. Both proteases were detected immunologically and enzymatically in somatic extracts of adult worms. The two proteases were expressed in baculovirus, and both cleaved human and dog hemoglobin (Hb) in vitro. Each protease digested Hb from its permissive host between twofold (whole molecule) and sixfold (synthetic peptides) more efficiently than Hb from the nonpermissive host, despite the two proteases' having identical residues lining their active site clefts. Furthermore, both proteases cleaved Hb at numerous distinct sites and showed different substrate preferences. The findings suggest that the paradigm of matching the molecular structure of the food source within a host to the molecular structure of the catabolic proteases of the parasite is an important contributing factor for host-parasite compatibility and host species range.
dc.format Print-Electronic
dc.language eng
dc.title Cleavage of hemoglobin by hookworm cathepsin D aspartic proteases and its potential contribution to host specificity.
dc.type Journal Article
dc.parent FASEB journal : official publication of the Federation of American Societies for Experimental Biology
dc.journal.volume 11
dc.journal.volume 16
dc.journal.number 9 en_US
dc.publocation Bethesda, USA en_US
dc.identifier.startpage 1458 en_US
dc.identifier.endpage 0 en_US
dc.cauo.name SCI.Medical and Molecular Biosciences en_US
dc.conference Verified OK en_US
dc.for 060502 Infectious Agents
dc.for 060107 Enzymes
dc.for 110803 Medical Parasitology
dc.personcode 030896
dc.percentage 40 en_US
dc.classification.name Enzymes en_US
dc.classification.type FOR-08 en_US
dc.edition en_US
dc.custom en_US
dc.date.activity en_US
dc.location.activity en_US
dc.description.keywords Human Eosinophilic Enteritis; Adult Haemonchus-contortus; Blood-feeding Parasites; Ancylostoma-caninum; Plasmodium-falciparum; Caenorhabditis-elegans; In-vivo; Degradation; Infection; Identification en_US
dc.description.keywords Digestive System
dc.description.keywords Animals
dc.description.keywords Dogs
dc.description.keywords Humans
dc.description.keywords Ancylostomatoidea
dc.description.keywords Cathepsin D
dc.description.keywords Peptides
dc.description.keywords Hemoglobins
dc.description.keywords Recombinant Proteins
dc.description.keywords Species Specificity
dc.description.keywords Substrate Specificity
dc.description.keywords Models, Biological
dc.description.keywords Host-Parasite Interactions
dc.description.keywords Animals
dc.description.keywords Dogs
dc.description.keywords Humans
dc.description.keywords Ancylostomatoidea
dc.description.keywords Peptides
dc.description.keywords Cathepsin D
dc.description.keywords Recombinant Proteins
dc.description.keywords Substrate Specificity
dc.description.keywords Species Specificity
dc.description.keywords Host-Parasite Interactions
dc.description.keywords Models, Biological
dc.description.keywords Digestive System
dc.description.keywords Hemoglobins
dc.description.keywords Animals
dc.description.keywords Dogs
dc.description.keywords Humans
dc.description.keywords Ancylostomatoidea
dc.description.keywords Peptides
dc.description.keywords Cathepsin D
dc.description.keywords Recombinant Proteins
dc.description.keywords Substrate Specificity
dc.description.keywords Species Specificity
dc.description.keywords Host-Parasite Interactions
dc.description.keywords Models, Biological
dc.description.keywords Digestive System
dc.description.keywords Hemoglobins
pubs.embargo.period Not known
pubs.organisational-group /University of Technology Sydney
pubs.organisational-group /University of Technology Sydney/Faculty of Science


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