The Fat Body of the Hematophagous Insect, Panstrongylus megistus (Hemiptera: Reduviidae): Histological Features and Participation of the β-Chain of ATP Synthase in the Lipophorin-Mediated Lipid Transfer. Issue 4 (26th July 2019)

• Record Type: Journal Article
• Authors: Fruttero, Leonardo L; Leyria, Jimena; Moyetta, Natalia R; Ramos, Fabian O; Settembrini, Beatriz P; Canavoso, Lilián E
• Is Part Of: Journal of insect science. Volume 19:Issue 4(2019)
• Publication Date: 2019-07-26
• Subjects: fat body -- lipophorin -- lipid metabolism -- Triatominae -- docking receptor; Insects -- Periodicals; Entomology -- Periodicals; Arthropoda -- Periodicals; Insects; Arthropods; Biology; Ecology; Entomologie -- Périodiques; Entomology; Insects; Electronic journals; Periodicals; 595.05
• DOI: 10.1093/jisesa/iez078
• Languages: English
• ISSNs: 1536-2442

Abstract

Abstract: In insects, lipid transfer to the tissues is mediated by lipophorin, the major circulating lipoprotein, mainly through a nonendocytic pathway involving docking receptors. Currently, the role of such receptors in lipid metabolism remains poorly understood. In this work, we performed a histological characterization of the fat body of the Chagas' disease vector, Panstrongylus megistus (Burmeister), subjected to different nutritional conditions. In addition, we addressed the role of the β-chain of ATP synthase (β-ATPase) in the process of lipid transfer from lipophorin to the fat body. Fifth-instar nymphs in either fasting or fed condition were employed in the assays. Histological examination revealed that the fat body was composed by diverse trophocyte phenotypes. In the fasting condition, the cells were smaller and presented a homogeneous cytoplasmic content. The fat body of fed insects increased in size mainly due to the enlargement of lipid stores. In this condition, trophocytes contained abundant lipid droplets, and the rough endoplasmic reticulum was highly developed and mitochondria appeared elongated. Immunofluorescence assays showed that the β-ATPase, a putative lipophorin receptor, was located on the surface of fat body cells colocalizing partially with lipophorin, which suggests their interaction. No changes in β-ATPase expression were found in fasting and fed insects. Blocking the lipophorin–β-ATPase interaction impaired the lipophorin-mediated lipid transfer to the fat body. The results showed that the nutritional status of the insect influenced the morphohistological features of the tissue. Besides, these findings suggest that β-ATPase functions as a lipophorin docking receptor in the fat body.