Beta-chain of ATP synthase as a lipophorin binding protein and its role in lipid transfer in the midgut of Panstrongylus megistus (Hemiptera: Reduviidae)

FRUTTERO LL; DE MARTINI, D; RUBIOLO ER; CARLINI, CR; CANAVOSO LE

INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY

PERGAMON-ELSEVIER SCIENCE LTD

Lugar: Amsterdam; Año: 2014 vol. 52 p. 1 - 1

0965-1748

ipophorin, the main lipoprotein in the circulation of the insects, cycles among peripheral tissues to exchange its lipid cargo at the plasma membrane of target cells, without synthesis or degradation of its apolipoprotein matrix. Currently, there are few characterized candidates supporting the functioning of the docking mechanism of lipophorin-mediated lipid transfer. In this work we combined ligand blotting assays and tandem mass spectrometry to characterize proteins with the property to bind lipophorin at the midgut membrane of Panstrongylus megistus, a vector of Chagas´ disease. We further evaluated the  role of lipophorin binding proteins in the transfer of lipids between the midgut and lipophorin. The b-subunit of the ATP synthase complex (b-ATPase) was identified as a lipophorin binding protein. b-ATPase was detected in enriched midgut membrane preparations free of mitochondria. It was shown that b-ATPase partially co-localizes with lipophorin at the plasma membrane of isolated