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Aphidius ervi Teratocytes Release Enolase and Fatty Acid Binding Protein Through Exosomal Vesicles.
Front Physiol 2019; 10:715FP

Abstract

The molecular bases of the host-parasitoid interactions in the biological system Acyrthosiphon pisum (Harris) (Homoptera, Aphididae) and Aphidius ervi (Haliday) (Hymenoptera, Braconidae) have been elucidated allowing the identification of a gamma-glutamyl transpeptidase, the active component of maternal venom secretion, and teratocytes, the embryonic parasitic factors responsible for host physiology regulation after parasitization. Teratocytes, cells deriving from the dissociation of the serosa, the parasitoid embryonic membrane, are responsible for extra-oral digestion of host tissues in order to provide a suitable nutritional environment for the development of parasitoid larvae. Teratocytes rapidly grow in size without undergoing any cell division, synthesize, and release in the host hemolymph two proteins: a fatty acid binding protein (Ae-FABP) and an enolase (Ae-ENO). Ae-FABP is involved in transport of fatty acids deriving from host tissues to the parasitoid larva. Ae-ENO is an extracellular glycolytic enzyme that functions as a plasminogen like receptor inducing its activation to plasmin. Both Ae-FABP and Ae-ENO lack their signal peptides, and they are released in the extracellular environment through an unknown secretion pathway. Here, we investigated the unconventional mechanism by which teratocytes release Ae-FABP and Ae-ENO in the extracellular space. Our results, obtained using immunogold staining coupled with TEM and western blot analyses, show that these two proteins are localized in vesicles released by teratocytes. The specific dimension of these vesicles and the immunodetection of ALIX and HSP70, two exosome markers, strongly support the hypothesis that these vesicles are exosomes.

Authors+Show Affiliations

Department of Sciences, University of Basilicata, Potenza, Italy.Department of Biotechnology and Life Sciences, University of Insubria, Varese, Italy.Department of Biotechnology and Life Sciences, University of Insubria, Varese, Italy.Department of Sciences, University of Basilicata, Potenza, Italy.Department of Sciences, University of Basilicata, Potenza, Italy.Department of Sciences, University of Basilicata, Potenza, Italy. Department of Geography, Environmental Management & Energy Studies, University of Johannesburg, Johannesburg, South Africa.Department of Entomology, Max Planck Institute for Chemical Ecology, Jena, Germany.Department of Sciences, University of Basilicata, Potenza, Italy.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

31275155

Citation

Salvia, Rosanna, et al. "Aphidius Ervi Teratocytes Release Enolase and Fatty Acid Binding Protein Through Exosomal Vesicles." Frontiers in Physiology, vol. 10, 2019, p. 715.
Salvia R, Grimaldi A, Girardello R, et al. Aphidius ervi Teratocytes Release Enolase and Fatty Acid Binding Protein Through Exosomal Vesicles. Front Physiol. 2019;10:715.
Salvia, R., Grimaldi, A., Girardello, R., Scieuzo, C., Scala, A., Bufo, S. A., ... Falabella, P. (2019). Aphidius ervi Teratocytes Release Enolase and Fatty Acid Binding Protein Through Exosomal Vesicles. Frontiers in Physiology, 10, p. 715. doi:10.3389/fphys.2019.00715.
Salvia R, et al. Aphidius Ervi Teratocytes Release Enolase and Fatty Acid Binding Protein Through Exosomal Vesicles. Front Physiol. 2019;10:715. PubMed PMID: 31275155.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Aphidius ervi Teratocytes Release Enolase and Fatty Acid Binding Protein Through Exosomal Vesicles. AU - Salvia,Rosanna, AU - Grimaldi,Annalisa, AU - Girardello,Rossana, AU - Scieuzo,Carmen, AU - Scala,Andrea, AU - Bufo,Sabino A, AU - Vogel,Heiko, AU - Falabella,Patrizia, Y1 - 2019/06/19/ PY - 2019/02/19/received PY - 2019/05/23/accepted PY - 2019/7/6/entrez PY - 2019/7/6/pubmed PY - 2019/7/6/medline KW - Aphidius ervi KW - enolase KW - exosomes KW - fatty acid binding protein KW - teratocytes KW - unconventional protein secretion KW - vesicles SP - 715 EP - 715 JF - Frontiers in physiology JO - Front Physiol VL - 10 N2 - The molecular bases of the host-parasitoid interactions in the biological system Acyrthosiphon pisum (Harris) (Homoptera, Aphididae) and Aphidius ervi (Haliday) (Hymenoptera, Braconidae) have been elucidated allowing the identification of a gamma-glutamyl transpeptidase, the active component of maternal venom secretion, and teratocytes, the embryonic parasitic factors responsible for host physiology regulation after parasitization. Teratocytes, cells deriving from the dissociation of the serosa, the parasitoid embryonic membrane, are responsible for extra-oral digestion of host tissues in order to provide a suitable nutritional environment for the development of parasitoid larvae. Teratocytes rapidly grow in size without undergoing any cell division, synthesize, and release in the host hemolymph two proteins: a fatty acid binding protein (Ae-FABP) and an enolase (Ae-ENO). Ae-FABP is involved in transport of fatty acids deriving from host tissues to the parasitoid larva. Ae-ENO is an extracellular glycolytic enzyme that functions as a plasminogen like receptor inducing its activation to plasmin. Both Ae-FABP and Ae-ENO lack their signal peptides, and they are released in the extracellular environment through an unknown secretion pathway. Here, we investigated the unconventional mechanism by which teratocytes release Ae-FABP and Ae-ENO in the extracellular space. Our results, obtained using immunogold staining coupled with TEM and western blot analyses, show that these two proteins are localized in vesicles released by teratocytes. The specific dimension of these vesicles and the immunodetection of ALIX and HSP70, two exosome markers, strongly support the hypothesis that these vesicles are exosomes. SN - 1664-042X UR - https://www.unboundmedicine.com/medline/citation/31275155/Aphidius_ervi_Teratocytes_Release_Enolase_and_Fatty_Acid_Binding_Protein_Through_Exosomal_Vesicles L2 - https://dx.doi.org/10.3389/fphys.2019.00715 DB - PRIME DP - Unbound Medicine ER -