ATPe Dynamics in Protozoan Parasites: Adapt or Perish

Autores
Lauri, Natalia; Bazzi, Zaher; Álvarez, Cora L.; Leal Denis, María F.; Schachter, Julieta; Herlax, Vanesa Silvana; Ostuni, Mariano A.; Schwarzbaum, Pablo J.
Año de publicación
2018
Idioma
inglés
Tipo de recurso
reseña artículo
Estado
versión publicada
Descripción
In most animals, transient increases of extracellular ATP (ATPe) are used for physiological signaling or as a danger signal in pathological conditions. ATPe dynamics are controlled by ATP release from viable cells and cell lysis, ATPe degradation and interconversion by ecto-nucleotidases, and interaction of ATPe and byproducts with cell surface purinergic receptors and purine salvage mechanisms. Infection by protozoan parasites may alter at least one of the mechanisms controlling ATPe concentration. Protozoan parasites display their own set of proteins directly altering ATPe dynamics, or control the activity of host proteins. Parasite dependent activation of ATPe conduits of the host may promote infection and systemic responses that are beneficial or detrimental to the parasite. For instance, activation of organic solute permeability at the host membrane can support the elevated metabolism of the parasite. On the other hand ecto-nucleotidases of protozoan parasites, by promoting ATPe degradation and purine/pyrimidine salvage, may be involved in parasite growth, infectivity, and virulence. In this review, we will describe the complex dynamics of ATPe regulation in the context of protozoan parasite–host interactions. Particular focus will be given to features of parasite membrane proteins strongly controlling ATPe dynamics. This includes evolutionary, genetic and cellular mechanisms, as well as structural-functional relationships.
Instituto de Investigaciones Bioquímicas de La Plata
Materia
Ciencias Médicas
Parasite
Membrane proteins
Host–parasite interaction
Transport
Pathogenesis
Evolution
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/118993

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network_name_str SEDICI (UNLP)
spelling ATPe Dynamics in Protozoan Parasites: Adapt or PerishLauri, NataliaBazzi, ZaherÁlvarez, Cora L.Leal Denis, María F.Schachter, JulietaHerlax, Vanesa SilvanaOstuni, Mariano A.Schwarzbaum, Pablo J.Ciencias MédicasParasiteMembrane proteinsHost–parasite interactionTransportPathogenesisEvolutionIn most animals, transient increases of extracellular ATP (ATPe) are used for physiological signaling or as a danger signal in pathological conditions. ATPe dynamics are controlled by ATP release from viable cells and cell lysis, ATPe degradation and interconversion by ecto-nucleotidases, and interaction of ATPe and byproducts with cell surface purinergic receptors and purine salvage mechanisms. Infection by protozoan parasites may alter at least one of the mechanisms controlling ATPe concentration. Protozoan parasites display their own set of proteins directly altering ATPe dynamics, or control the activity of host proteins. Parasite dependent activation of ATPe conduits of the host may promote infection and systemic responses that are beneficial or detrimental to the parasite. For instance, activation of organic solute permeability at the host membrane can support the elevated metabolism of the parasite. On the other hand ecto-nucleotidases of protozoan parasites, by promoting ATPe degradation and purine/pyrimidine salvage, may be involved in parasite growth, infectivity, and virulence. In this review, we will describe the complex dynamics of ATPe regulation in the context of protozoan parasite–host interactions. Particular focus will be given to features of parasite membrane proteins strongly controlling ATPe dynamics. This includes evolutionary, genetic and cellular mechanisms, as well as structural-functional relationships.Instituto de Investigaciones Bioquímicas de La Plata2018info:eu-repo/semantics/reviewinfo:eu-repo/semantics/publishedVersionRevisionhttp://purl.org/coar/resource_type/c_dcae04bcinfo:ar-repo/semantics/resenaArticuloapplication/pdfhttp://sedici.unlp.edu.ar/handle/10915/118993enginfo:eu-repo/semantics/altIdentifier/issn/2073-4425info:eu-repo/semantics/altIdentifier/doi/10.3390/genes10010016info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-10-22T17:08:56Zoai:sedici.unlp.edu.ar:10915/118993Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-10-22 17:08:56.339SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv ATPe Dynamics in Protozoan Parasites: Adapt or Perish
title ATPe Dynamics in Protozoan Parasites: Adapt or Perish
spellingShingle ATPe Dynamics in Protozoan Parasites: Adapt or Perish
Lauri, Natalia
Ciencias Médicas
Parasite
Membrane proteins
Host–parasite interaction
Transport
Pathogenesis
Evolution
title_short ATPe Dynamics in Protozoan Parasites: Adapt or Perish
title_full ATPe Dynamics in Protozoan Parasites: Adapt or Perish
title_fullStr ATPe Dynamics in Protozoan Parasites: Adapt or Perish
title_full_unstemmed ATPe Dynamics in Protozoan Parasites: Adapt or Perish
title_sort ATPe Dynamics in Protozoan Parasites: Adapt or Perish
dc.creator.none.fl_str_mv Lauri, Natalia
Bazzi, Zaher
Álvarez, Cora L.
Leal Denis, María F.
Schachter, Julieta
Herlax, Vanesa Silvana
Ostuni, Mariano A.
Schwarzbaum, Pablo J.
author Lauri, Natalia
author_facet Lauri, Natalia
Bazzi, Zaher
Álvarez, Cora L.
Leal Denis, María F.
Schachter, Julieta
Herlax, Vanesa Silvana
Ostuni, Mariano A.
Schwarzbaum, Pablo J.
author_role author
author2 Bazzi, Zaher
Álvarez, Cora L.
Leal Denis, María F.
Schachter, Julieta
Herlax, Vanesa Silvana
Ostuni, Mariano A.
Schwarzbaum, Pablo J.
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Ciencias Médicas
Parasite
Membrane proteins
Host–parasite interaction
Transport
Pathogenesis
Evolution
topic Ciencias Médicas
Parasite
Membrane proteins
Host–parasite interaction
Transport
Pathogenesis
Evolution
dc.description.none.fl_txt_mv In most animals, transient increases of extracellular ATP (ATPe) are used for physiological signaling or as a danger signal in pathological conditions. ATPe dynamics are controlled by ATP release from viable cells and cell lysis, ATPe degradation and interconversion by ecto-nucleotidases, and interaction of ATPe and byproducts with cell surface purinergic receptors and purine salvage mechanisms. Infection by protozoan parasites may alter at least one of the mechanisms controlling ATPe concentration. Protozoan parasites display their own set of proteins directly altering ATPe dynamics, or control the activity of host proteins. Parasite dependent activation of ATPe conduits of the host may promote infection and systemic responses that are beneficial or detrimental to the parasite. For instance, activation of organic solute permeability at the host membrane can support the elevated metabolism of the parasite. On the other hand ecto-nucleotidases of protozoan parasites, by promoting ATPe degradation and purine/pyrimidine salvage, may be involved in parasite growth, infectivity, and virulence. In this review, we will describe the complex dynamics of ATPe regulation in the context of protozoan parasite–host interactions. Particular focus will be given to features of parasite membrane proteins strongly controlling ATPe dynamics. This includes evolutionary, genetic and cellular mechanisms, as well as structural-functional relationships.
Instituto de Investigaciones Bioquímicas de La Plata
description In most animals, transient increases of extracellular ATP (ATPe) are used for physiological signaling or as a danger signal in pathological conditions. ATPe dynamics are controlled by ATP release from viable cells and cell lysis, ATPe degradation and interconversion by ecto-nucleotidases, and interaction of ATPe and byproducts with cell surface purinergic receptors and purine salvage mechanisms. Infection by protozoan parasites may alter at least one of the mechanisms controlling ATPe concentration. Protozoan parasites display their own set of proteins directly altering ATPe dynamics, or control the activity of host proteins. Parasite dependent activation of ATPe conduits of the host may promote infection and systemic responses that are beneficial or detrimental to the parasite. For instance, activation of organic solute permeability at the host membrane can support the elevated metabolism of the parasite. On the other hand ecto-nucleotidases of protozoan parasites, by promoting ATPe degradation and purine/pyrimidine salvage, may be involved in parasite growth, infectivity, and virulence. In this review, we will describe the complex dynamics of ATPe regulation in the context of protozoan parasite–host interactions. Particular focus will be given to features of parasite membrane proteins strongly controlling ATPe dynamics. This includes evolutionary, genetic and cellular mechanisms, as well as structural-functional relationships.
publishDate 2018
dc.date.none.fl_str_mv 2018
dc.type.none.fl_str_mv info:eu-repo/semantics/review
info:eu-repo/semantics/publishedVersion
Revision
http://purl.org/coar/resource_type/c_dcae04bc
info:ar-repo/semantics/resenaArticulo
format review
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/118993
url http://sedici.unlp.edu.ar/handle/10915/118993
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/2073-4425
info:eu-repo/semantics/altIdentifier/doi/10.3390/genes10010016
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
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repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
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