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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/269123
Acceder
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 Técnicas2025-10-22T11:46:16Zoai: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:34982025-10-22 11:46:16.395CONICET 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_ 1846782163988512768
score 12.982451

Publicaciones similares