Suppression of the prophenoloxidase system in Rhodnius prolixus orally infected with Trypanosoma rangeli.
Investigations were carried out to compare aspects of the prophenoloxidase (proPO)-activating pathway in Rhodnius prolixus hemolymph in response to oral infection and inoculation of the insects with two developmental forms of Trypanosoma rangeli epimastigotes strain H14. In vivo experiments demonstrated that in control insects fed on uninfected blood, inoculation challenge with short epimastigotes resulted in high phenoloxidase (PO) activity. In contrast, previous feeding on blood containing either short or long epimastigotes was able to suppress the proPO activation induced by thoracic inoculation of the short forms. In vitro assays in the presence of short epimastigotes demonstrated that control hemolymph or hemolymph provided by insects previously fed on blood containing epimastigotes incubated with fat body homogenates from control insects significantly increased the PO activity. However, fat body homogenates from insects previously fed on blood containing epimastigotes, incubated with hemolymph taken from insects fed on control blood or blood infected with epimastigotes, drastically reduced the proPO activation. The proteolytic activity in the fat body homogenates of control insects was significantly higher than in those obtained from fat body extracts of insects previously fed on blood containing epimastigotes. These findings indicate that the reduction of the proteolytic activities in the fat body from insects fed on infected blood no longer allows a significant response of the proPO system against parasite challenge. It also provides a better understanding of T. rangeli infection in the vector and offer novel insights into basic immune processes in their invertebrate hosts.
Gomes
S A O
SA
Instituto Oswaldo Cruz, Fundação Oswaldo Cruz, Departamento de Bioquímica e Biologia Molecular, Av. Brasil 4365, Rio de Janeiro 21045-900, Brazil.
Feder
D
D
Garcia
E S
ES
Azambuja
P
P
D000818:Animals; D004156:Catechol Oxidase / Q000378:metabolism*; D015536:Down-Regulation; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000378:metabolism*; D005216:Fat Body / Q000201:enzymology; D006458:Hemolymph / Q000201:enzymology; D012239:Rhodnius / Q000201:enzymology* / Q000469:parasitology*; D013997:Time Factors; D014345:Trypanosoma / Q000254:growth & development / Q000502:physiology*; D014357:Trypsin / Q000378:metabolism
D004792:Enzyme Precursors; C038451:pro-phenoloxidase; D004156:Catechol Oxidase; D014357:Trypsin