Critical Role for Heat Shock Protein 20 (HSP20) in Migration of Malarial Sporozoites
- Autores
- Montagna, Georgina Nuri; Buscaglia, Carlos Andres; Münter, Sylvia; Goosmann, Christian; Frischknecht, Friedrich; Brinkmann, Volker; Matuschewski, Kai
- Año de publicación
- 2012
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Plasmodium sporozoites, single cell eukaryotic pathogens, use their own actin/myosin-based motor machinery for life cycle progression, which includes forward locomotion, penetration of cellular barriers, and invasion of target cells. To display fast gliding motility, the parasite uses a high turnover of actin polymerization and adhesion sites. Paradoxically, only a few classic actin regulatory proteins appear to be encoded in the Plasmodium genome. Small heat shock proteins have been associated with cytoskeleton modulation in various biological processes. In this study, we identify HSP20 as a novel player in Plasmodium motility and provide molecular genetics evidence for a critical role of a small heat shock protein in cell traction and motility. We demonstrate that HSP20 ablation profoundly affects sporozoite-substrate adhesion, which translates into aberrant speed and directionality in vitro. Loss of HSP20 function impairs migration in the host, an important sporozoite trait required to find a blood vessel and reach the liver after being deposited in the skin by the mosquito. Our study also shows that fast locomotion of sporozoites is crucial during natural malaria transmission.sporozoites, single cell eukaryotic pathogens, use their own actin/myosin-based motor machinery for life cycle progression, which includes forward locomotion, penetration of cellular barriers, and invasion of target cells. To display fast gliding motility, the parasite uses a high turnover of actin polymerization and adhesion sites. Paradoxically, only a few classic actin regulatory proteins appear to be encoded in the Plasmodium genome. Small heat shock proteins have been associated with cytoskeleton modulation in various biological processes. In this study, we identify HSP20 as a novel player in Plasmodium motility and provide molecular genetics evidence for a critical role of a small heat shock protein in cell traction and motility. We demonstrate that HSP20 ablation profoundly affects sporozoite-substrate adhesion, which translates into aberrant speed and directionality in vitro. Loss of HSP20 function impairs migration in the host, an important sporozoite trait required to find a blood vessel and reach the liver after being deposited in the skin by the mosquito. Our study also shows that fast locomotion of sporozoites is crucial during natural malaria transmission.
Fil: Montagna, Georgina Nuri. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina. Max Planck Institute for Infection Biology; Alemania
Fil: Buscaglia, Carlos Andres. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina
Fil: Münter, Sylvia. Ruprecht Karls Universitat Heidelberg; Alemania
Fil: Goosmann, Christian. Max Planck Institute for Infection Biology; Alemania
Fil: Frischknecht, Friedrich. Ruprecht Karls Universitat Heidelberg; Alemania
Fil: Brinkmann, Volker. Max Planck Institute for Infection Biology; Alemania
Fil: Matuschewski, Kai. Max Planck Institute for Infection Biology; Alemania - Materia
-
Plasmodium
Sporozoite
Motility
Hsp20 - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/269123
Ver los metadatos del registro completo
id |
CONICETDig_8a59f2a166e015f3d4449e1baa3db0e0 |
---|---|
oai_identifier_str |
oai:ri.conicet.gov.ar:11336/269123 |
network_acronym_str |
CONICETDig |
repository_id_str |
3498 |
network_name_str |
CONICET Digital (CONICET) |
spelling |
Critical Role for Heat Shock Protein 20 (HSP20) in Migration of Malarial SporozoitesMontagna, Georgina NuriBuscaglia, Carlos AndresMünter, SylviaGoosmann, ChristianFrischknecht, FriedrichBrinkmann, VolkerMatuschewski, KaiPlasmodiumSporozoiteMotilityHsp20https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Plasmodium sporozoites, single cell eukaryotic pathogens, use their own actin/myosin-based motor machinery for life cycle progression, which includes forward locomotion, penetration of cellular barriers, and invasion of target cells. To display fast gliding motility, the parasite uses a high turnover of actin polymerization and adhesion sites. Paradoxically, only a few classic actin regulatory proteins appear to be encoded in the Plasmodium genome. Small heat shock proteins have been associated with cytoskeleton modulation in various biological processes. In this study, we identify HSP20 as a novel player in Plasmodium motility and provide molecular genetics evidence for a critical role of a small heat shock protein in cell traction and motility. We demonstrate that HSP20 ablation profoundly affects sporozoite-substrate adhesion, which translates into aberrant speed and directionality in vitro. Loss of HSP20 function impairs migration in the host, an important sporozoite trait required to find a blood vessel and reach the liver after being deposited in the skin by the mosquito. Our study also shows that fast locomotion of sporozoites is crucial during natural malaria transmission.sporozoites, single cell eukaryotic pathogens, use their own actin/myosin-based motor machinery for life cycle progression, which includes forward locomotion, penetration of cellular barriers, and invasion of target cells. To display fast gliding motility, the parasite uses a high turnover of actin polymerization and adhesion sites. Paradoxically, only a few classic actin regulatory proteins appear to be encoded in the Plasmodium genome. Small heat shock proteins have been associated with cytoskeleton modulation in various biological processes. In this study, we identify HSP20 as a novel player in Plasmodium motility and provide molecular genetics evidence for a critical role of a small heat shock protein in cell traction and motility. We demonstrate that HSP20 ablation profoundly affects sporozoite-substrate adhesion, which translates into aberrant speed and directionality in vitro. Loss of HSP20 function impairs migration in the host, an important sporozoite trait required to find a blood vessel and reach the liver after being deposited in the skin by the mosquito. Our study also shows that fast locomotion of sporozoites is crucial during natural malaria transmission.Fil: Montagna, Georgina Nuri. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina. Max Planck Institute for Infection Biology; AlemaniaFil: Buscaglia, Carlos Andres. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); ArgentinaFil: Münter, Sylvia. Ruprecht Karls Universitat Heidelberg; AlemaniaFil: Goosmann, Christian. Max Planck Institute for Infection Biology; AlemaniaFil: Frischknecht, Friedrich. Ruprecht Karls Universitat Heidelberg; AlemaniaFil: Brinkmann, Volker. Max Planck Institute for Infection Biology; AlemaniaFil: Matuschewski, Kai. Max Planck Institute for Infection Biology; AlemaniaAmerican Society for Biochemistry and Molecular Biology2012-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/269123Montagna, Georgina Nuri; Buscaglia, Carlos Andres; Münter, Sylvia; Goosmann, Christian; Frischknecht, Friedrich; et al.; Critical Role for Heat Shock Protein 20 (HSP20) in Migration of Malarial Sporozoites; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 287; 4; 1-2012; 2410-24220021-9258CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0021925820532031info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M111.302109info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:16:07Zoai:ri.conicet.gov.ar:11336/269123instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:16:07.724CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Critical Role for Heat Shock Protein 20 (HSP20) in Migration of Malarial Sporozoites |
title |
Critical Role for Heat Shock Protein 20 (HSP20) in Migration of Malarial Sporozoites |
spellingShingle |
Critical Role for Heat Shock Protein 20 (HSP20) in Migration of Malarial Sporozoites Montagna, Georgina Nuri Plasmodium Sporozoite Motility Hsp20 |
title_short |
Critical Role for Heat Shock Protein 20 (HSP20) in Migration of Malarial Sporozoites |
title_full |
Critical Role for Heat Shock Protein 20 (HSP20) in Migration of Malarial Sporozoites |
title_fullStr |
Critical Role for Heat Shock Protein 20 (HSP20) in Migration of Malarial Sporozoites |
title_full_unstemmed |
Critical Role for Heat Shock Protein 20 (HSP20) in Migration of Malarial Sporozoites |
title_sort |
Critical Role for Heat Shock Protein 20 (HSP20) in Migration of Malarial Sporozoites |
dc.creator.none.fl_str_mv |
Montagna, Georgina Nuri Buscaglia, Carlos Andres Münter, Sylvia Goosmann, Christian Frischknecht, Friedrich Brinkmann, Volker Matuschewski, Kai |
author |
Montagna, Georgina Nuri |
author_facet |
Montagna, Georgina Nuri Buscaglia, Carlos Andres Münter, Sylvia Goosmann, Christian Frischknecht, Friedrich Brinkmann, Volker Matuschewski, Kai |
author_role |
author |
author2 |
Buscaglia, Carlos Andres Münter, Sylvia Goosmann, Christian Frischknecht, Friedrich Brinkmann, Volker Matuschewski, Kai |
author2_role |
author author author author author author |
dc.subject.none.fl_str_mv |
Plasmodium Sporozoite Motility Hsp20 |
topic |
Plasmodium Sporozoite Motility Hsp20 |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Plasmodium sporozoites, single cell eukaryotic pathogens, use their own actin/myosin-based motor machinery for life cycle progression, which includes forward locomotion, penetration of cellular barriers, and invasion of target cells. To display fast gliding motility, the parasite uses a high turnover of actin polymerization and adhesion sites. Paradoxically, only a few classic actin regulatory proteins appear to be encoded in the Plasmodium genome. Small heat shock proteins have been associated with cytoskeleton modulation in various biological processes. In this study, we identify HSP20 as a novel player in Plasmodium motility and provide molecular genetics evidence for a critical role of a small heat shock protein in cell traction and motility. We demonstrate that HSP20 ablation profoundly affects sporozoite-substrate adhesion, which translates into aberrant speed and directionality in vitro. Loss of HSP20 function impairs migration in the host, an important sporozoite trait required to find a blood vessel and reach the liver after being deposited in the skin by the mosquito. Our study also shows that fast locomotion of sporozoites is crucial during natural malaria transmission.sporozoites, single cell eukaryotic pathogens, use their own actin/myosin-based motor machinery for life cycle progression, which includes forward locomotion, penetration of cellular barriers, and invasion of target cells. To display fast gliding motility, the parasite uses a high turnover of actin polymerization and adhesion sites. Paradoxically, only a few classic actin regulatory proteins appear to be encoded in the Plasmodium genome. Small heat shock proteins have been associated with cytoskeleton modulation in various biological processes. In this study, we identify HSP20 as a novel player in Plasmodium motility and provide molecular genetics evidence for a critical role of a small heat shock protein in cell traction and motility. We demonstrate that HSP20 ablation profoundly affects sporozoite-substrate adhesion, which translates into aberrant speed and directionality in vitro. Loss of HSP20 function impairs migration in the host, an important sporozoite trait required to find a blood vessel and reach the liver after being deposited in the skin by the mosquito. Our study also shows that fast locomotion of sporozoites is crucial during natural malaria transmission. Fil: Montagna, Georgina Nuri. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina. Max Planck Institute for Infection Biology; Alemania Fil: Buscaglia, Carlos Andres. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina Fil: Münter, Sylvia. Ruprecht Karls Universitat Heidelberg; Alemania Fil: Goosmann, Christian. Max Planck Institute for Infection Biology; Alemania Fil: Frischknecht, Friedrich. Ruprecht Karls Universitat Heidelberg; Alemania Fil: Brinkmann, Volker. Max Planck Institute for Infection Biology; Alemania Fil: Matuschewski, Kai. Max Planck Institute for Infection Biology; Alemania |
description |
Plasmodium sporozoites, single cell eukaryotic pathogens, use their own actin/myosin-based motor machinery for life cycle progression, which includes forward locomotion, penetration of cellular barriers, and invasion of target cells. To display fast gliding motility, the parasite uses a high turnover of actin polymerization and adhesion sites. Paradoxically, only a few classic actin regulatory proteins appear to be encoded in the Plasmodium genome. Small heat shock proteins have been associated with cytoskeleton modulation in various biological processes. In this study, we identify HSP20 as a novel player in Plasmodium motility and provide molecular genetics evidence for a critical role of a small heat shock protein in cell traction and motility. We demonstrate that HSP20 ablation profoundly affects sporozoite-substrate adhesion, which translates into aberrant speed and directionality in vitro. Loss of HSP20 function impairs migration in the host, an important sporozoite trait required to find a blood vessel and reach the liver after being deposited in the skin by the mosquito. Our study also shows that fast locomotion of sporozoites is crucial during natural malaria transmission.sporozoites, single cell eukaryotic pathogens, use their own actin/myosin-based motor machinery for life cycle progression, which includes forward locomotion, penetration of cellular barriers, and invasion of target cells. To display fast gliding motility, the parasite uses a high turnover of actin polymerization and adhesion sites. Paradoxically, only a few classic actin regulatory proteins appear to be encoded in the Plasmodium genome. Small heat shock proteins have been associated with cytoskeleton modulation in various biological processes. In this study, we identify HSP20 as a novel player in Plasmodium motility and provide molecular genetics evidence for a critical role of a small heat shock protein in cell traction and motility. We demonstrate that HSP20 ablation profoundly affects sporozoite-substrate adhesion, which translates into aberrant speed and directionality in vitro. Loss of HSP20 function impairs migration in the host, an important sporozoite trait required to find a blood vessel and reach the liver after being deposited in the skin by the mosquito. Our study also shows that fast locomotion of sporozoites is crucial during natural malaria transmission. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-01 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/269123 Montagna, Georgina Nuri; Buscaglia, Carlos Andres; Münter, Sylvia; Goosmann, Christian; Frischknecht, Friedrich; et al.; Critical Role for Heat Shock Protein 20 (HSP20) in Migration of Malarial Sporozoites; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 287; 4; 1-2012; 2410-2422 0021-9258 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/269123 |
identifier_str_mv |
Montagna, Georgina Nuri; Buscaglia, Carlos Andres; Münter, Sylvia; Goosmann, Christian; Frischknecht, Friedrich; et al.; Critical Role for Heat Shock Protein 20 (HSP20) in Migration of Malarial Sporozoites; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 287; 4; 1-2012; 2410-2422 0021-9258 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0021925820532031 info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M111.302109 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
American Society for Biochemistry and Molecular Biology |
publisher.none.fl_str_mv |
American Society for Biochemistry and Molecular Biology |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
_version_ |
1844614103099768832 |
score |
13.070432 |