A multifunctional serine protease primes the malaria parasite for red blood cell invasion
Autor(a) principal: | |
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Data de Publicação: | 2009 |
Outros Autores: | , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | http://repositorio.unifesp.br/handle/11600/31385 http://dx.doi.org/10.1038/emboj.2009.22 |
Resumo: | The malaria parasite Plasmodium falciparum replicates within an intraerythrocytic parasitophorous vacuole (PV). Rupture of the host cell allows release (egress) of daughter merozoites, which invade fresh erythrocytes. We previously showed that a subtilisin-like protease called PfSUB1 regulates egress by being discharged into the PV in the final stages of merozoite development to proteolytically modify the SERA family of papain-like proteins. Here, we report that PfSUB1 has a further role in 'priming' the merozoite prior to invasion. the major protein complex on the merozoite surface comprises three proteins called merozoite surface protein 1 (MSP1), MSP6 and MSP7. We show that just before egress, all undergo proteolytic maturation by PfSUB1. Inhibition of PfSUB1 activity results in the accumulation of unprocessed MSPs on the merozoite surface, and erythrocyte invasion is significantly reduced. We propose that PfSUB1 is a multifunctional processing protease with an essential role in both egress of the malaria merozoite and remodelling of its surface in preparation for erythrocyte invasion. |
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Koussis, KonstantinosWithers-Martinez, ChrislaineYeoh, SharonChild, MatthewHackett, FionaKnuepfer, EllenJuliano, Luiz [UNIFESP]Woehlbier, UteBujard, HermannBlackman, Michael J.Natl Inst Med ResUniversidade Federal de São Paulo (UNIFESP)Univ Heidelberg2016-01-24T13:52:21Z2016-01-24T13:52:21Z2009-03-18Embo Journal. New York: Nature Publishing Group, v. 28, n. 6, p. 725-735, 2009.0261-4189http://repositorio.unifesp.br/handle/11600/31385http://dx.doi.org/10.1038/emboj.2009.22WOS000264437300013.pdf10.1038/emboj.2009.22WOS:000264437300013The malaria parasite Plasmodium falciparum replicates within an intraerythrocytic parasitophorous vacuole (PV). Rupture of the host cell allows release (egress) of daughter merozoites, which invade fresh erythrocytes. We previously showed that a subtilisin-like protease called PfSUB1 regulates egress by being discharged into the PV in the final stages of merozoite development to proteolytically modify the SERA family of papain-like proteins. Here, we report that PfSUB1 has a further role in 'priming' the merozoite prior to invasion. the major protein complex on the merozoite surface comprises three proteins called merozoite surface protein 1 (MSP1), MSP6 and MSP7. We show that just before egress, all undergo proteolytic maturation by PfSUB1. Inhibition of PfSUB1 activity results in the accumulation of unprocessed MSPs on the merozoite surface, and erythrocyte invasion is significantly reduced. We propose that PfSUB1 is a multifunctional processing protease with an essential role in both egress of the malaria merozoite and remodelling of its surface in preparation for erythrocyte invasion.Medical Research Council, UKFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Priority 1 'Life Sciences, Genomics and Biotechnology for Health' in the sixth Framework ProgrammeNatl Inst Med Res, Div Parasitol, London NW7 1AA, EnglandUniversidade Federal de São Paulo, Dept Biophys, Escola Paulista Med, São Paulo, BrazilUniv Heidelberg, Zentrum Mol Biol Heidelberg, Heidelberg, GermanyUniversidade Federal de São Paulo, Dept Biophys, Escola Paulista Med, São Paulo, BrazilPriority 1 'Life Sciences, Genomics and Biotechnology for Health' in the sixth Framework Programme: LSHP-CT-2004-503578Web of Science725-735engNature Publishing GroupEmbo JournalmalariamerozoiteMSPPfSUB1Plasmodium falciparumA multifunctional serine protease primes the malaria parasite for red blood cell invasioninfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESPORIGINALWOS000264437300013.pdfapplication/pdf481792${dspace.ui.url}/bitstream/11600/31385/1/WOS000264437300013.pdfc37de8d6ac253eab3f2bdc8796d09834MD51open accessTEXTWOS000264437300013.pdf.txtWOS000264437300013.pdf.txtExtracted texttext/plain59932${dspace.ui.url}/bitstream/11600/31385/2/WOS000264437300013.pdf.txt2e1eb4accbb759807b1c95fc8ecfc1a9MD52open access11600/313852022-09-27 11:18:57.107open accessoai:repositorio.unifesp.br:11600/31385Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652022-09-27T14:18:57Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.fl_str_mv |
A multifunctional serine protease primes the malaria parasite for red blood cell invasion |
title |
A multifunctional serine protease primes the malaria parasite for red blood cell invasion |
spellingShingle |
A multifunctional serine protease primes the malaria parasite for red blood cell invasion Koussis, Konstantinos malaria merozoite MSP PfSUB1 Plasmodium falciparum |
title_short |
A multifunctional serine protease primes the malaria parasite for red blood cell invasion |
title_full |
A multifunctional serine protease primes the malaria parasite for red blood cell invasion |
title_fullStr |
A multifunctional serine protease primes the malaria parasite for red blood cell invasion |
title_full_unstemmed |
A multifunctional serine protease primes the malaria parasite for red blood cell invasion |
title_sort |
A multifunctional serine protease primes the malaria parasite for red blood cell invasion |
author |
Koussis, Konstantinos |
author_facet |
Koussis, Konstantinos Withers-Martinez, Chrislaine Yeoh, Sharon Child, Matthew Hackett, Fiona Knuepfer, Ellen Juliano, Luiz [UNIFESP] Woehlbier, Ute Bujard, Hermann Blackman, Michael J. |
author_role |
author |
author2 |
Withers-Martinez, Chrislaine Yeoh, Sharon Child, Matthew Hackett, Fiona Knuepfer, Ellen Juliano, Luiz [UNIFESP] Woehlbier, Ute Bujard, Hermann Blackman, Michael J. |
author2_role |
author author author author author author author author author |
dc.contributor.institution.none.fl_str_mv |
Natl Inst Med Res Universidade Federal de São Paulo (UNIFESP) Univ Heidelberg |
dc.contributor.author.fl_str_mv |
Koussis, Konstantinos Withers-Martinez, Chrislaine Yeoh, Sharon Child, Matthew Hackett, Fiona Knuepfer, Ellen Juliano, Luiz [UNIFESP] Woehlbier, Ute Bujard, Hermann Blackman, Michael J. |
dc.subject.eng.fl_str_mv |
malaria merozoite MSP PfSUB1 Plasmodium falciparum |
topic |
malaria merozoite MSP PfSUB1 Plasmodium falciparum |
description |
The malaria parasite Plasmodium falciparum replicates within an intraerythrocytic parasitophorous vacuole (PV). Rupture of the host cell allows release (egress) of daughter merozoites, which invade fresh erythrocytes. We previously showed that a subtilisin-like protease called PfSUB1 regulates egress by being discharged into the PV in the final stages of merozoite development to proteolytically modify the SERA family of papain-like proteins. Here, we report that PfSUB1 has a further role in 'priming' the merozoite prior to invasion. the major protein complex on the merozoite surface comprises three proteins called merozoite surface protein 1 (MSP1), MSP6 and MSP7. We show that just before egress, all undergo proteolytic maturation by PfSUB1. Inhibition of PfSUB1 activity results in the accumulation of unprocessed MSPs on the merozoite surface, and erythrocyte invasion is significantly reduced. We propose that PfSUB1 is a multifunctional processing protease with an essential role in both egress of the malaria merozoite and remodelling of its surface in preparation for erythrocyte invasion. |
publishDate |
2009 |
dc.date.issued.fl_str_mv |
2009-03-18 |
dc.date.accessioned.fl_str_mv |
2016-01-24T13:52:21Z |
dc.date.available.fl_str_mv |
2016-01-24T13:52:21Z |
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info:eu-repo/semantics/publishedVersion |
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info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
Embo Journal. New York: Nature Publishing Group, v. 28, n. 6, p. 725-735, 2009. |
dc.identifier.uri.fl_str_mv |
http://repositorio.unifesp.br/handle/11600/31385 http://dx.doi.org/10.1038/emboj.2009.22 |
dc.identifier.issn.none.fl_str_mv |
0261-4189 |
dc.identifier.file.none.fl_str_mv |
WOS000264437300013.pdf |
dc.identifier.doi.none.fl_str_mv |
10.1038/emboj.2009.22 |
dc.identifier.wos.none.fl_str_mv |
WOS:000264437300013 |
identifier_str_mv |
Embo Journal. New York: Nature Publishing Group, v. 28, n. 6, p. 725-735, 2009. 0261-4189 WOS000264437300013.pdf 10.1038/emboj.2009.22 WOS:000264437300013 |
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http://repositorio.unifesp.br/handle/11600/31385 http://dx.doi.org/10.1038/emboj.2009.22 |
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Nature Publishing Group |
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Nature Publishing Group |
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