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Insect venom phospholipases A1 and A2: Roles in the envenoming process and allergy

Detalhes bibliográficos
Autor(a) principal: Perez-Riverol, Amilcar [UNESP]
Data de Publicação: 2019
Outros Autores: Lasa, Alexis Musacchio, dos Santos-Pinto, José Roberto Aparecido [UNESP], Palma, Mario Sergio [UNESP]
Tipo de documento: Outros
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1016/j.ibmb.2018.12.011
http://hdl.handle.net/11449/188566
Resumo: Insect venom phospholipases have been identified in nearly all clinically relevant social Hymenoptera, including bees, wasps and ants. Among other biological roles, during the envenoming process these enzymes cause the disruption of cellular membranes and induce hypersensitive reactions, including life threatening anaphylaxis. While phospholipase A2 (PLA2) is a predominant component of bee venoms, phospholipase A1 (PLA1) is highly abundant in wasps and ants. The pronounced prevalence of IgE-mediated reactivity to these allergens in sensitized patients emphasizes their important role as major elicitors of Hymenoptera venom allergy (HVA). PLA1 and -A2 represent valuable marker allergens for differentiation of genuine sensitizations to bee and/or wasp venoms from cross-reactivity. Moreover, in massive attacks, insect venom phospholipases often cause several pathologies that can lead to fatalities. This review summarizes the available data related to structure, model of enzymatic activity and pathophysiological roles during envenoming process of insect venom phospholipases A1 and -A2.
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spelling Insect venom phospholipases A1 and A2: Roles in the envenoming process and allergyAllergy diagnosisHymenopteraHypersensitive reactionsToxic effectsVenom phospholipases A1 and A2Insect venom phospholipases have been identified in nearly all clinically relevant social Hymenoptera, including bees, wasps and ants. Among other biological roles, during the envenoming process these enzymes cause the disruption of cellular membranes and induce hypersensitive reactions, including life threatening anaphylaxis. While phospholipase A2 (PLA2) is a predominant component of bee venoms, phospholipase A1 (PLA1) is highly abundant in wasps and ants. The pronounced prevalence of IgE-mediated reactivity to these allergens in sensitized patients emphasizes their important role as major elicitors of Hymenoptera venom allergy (HVA). PLA1 and -A2 represent valuable marker allergens for differentiation of genuine sensitizations to bee and/or wasp venoms from cross-reactivity. Moreover, in massive attacks, insect venom phospholipases often cause several pathologies that can lead to fatalities. This review summarizes the available data related to structure, model of enzymatic activity and pathophysiological roles during envenoming process of insect venom phospholipases A1 and -A2.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Center of the Study of Social Insects Department of Biology Institute of Biosciences of Rio Claro São Paulo State University (UNESP)Center for Genetic Engineering and Biotechnology Biomedical Research Division Department of System Biology, Ave. 31, e/158 and 190, P.O. Box 6162, Cubanacan, PlayaCenter of the Study of Social Insects Department of Biology Institute of Biosciences of Rio Claro São Paulo State University (UNESP)FAPESP: #2016/16212-5FAPESP: #2017/22405-3CNPq: 150699/2017-4CNPq: 301656/2013-4Universidade Estadual Paulista (Unesp)Biomedical Research DivisionPerez-Riverol, Amilcar [UNESP]Lasa, Alexis Musacchiodos Santos-Pinto, José Roberto Aparecido [UNESP]Palma, Mario Sergio [UNESP]2019-10-06T16:12:18Z2019-10-06T16:12:18Z2019-02-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/other10-24http://dx.doi.org/10.1016/j.ibmb.2018.12.011Insect Biochemistry and Molecular Biology, v. 105, p. 10-24.1879-02400965-1748http://hdl.handle.net/11449/18856610.1016/j.ibmb.2018.12.0112-s2.0-850594477062901888624506535Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengInsect Biochemistry and Molecular Biologyinfo:eu-repo/semantics/openAccess2024-10-17T18:20:40Zoai:repositorio.unesp.br:11449/188566Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestrepositoriounesp@unesp.bropendoar:29462024-10-17T18:20:40Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Insect venom phospholipases A1 and A2: Roles in the envenoming process and allergy
title Insect venom phospholipases A1 and A2: Roles in the envenoming process and allergy
spellingShingle Insect venom phospholipases A1 and A2: Roles in the envenoming process and allergy
Perez-Riverol, Amilcar [UNESP]
Allergy diagnosis
Hymenoptera
Hypersensitive reactions
Toxic effects
Venom phospholipases A1 and A2
title_short Insect venom phospholipases A1 and A2: Roles in the envenoming process and allergy
title_full Insect venom phospholipases A1 and A2: Roles in the envenoming process and allergy
title_fullStr Insect venom phospholipases A1 and A2: Roles in the envenoming process and allergy
title_full_unstemmed Insect venom phospholipases A1 and A2: Roles in the envenoming process and allergy
title_sort Insect venom phospholipases A1 and A2: Roles in the envenoming process and allergy
author Perez-Riverol, Amilcar [UNESP]
author_facet Perez-Riverol, Amilcar [UNESP]
Lasa, Alexis Musacchio
dos Santos-Pinto, José Roberto Aparecido [UNESP]
Palma, Mario Sergio [UNESP]
author_role author
author2 Lasa, Alexis Musacchio
dos Santos-Pinto, José Roberto Aparecido [UNESP]
Palma, Mario Sergio [UNESP]
author2_role author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
Biomedical Research Division
dc.contributor.author.fl_str_mv Perez-Riverol, Amilcar [UNESP]
Lasa, Alexis Musacchio
dos Santos-Pinto, José Roberto Aparecido [UNESP]
Palma, Mario Sergio [UNESP]
dc.subject.por.fl_str_mv Allergy diagnosis
Hymenoptera
Hypersensitive reactions
Toxic effects
Venom phospholipases A1 and A2
topic Allergy diagnosis
Hymenoptera
Hypersensitive reactions
Toxic effects
Venom phospholipases A1 and A2
description Insect venom phospholipases have been identified in nearly all clinically relevant social Hymenoptera, including bees, wasps and ants. Among other biological roles, during the envenoming process these enzymes cause the disruption of cellular membranes and induce hypersensitive reactions, including life threatening anaphylaxis. While phospholipase A2 (PLA2) is a predominant component of bee venoms, phospholipase A1 (PLA1) is highly abundant in wasps and ants. The pronounced prevalence of IgE-mediated reactivity to these allergens in sensitized patients emphasizes their important role as major elicitors of Hymenoptera venom allergy (HVA). PLA1 and -A2 represent valuable marker allergens for differentiation of genuine sensitizations to bee and/or wasp venoms from cross-reactivity. Moreover, in massive attacks, insect venom phospholipases often cause several pathologies that can lead to fatalities. This review summarizes the available data related to structure, model of enzymatic activity and pathophysiological roles during envenoming process of insect venom phospholipases A1 and -A2.
publishDate 2019
dc.date.none.fl_str_mv 2019-10-06T16:12:18Z
2019-10-06T16:12:18Z
2019-02-01
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/other
format other
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1016/j.ibmb.2018.12.011
Insect Biochemistry and Molecular Biology, v. 105, p. 10-24.
1879-0240
0965-1748
http://hdl.handle.net/11449/188566
10.1016/j.ibmb.2018.12.011
2-s2.0-85059447706
2901888624506535
url http://dx.doi.org/10.1016/j.ibmb.2018.12.011
http://hdl.handle.net/11449/188566
identifier_str_mv Insect Biochemistry and Molecular Biology, v. 105, p. 10-24.
1879-0240
0965-1748
10.1016/j.ibmb.2018.12.011
2-s2.0-85059447706
2901888624506535
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Insect Biochemistry and Molecular Biology
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 10-24
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv repositoriounesp@unesp.br
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