A comprehensive proteomics analysis of the hemolymph composition of sugar-fed Aedes aegypti female and male mosquitoes

ABSTRACT: In arthropods, hemolymph carries immune cells and solubilizes and transport nutrients, hormones, and other molecules that are involved in diverse physiological processes including immunity, metabolism and reproduction. However, despite such physiological importance, little is known about its composition. We applied mass spectrometry-based label free quantification approaches to study the proteome of hemolymph perfused from sugar-fed female and male Aedes aegypti mosquitoes. A total of 1,403 proteins were identified, 447 of them predicted to be extracellular. In both sexes almost half of these extracellular proteins were predicted to be involved in defense/immune response, and their relative abundance (based on their intensity based absolute quantification, iBAQ) were 37.9% and 33.2%, respectively. Interestingly, among them 102 serine proteases/serine protease-homologs were identified, almost half of them containing CLIP regulatory domains. Moreover, proteins belonging to families classically described as chemoreceptors, like odorant-binding proteins (OBPs) and chemosensory proteins (CSPs) were also highly abundant in the hemolymph of both sexes. Our data provide a comprehensive catalogue of Ae. aegypti hemolymph basal protein content, revealing numerous unexplored targets for future research on mosquito physiology and disease transmission. It also provides a reference for future studies on the effect of blood meal and infection on the hemolymph composition.

INSTRUMENT(S):

ORGANISM(S): Aedes Aegypti

TISSUE(S): Hemolymph

SUBMITTER: Thiago Silva  

LAB HEAD: Jose Marcos Chaves Ribeiro

PROVIDER: PXD047714 | Pride | 2026-07-06

REPOSITORIES: Pride