posted on 2024-03-05, 14:37authored byPatricia H. Alvarenga, Thiago Luiz Alves e Silva, Motoshi Suzuki, Glenn Nardone, Pedro Cecilio, Joel Vega-Rodriguez, Jose M.C. Ribeiro, John F. Andersen
In
arthropods, hemolymph carries immune cells and solubilizes and
transports 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 1403 proteins were identified, out of which
447 of them were 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 abundances (based on
their intensity-based absolute quantification, iBAQ) were 37.9 and
33.2%, respectively. Interestingly, among them, 102 serine proteases/serine
protease-homologues were identified, with almost half of them containing
CLIP regulatory domains. Moreover, proteins belonging to families
classically described as chemoreceptors, such as 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 A. 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 hemolymph composition.