Aspartic protease activities of schistosomes cleave mammalian hemoglobins in a host-specific manner

Detalhes bibliográficos
Autor(a) principal: Koehler,Jeffrey W
Data de Publicação: 2007
Outros Autores: Morales,Maria E, Shelby,Bryan D, Brindley,Paul J
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Memórias do Instituto Oswaldo Cruz
Texto Completo: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762007000100014
Resumo: We examined the efficiency of digestion of hemoglobin from four mammalian species, human, cow, sheep, and horse by acidic extracts of mixed sex adults of Schistosoma japonicum and S. mansoni. Activity ascribable to aspartic protease(s) from S. japonicum and S. mansoni cleaved human hemoglobin. In addition, aspartic protease activities from S. japonicum cleaved hemoglobin from bovine, sheep, and horse blood more efficiently than did the activity from extracts of S. mansoni. These findings support the hypothesis that substrate specificity of hemoglobin-degrading proteases employed by blood feeding helminth parasites influences parasite host species range; differences in amino acid sequences in key sites of the parasite proteases interact less or more efficiently with the hemoglobins of permissive or non-permissive hosts.
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spelling Aspartic protease activities of schistosomes cleave mammalian hemoglobins in a host-specific mannerschistosomehemoglobinaspartic proteasecathepsin Dhost specificityhost rangeWe examined the efficiency of digestion of hemoglobin from four mammalian species, human, cow, sheep, and horse by acidic extracts of mixed sex adults of Schistosoma japonicum and S. mansoni. Activity ascribable to aspartic protease(s) from S. japonicum and S. mansoni cleaved human hemoglobin. In addition, aspartic protease activities from S. japonicum cleaved hemoglobin from bovine, sheep, and horse blood more efficiently than did the activity from extracts of S. mansoni. These findings support the hypothesis that substrate specificity of hemoglobin-degrading proteases employed by blood feeding helminth parasites influences parasite host species range; differences in amino acid sequences in key sites of the parasite proteases interact less or more efficiently with the hemoglobins of permissive or non-permissive hosts.Instituto Oswaldo Cruz, Ministério da Saúde2007-02-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762007000100014Memórias do Instituto Oswaldo Cruz v.102 n.1 2007reponame:Memórias do Instituto Oswaldo Cruzinstname:Fundação Oswaldo Cruzinstacron:FIOCRUZ10.1590/S0074-02762007000100014info:eu-repo/semantics/openAccessKoehler,Jeffrey WMorales,Maria EShelby,Bryan DBrindley,Paul Jeng2020-04-25T17:49:48Zhttp://www.scielo.br/oai/scielo-oai.php0074-02761678-8060opendoar:null2020-04-26 02:14:29.349Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruztrue
dc.title.none.fl_str_mv Aspartic protease activities of schistosomes cleave mammalian hemoglobins in a host-specific manner
title Aspartic protease activities of schistosomes cleave mammalian hemoglobins in a host-specific manner
spellingShingle Aspartic protease activities of schistosomes cleave mammalian hemoglobins in a host-specific manner
Koehler,Jeffrey W
schistosome
hemoglobin
aspartic protease
cathepsin D
host specificity
host range
title_short Aspartic protease activities of schistosomes cleave mammalian hemoglobins in a host-specific manner
title_full Aspartic protease activities of schistosomes cleave mammalian hemoglobins in a host-specific manner
title_fullStr Aspartic protease activities of schistosomes cleave mammalian hemoglobins in a host-specific manner
title_full_unstemmed Aspartic protease activities of schistosomes cleave mammalian hemoglobins in a host-specific manner
title_sort Aspartic protease activities of schistosomes cleave mammalian hemoglobins in a host-specific manner
author Koehler,Jeffrey W
author_facet Koehler,Jeffrey W
Morales,Maria E
Shelby,Bryan D
Brindley,Paul J
author_role author
author2 Morales,Maria E
Shelby,Bryan D
Brindley,Paul J
author2_role author
author
author
dc.contributor.author.fl_str_mv Koehler,Jeffrey W
Morales,Maria E
Shelby,Bryan D
Brindley,Paul J
dc.subject.por.fl_str_mv schistosome
hemoglobin
aspartic protease
cathepsin D
host specificity
host range
topic schistosome
hemoglobin
aspartic protease
cathepsin D
host specificity
host range
dc.description.none.fl_txt_mv We examined the efficiency of digestion of hemoglobin from four mammalian species, human, cow, sheep, and horse by acidic extracts of mixed sex adults of Schistosoma japonicum and S. mansoni. Activity ascribable to aspartic protease(s) from S. japonicum and S. mansoni cleaved human hemoglobin. In addition, aspartic protease activities from S. japonicum cleaved hemoglobin from bovine, sheep, and horse blood more efficiently than did the activity from extracts of S. mansoni. These findings support the hypothesis that substrate specificity of hemoglobin-degrading proteases employed by blood feeding helminth parasites influences parasite host species range; differences in amino acid sequences in key sites of the parasite proteases interact less or more efficiently with the hemoglobins of permissive or non-permissive hosts.
description We examined the efficiency of digestion of hemoglobin from four mammalian species, human, cow, sheep, and horse by acidic extracts of mixed sex adults of Schistosoma japonicum and S. mansoni. Activity ascribable to aspartic protease(s) from S. japonicum and S. mansoni cleaved human hemoglobin. In addition, aspartic protease activities from S. japonicum cleaved hemoglobin from bovine, sheep, and horse blood more efficiently than did the activity from extracts of S. mansoni. These findings support the hypothesis that substrate specificity of hemoglobin-degrading proteases employed by blood feeding helminth parasites influences parasite host species range; differences in amino acid sequences in key sites of the parasite proteases interact less or more efficiently with the hemoglobins of permissive or non-permissive hosts.
publishDate 2007
dc.date.none.fl_str_mv 2007-02-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762007000100014
url http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762007000100014
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0074-02762007000100014
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Instituto Oswaldo Cruz, Ministério da Saúde
publisher.none.fl_str_mv Instituto Oswaldo Cruz, Ministério da Saúde
dc.source.none.fl_str_mv Memórias do Instituto Oswaldo Cruz v.102 n.1 2007
reponame:Memórias do Instituto Oswaldo Cruz
instname:Fundação Oswaldo Cruz
instacron:FIOCRUZ
reponame_str Memórias do Instituto Oswaldo Cruz
collection Memórias do Instituto Oswaldo Cruz
instname_str Fundação Oswaldo Cruz
instacron_str FIOCRUZ
institution FIOCRUZ
repository.name.fl_str_mv Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruz
repository.mail.fl_str_mv
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