Proteomic characterization of extracellular vesicles released by third stage larvae of the zoonotic parasite Anisakis pegreffii (Nematoda: Anisakidae)
IntroductionAnisakis pegreffii is a sibling species within the A. simplex (s.l.) complex requiring marine homeothermic (mainly cetaceans) and heterothermic (crustaceans, fish, and cephalopods) organisms to complete its life cycle. It is also a zoonotic species, able to accidentally infect humans (an...
Ausführliche Beschreibung
Autor*in: |
Marialetizia Palomba [verfasserIn] Aurelia Rughetti [verfasserIn] Giuseppina Mignogna [verfasserIn] Tiziana Castrignanò [verfasserIn] Hassan Rahimi [verfasserIn] Laura Masuelli [verfasserIn] Chiara Napoletano [verfasserIn] Valentina Pinna [verfasserIn] Alessandra Giorgi [verfasserIn] Mario Santoro [verfasserIn] Maria Eugenia Schininà [verfasserIn] Bruno Maras [verfasserIn] Simonetta Mattiucci [verfasserIn] |
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E-Artikel |
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Englisch |
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2023 |
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Übergeordnetes Werk: |
In: Frontiers in Cellular and Infection Microbiology - Frontiers Media S.A., 2016, 13(2023) |
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Übergeordnetes Werk: |
volume:13 ; year:2023 |
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DOI / URN: |
10.3389/fcimb.2023.1079991 |
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Katalog-ID: |
DOAJ088587711 |
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520 | |a IntroductionAnisakis pegreffii is a sibling species within the A. simplex (s.l.) complex requiring marine homeothermic (mainly cetaceans) and heterothermic (crustaceans, fish, and cephalopods) organisms to complete its life cycle. It is also a zoonotic species, able to accidentally infect humans (anisakiasis). To investigate the molecular signals involved in this host-parasite interaction and pathogenesis, the proteomic composition of the extracellular vesicles (EVs) released by the third-stage larvae (L3) of A. pegreffii, was characterized.MethodsGenetically identified L3 of A. pegreffii were maintained for 24 h at 37°C and EVs were isolated by serial centrifugation and ultracentrifugation of culture media. Proteomic analysis was performed by Shotgun Analysis.Results and discussionEVs showed spherical shaped structure (size 65-295 nm). Proteomic results were blasted against the A. pegreffii specific transcriptomic database, and 153 unique proteins were identified. Gene Ontology and Kyoto Encyclopedia of Genes and Genomes analysis predicted several proteins belonging to distinct metabolic pathways. The similarity search employing selected parasitic nematodes database revealed that proteins associated with A. pegreffii EVs might be involved in parasite survival and adaptation, as well as in pathogenic processes. Further, a possible link between the A. pegreffii EVs proteins versus those of human and cetaceans’ hosts, were predicted by using HPIDB database. The results, herein described, expand knowledge concerning the proteins possibly implied in the host-parasite interactions between this parasite and its natural and accidental hosts. | ||
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10.3389/fcimb.2023.1079991 doi (DE-627)DOAJ088587711 (DE-599)DOAJ98fdf2d84911499f93b3dba3cd751edf DE-627 ger DE-627 rakwb eng QR1-502 Marialetizia Palomba verfasserin aut Proteomic characterization of extracellular vesicles released by third stage larvae of the zoonotic parasite Anisakis pegreffii (Nematoda: Anisakidae) 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier IntroductionAnisakis pegreffii is a sibling species within the A. simplex (s.l.) complex requiring marine homeothermic (mainly cetaceans) and heterothermic (crustaceans, fish, and cephalopods) organisms to complete its life cycle. It is also a zoonotic species, able to accidentally infect humans (anisakiasis). To investigate the molecular signals involved in this host-parasite interaction and pathogenesis, the proteomic composition of the extracellular vesicles (EVs) released by the third-stage larvae (L3) of A. pegreffii, was characterized.MethodsGenetically identified L3 of A. pegreffii were maintained for 24 h at 37°C and EVs were isolated by serial centrifugation and ultracentrifugation of culture media. Proteomic analysis was performed by Shotgun Analysis.Results and discussionEVs showed spherical shaped structure (size 65-295 nm). Proteomic results were blasted against the A. pegreffii specific transcriptomic database, and 153 unique proteins were identified. Gene Ontology and Kyoto Encyclopedia of Genes and Genomes analysis predicted several proteins belonging to distinct metabolic pathways. The similarity search employing selected parasitic nematodes database revealed that proteins associated with A. pegreffii EVs might be involved in parasite survival and adaptation, as well as in pathogenic processes. Further, a possible link between the A. pegreffii EVs proteins versus those of human and cetaceans’ hosts, were predicted by using HPIDB database. The results, herein described, expand knowledge concerning the proteins possibly implied in the host-parasite interactions between this parasite and its natural and accidental hosts. Anisakis pegreffii zoonotic parasite third stage larvae extracellular vesicles proteomics heat shock proteins Microbiology Aurelia Rughetti verfasserin aut Giuseppina Mignogna verfasserin aut Tiziana Castrignanò verfasserin aut Hassan Rahimi verfasserin aut Laura Masuelli verfasserin aut Chiara Napoletano verfasserin aut Valentina Pinna verfasserin aut Alessandra Giorgi verfasserin aut Mario Santoro verfasserin aut Maria Eugenia Schininà verfasserin aut Bruno Maras verfasserin aut Simonetta Mattiucci verfasserin aut In Frontiers in Cellular and Infection Microbiology Frontiers Media S.A., 2016 13(2023) (DE-627)664968554 (DE-600)2619676-1 22352988 nnns volume:13 year:2023 https://doi.org/10.3389/fcimb.2023.1079991 kostenfrei https://doaj.org/article/98fdf2d84911499f93b3dba3cd751edf kostenfrei https://www.frontiersin.org/articles/10.3389/fcimb.2023.1079991/full kostenfrei https://doaj.org/toc/2235-2988 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 13 2023 |
spelling |
10.3389/fcimb.2023.1079991 doi (DE-627)DOAJ088587711 (DE-599)DOAJ98fdf2d84911499f93b3dba3cd751edf DE-627 ger DE-627 rakwb eng QR1-502 Marialetizia Palomba verfasserin aut Proteomic characterization of extracellular vesicles released by third stage larvae of the zoonotic parasite Anisakis pegreffii (Nematoda: Anisakidae) 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier IntroductionAnisakis pegreffii is a sibling species within the A. simplex (s.l.) complex requiring marine homeothermic (mainly cetaceans) and heterothermic (crustaceans, fish, and cephalopods) organisms to complete its life cycle. It is also a zoonotic species, able to accidentally infect humans (anisakiasis). To investigate the molecular signals involved in this host-parasite interaction and pathogenesis, the proteomic composition of the extracellular vesicles (EVs) released by the third-stage larvae (L3) of A. pegreffii, was characterized.MethodsGenetically identified L3 of A. pegreffii were maintained for 24 h at 37°C and EVs were isolated by serial centrifugation and ultracentrifugation of culture media. Proteomic analysis was performed by Shotgun Analysis.Results and discussionEVs showed spherical shaped structure (size 65-295 nm). Proteomic results were blasted against the A. pegreffii specific transcriptomic database, and 153 unique proteins were identified. Gene Ontology and Kyoto Encyclopedia of Genes and Genomes analysis predicted several proteins belonging to distinct metabolic pathways. The similarity search employing selected parasitic nematodes database revealed that proteins associated with A. pegreffii EVs might be involved in parasite survival and adaptation, as well as in pathogenic processes. Further, a possible link between the A. pegreffii EVs proteins versus those of human and cetaceans’ hosts, were predicted by using HPIDB database. The results, herein described, expand knowledge concerning the proteins possibly implied in the host-parasite interactions between this parasite and its natural and accidental hosts. Anisakis pegreffii zoonotic parasite third stage larvae extracellular vesicles proteomics heat shock proteins Microbiology Aurelia Rughetti verfasserin aut Giuseppina Mignogna verfasserin aut Tiziana Castrignanò verfasserin aut Hassan Rahimi verfasserin aut Laura Masuelli verfasserin aut Chiara Napoletano verfasserin aut Valentina Pinna verfasserin aut Alessandra Giorgi verfasserin aut Mario Santoro verfasserin aut Maria Eugenia Schininà verfasserin aut Bruno Maras verfasserin aut Simonetta Mattiucci verfasserin aut In Frontiers in Cellular and Infection Microbiology Frontiers Media S.A., 2016 13(2023) (DE-627)664968554 (DE-600)2619676-1 22352988 nnns volume:13 year:2023 https://doi.org/10.3389/fcimb.2023.1079991 kostenfrei https://doaj.org/article/98fdf2d84911499f93b3dba3cd751edf kostenfrei https://www.frontiersin.org/articles/10.3389/fcimb.2023.1079991/full kostenfrei https://doaj.org/toc/2235-2988 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 13 2023 |
allfields_unstemmed |
10.3389/fcimb.2023.1079991 doi (DE-627)DOAJ088587711 (DE-599)DOAJ98fdf2d84911499f93b3dba3cd751edf DE-627 ger DE-627 rakwb eng QR1-502 Marialetizia Palomba verfasserin aut Proteomic characterization of extracellular vesicles released by third stage larvae of the zoonotic parasite Anisakis pegreffii (Nematoda: Anisakidae) 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier IntroductionAnisakis pegreffii is a sibling species within the A. simplex (s.l.) complex requiring marine homeothermic (mainly cetaceans) and heterothermic (crustaceans, fish, and cephalopods) organisms to complete its life cycle. It is also a zoonotic species, able to accidentally infect humans (anisakiasis). To investigate the molecular signals involved in this host-parasite interaction and pathogenesis, the proteomic composition of the extracellular vesicles (EVs) released by the third-stage larvae (L3) of A. pegreffii, was characterized.MethodsGenetically identified L3 of A. pegreffii were maintained for 24 h at 37°C and EVs were isolated by serial centrifugation and ultracentrifugation of culture media. Proteomic analysis was performed by Shotgun Analysis.Results and discussionEVs showed spherical shaped structure (size 65-295 nm). Proteomic results were blasted against the A. pegreffii specific transcriptomic database, and 153 unique proteins were identified. Gene Ontology and Kyoto Encyclopedia of Genes and Genomes analysis predicted several proteins belonging to distinct metabolic pathways. The similarity search employing selected parasitic nematodes database revealed that proteins associated with A. pegreffii EVs might be involved in parasite survival and adaptation, as well as in pathogenic processes. Further, a possible link between the A. pegreffii EVs proteins versus those of human and cetaceans’ hosts, were predicted by using HPIDB database. The results, herein described, expand knowledge concerning the proteins possibly implied in the host-parasite interactions between this parasite and its natural and accidental hosts. Anisakis pegreffii zoonotic parasite third stage larvae extracellular vesicles proteomics heat shock proteins Microbiology Aurelia Rughetti verfasserin aut Giuseppina Mignogna verfasserin aut Tiziana Castrignanò verfasserin aut Hassan Rahimi verfasserin aut Laura Masuelli verfasserin aut Chiara Napoletano verfasserin aut Valentina Pinna verfasserin aut Alessandra Giorgi verfasserin aut Mario Santoro verfasserin aut Maria Eugenia Schininà verfasserin aut Bruno Maras verfasserin aut Simonetta Mattiucci verfasserin aut In Frontiers in Cellular and Infection Microbiology Frontiers Media S.A., 2016 13(2023) (DE-627)664968554 (DE-600)2619676-1 22352988 nnns volume:13 year:2023 https://doi.org/10.3389/fcimb.2023.1079991 kostenfrei https://doaj.org/article/98fdf2d84911499f93b3dba3cd751edf kostenfrei https://www.frontiersin.org/articles/10.3389/fcimb.2023.1079991/full kostenfrei https://doaj.org/toc/2235-2988 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 13 2023 |
allfieldsGer |
10.3389/fcimb.2023.1079991 doi (DE-627)DOAJ088587711 (DE-599)DOAJ98fdf2d84911499f93b3dba3cd751edf DE-627 ger DE-627 rakwb eng QR1-502 Marialetizia Palomba verfasserin aut Proteomic characterization of extracellular vesicles released by third stage larvae of the zoonotic parasite Anisakis pegreffii (Nematoda: Anisakidae) 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier IntroductionAnisakis pegreffii is a sibling species within the A. simplex (s.l.) complex requiring marine homeothermic (mainly cetaceans) and heterothermic (crustaceans, fish, and cephalopods) organisms to complete its life cycle. It is also a zoonotic species, able to accidentally infect humans (anisakiasis). To investigate the molecular signals involved in this host-parasite interaction and pathogenesis, the proteomic composition of the extracellular vesicles (EVs) released by the third-stage larvae (L3) of A. pegreffii, was characterized.MethodsGenetically identified L3 of A. pegreffii were maintained for 24 h at 37°C and EVs were isolated by serial centrifugation and ultracentrifugation of culture media. Proteomic analysis was performed by Shotgun Analysis.Results and discussionEVs showed spherical shaped structure (size 65-295 nm). Proteomic results were blasted against the A. pegreffii specific transcriptomic database, and 153 unique proteins were identified. Gene Ontology and Kyoto Encyclopedia of Genes and Genomes analysis predicted several proteins belonging to distinct metabolic pathways. The similarity search employing selected parasitic nematodes database revealed that proteins associated with A. pegreffii EVs might be involved in parasite survival and adaptation, as well as in pathogenic processes. Further, a possible link between the A. pegreffii EVs proteins versus those of human and cetaceans’ hosts, were predicted by using HPIDB database. The results, herein described, expand knowledge concerning the proteins possibly implied in the host-parasite interactions between this parasite and its natural and accidental hosts. Anisakis pegreffii zoonotic parasite third stage larvae extracellular vesicles proteomics heat shock proteins Microbiology Aurelia Rughetti verfasserin aut Giuseppina Mignogna verfasserin aut Tiziana Castrignanò verfasserin aut Hassan Rahimi verfasserin aut Laura Masuelli verfasserin aut Chiara Napoletano verfasserin aut Valentina Pinna verfasserin aut Alessandra Giorgi verfasserin aut Mario Santoro verfasserin aut Maria Eugenia Schininà verfasserin aut Bruno Maras verfasserin aut Simonetta Mattiucci verfasserin aut In Frontiers in Cellular and Infection Microbiology Frontiers Media S.A., 2016 13(2023) (DE-627)664968554 (DE-600)2619676-1 22352988 nnns volume:13 year:2023 https://doi.org/10.3389/fcimb.2023.1079991 kostenfrei https://doaj.org/article/98fdf2d84911499f93b3dba3cd751edf kostenfrei https://www.frontiersin.org/articles/10.3389/fcimb.2023.1079991/full kostenfrei https://doaj.org/toc/2235-2988 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 13 2023 |
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10.3389/fcimb.2023.1079991 doi (DE-627)DOAJ088587711 (DE-599)DOAJ98fdf2d84911499f93b3dba3cd751edf DE-627 ger DE-627 rakwb eng QR1-502 Marialetizia Palomba verfasserin aut Proteomic characterization of extracellular vesicles released by third stage larvae of the zoonotic parasite Anisakis pegreffii (Nematoda: Anisakidae) 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier IntroductionAnisakis pegreffii is a sibling species within the A. simplex (s.l.) complex requiring marine homeothermic (mainly cetaceans) and heterothermic (crustaceans, fish, and cephalopods) organisms to complete its life cycle. It is also a zoonotic species, able to accidentally infect humans (anisakiasis). To investigate the molecular signals involved in this host-parasite interaction and pathogenesis, the proteomic composition of the extracellular vesicles (EVs) released by the third-stage larvae (L3) of A. pegreffii, was characterized.MethodsGenetically identified L3 of A. pegreffii were maintained for 24 h at 37°C and EVs were isolated by serial centrifugation and ultracentrifugation of culture media. Proteomic analysis was performed by Shotgun Analysis.Results and discussionEVs showed spherical shaped structure (size 65-295 nm). Proteomic results were blasted against the A. pegreffii specific transcriptomic database, and 153 unique proteins were identified. Gene Ontology and Kyoto Encyclopedia of Genes and Genomes analysis predicted several proteins belonging to distinct metabolic pathways. The similarity search employing selected parasitic nematodes database revealed that proteins associated with A. pegreffii EVs might be involved in parasite survival and adaptation, as well as in pathogenic processes. Further, a possible link between the A. pegreffii EVs proteins versus those of human and cetaceans’ hosts, were predicted by using HPIDB database. The results, herein described, expand knowledge concerning the proteins possibly implied in the host-parasite interactions between this parasite and its natural and accidental hosts. Anisakis pegreffii zoonotic parasite third stage larvae extracellular vesicles proteomics heat shock proteins Microbiology Aurelia Rughetti verfasserin aut Giuseppina Mignogna verfasserin aut Tiziana Castrignanò verfasserin aut Hassan Rahimi verfasserin aut Laura Masuelli verfasserin aut Chiara Napoletano verfasserin aut Valentina Pinna verfasserin aut Alessandra Giorgi verfasserin aut Mario Santoro verfasserin aut Maria Eugenia Schininà verfasserin aut Bruno Maras verfasserin aut Simonetta Mattiucci verfasserin aut In Frontiers in Cellular and Infection Microbiology Frontiers Media S.A., 2016 13(2023) (DE-627)664968554 (DE-600)2619676-1 22352988 nnns volume:13 year:2023 https://doi.org/10.3389/fcimb.2023.1079991 kostenfrei https://doaj.org/article/98fdf2d84911499f93b3dba3cd751edf kostenfrei https://www.frontiersin.org/articles/10.3389/fcimb.2023.1079991/full kostenfrei https://doaj.org/toc/2235-2988 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 13 2023 |
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Proteomic characterization of extracellular vesicles released by third stage larvae of the zoonotic parasite Anisakis pegreffii (Nematoda: Anisakidae) |
abstract |
IntroductionAnisakis pegreffii is a sibling species within the A. simplex (s.l.) complex requiring marine homeothermic (mainly cetaceans) and heterothermic (crustaceans, fish, and cephalopods) organisms to complete its life cycle. It is also a zoonotic species, able to accidentally infect humans (anisakiasis). To investigate the molecular signals involved in this host-parasite interaction and pathogenesis, the proteomic composition of the extracellular vesicles (EVs) released by the third-stage larvae (L3) of A. pegreffii, was characterized.MethodsGenetically identified L3 of A. pegreffii were maintained for 24 h at 37°C and EVs were isolated by serial centrifugation and ultracentrifugation of culture media. Proteomic analysis was performed by Shotgun Analysis.Results and discussionEVs showed spherical shaped structure (size 65-295 nm). Proteomic results were blasted against the A. pegreffii specific transcriptomic database, and 153 unique proteins were identified. Gene Ontology and Kyoto Encyclopedia of Genes and Genomes analysis predicted several proteins belonging to distinct metabolic pathways. The similarity search employing selected parasitic nematodes database revealed that proteins associated with A. pegreffii EVs might be involved in parasite survival and adaptation, as well as in pathogenic processes. Further, a possible link between the A. pegreffii EVs proteins versus those of human and cetaceans’ hosts, were predicted by using HPIDB database. The results, herein described, expand knowledge concerning the proteins possibly implied in the host-parasite interactions between this parasite and its natural and accidental hosts. |
abstractGer |
IntroductionAnisakis pegreffii is a sibling species within the A. simplex (s.l.) complex requiring marine homeothermic (mainly cetaceans) and heterothermic (crustaceans, fish, and cephalopods) organisms to complete its life cycle. It is also a zoonotic species, able to accidentally infect humans (anisakiasis). To investigate the molecular signals involved in this host-parasite interaction and pathogenesis, the proteomic composition of the extracellular vesicles (EVs) released by the third-stage larvae (L3) of A. pegreffii, was characterized.MethodsGenetically identified L3 of A. pegreffii were maintained for 24 h at 37°C and EVs were isolated by serial centrifugation and ultracentrifugation of culture media. Proteomic analysis was performed by Shotgun Analysis.Results and discussionEVs showed spherical shaped structure (size 65-295 nm). Proteomic results were blasted against the A. pegreffii specific transcriptomic database, and 153 unique proteins were identified. Gene Ontology and Kyoto Encyclopedia of Genes and Genomes analysis predicted several proteins belonging to distinct metabolic pathways. The similarity search employing selected parasitic nematodes database revealed that proteins associated with A. pegreffii EVs might be involved in parasite survival and adaptation, as well as in pathogenic processes. Further, a possible link between the A. pegreffii EVs proteins versus those of human and cetaceans’ hosts, were predicted by using HPIDB database. The results, herein described, expand knowledge concerning the proteins possibly implied in the host-parasite interactions between this parasite and its natural and accidental hosts. |
abstract_unstemmed |
IntroductionAnisakis pegreffii is a sibling species within the A. simplex (s.l.) complex requiring marine homeothermic (mainly cetaceans) and heterothermic (crustaceans, fish, and cephalopods) organisms to complete its life cycle. It is also a zoonotic species, able to accidentally infect humans (anisakiasis). To investigate the molecular signals involved in this host-parasite interaction and pathogenesis, the proteomic composition of the extracellular vesicles (EVs) released by the third-stage larvae (L3) of A. pegreffii, was characterized.MethodsGenetically identified L3 of A. pegreffii were maintained for 24 h at 37°C and EVs were isolated by serial centrifugation and ultracentrifugation of culture media. Proteomic analysis was performed by Shotgun Analysis.Results and discussionEVs showed spherical shaped structure (size 65-295 nm). Proteomic results were blasted against the A. pegreffii specific transcriptomic database, and 153 unique proteins were identified. Gene Ontology and Kyoto Encyclopedia of Genes and Genomes analysis predicted several proteins belonging to distinct metabolic pathways. The similarity search employing selected parasitic nematodes database revealed that proteins associated with A. pegreffii EVs might be involved in parasite survival and adaptation, as well as in pathogenic processes. Further, a possible link between the A. pegreffii EVs proteins versus those of human and cetaceans’ hosts, were predicted by using HPIDB database. The results, herein described, expand knowledge concerning the proteins possibly implied in the host-parasite interactions between this parasite and its natural and accidental hosts. |
collection_details |
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title_short |
Proteomic characterization of extracellular vesicles released by third stage larvae of the zoonotic parasite Anisakis pegreffii (Nematoda: Anisakidae) |
url |
https://doi.org/10.3389/fcimb.2023.1079991 https://doaj.org/article/98fdf2d84911499f93b3dba3cd751edf https://www.frontiersin.org/articles/10.3389/fcimb.2023.1079991/full https://doaj.org/toc/2235-2988 |
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author2 |
Aurelia Rughetti Giuseppina Mignogna Tiziana Castrignanò Hassan Rahimi Laura Masuelli Chiara Napoletano Valentina Pinna Alessandra Giorgi Mario Santoro Maria Eugenia Schininà Bruno Maras Simonetta Mattiucci |
author2Str |
Aurelia Rughetti Giuseppina Mignogna Tiziana Castrignanò Hassan Rahimi Laura Masuelli Chiara Napoletano Valentina Pinna Alessandra Giorgi Mario Santoro Maria Eugenia Schininà Bruno Maras Simonetta Mattiucci |
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doi_str |
10.3389/fcimb.2023.1079991 |
callnumber-a |
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up_date |
2024-07-03T18:29:48.215Z |
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