Inhibition of the complement system by saliva of Anopheles (Nyssorhynchus) aquasalis

dc.creatorSousa, Antonio Ferreira Mendes
dc.creatorVale, Vladimir Fazito
dc.creatorQueiroz, Daniel Costa
dc.creatorPereira Filho, Adalberto Alves
dc.creatorSilva, Naylene Carvalho Sales da
dc.creatorKoerich, Leonardo Barbosa
dc.creatorMoreira, Luciano Andrade
dc.creatorPereira, Marcos Horácio
dc.creatorSant’Anna, Maurício Roberto
dc.creatorAraújo, Ricardo Nascimento
dc.creatorAndersen, John
dc.creatorValenzuela, Jesus Gilberto
dc.creatorGontijo, Nelder Figueiredo
dc.date2018-03-21T13:58:53Z
dc.date2018-03-21T13:58:53Z
dc.date2018
dc.date.accessioned2023-09-26T20:36:45Z
dc.date.available2023-09-26T20:36:45Z
dc.identifierSOUSA, Antonio Ferreira Mendes et al. Inhibition of the complement system by saliva of Anopheles (Nyssorhynchus) aquasalis. Insect Biochemistry and Molecular Biology, v. 92, p. 12-20, 2018.
dc.identifier0965-1748
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/25440
dc.identifier10.1016/j.ibmb.2017.11.004
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8860573
dc.descriptionAnopheline mosquitoes are vectors of malaria parasites. Their saliva contains anti-hemostatic and immune-modulator molecules that favor blood feeding and parasite transmission. In this study, we describe the inhibition of the alternative pathway of the complement system (AP) by Anopheles aquasalis salivary gland extracts (SGE). According to our results, the inhibitor present in SGE acts on the initial step of the AP blocking deposition of C3b on the activation surfaces. Properdin, which is a positive regulatory molecule of the AP, binds to SGE. When SGE was treated with an excess of properdin, it was unable to inhibit the AP. Through SDS-PAGE analysis, A. aquasalis presented a salivary protein with the same molecular weight as recombinant complement inhibitors belonging to the SG7 family described in the saliva of other anopheline species. At least some SG7 proteins bind to properdin and are AP inhibitors. Searching for SG7 proteins in the A. aquasalis genome, we retrieved a salivary protein that shared an 85% identity with albicin, which is the salivary alternative pathway inhibitor from A. albimanus. This A. aquasalis sequence was also very similar (81% ID) to the SG7 protein from A. darlingi, which is also an AP inhibitor. Our results suggest that the salivary complement inhibitor from A. aquasalis is an SG7 protein that can inhibit the AP by binding to properdin and abrogating its stabilizing activity. Albicin, which is the SG7 from A. albimanus, can directly inhibit AP convertase. Given the high similarity of SG7 proteins, the SG7 from A. aquasalis may also directly inhibit AP convertase in the absence of properdin.
dc.description2024-01-01
dc.formatapplication/pdf
dc.languageeng
dc.publisherPergamon Press
dc.rightsrestricted access
dc.subjectAnopheles aquasalis
dc.subjectsistema complementar
dc.subjectAnopheles aquasalis
dc.subjectSaliva
dc.subjectComplement system
dc.subjectAlternative pathway
dc.subjectComplement system inhibition
dc.subjectHematophagy
dc.titleInhibition of the complement system by saliva of Anopheles (Nyssorhynchus) aquasalis
dc.typeArticle


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