β-ATPase of the Insect Panstrongylus megistus: Cloning, Bioinformatics Analysis, and Study of Its Interaction With Lipophorin.

ABSTRACT: Lipophorin is the main lipoprotein of the insect's hemolymph. Although its role in lipid metabolism has been extensively analyzed, the mechanisms of lipid delivery to target tissues mediated by lipophorin are not completely understood. It has been reported that the β-chain of the ATP synthase complex (β-ATPase) acts as a nonendocytic receptor for lipophorin in the hematophagous insect Panstrongylus megistus, and this function is relevant for the transfer of lipids. The aim of this study was to gather new information regarding the β-ATPase, including its sequence and interaction with lipophorin. A β-ATPase cDNA encoding a 521-amino acid protein was cloned from P. megistus. β-ATPase is highly conserved, and molecular phylogenetic analyses grouped the deduced amino acid sequences according to

SUBMITTER: Fruttero LL 

PROVIDER: S-EPMC12316553 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature