A comparative approach on the activation of the three complement system pathways in different hosts of Visceral Leishmaniasis after stimulation with Leishmania infantum. (July 2021)

• Record Type: Journal Article
• Authors: Tirado, Thais Cristina; Bavia, Lorena; Ambrosio, Altair Rogerio; Campos, Monique Paiva; de Almeida Santiago, Marta; Messias-Reason, Iara Jose; Figueiredo, Fabiano Borges
• Is Part Of: Developmental and comparative immunology. Volume 120(2021)
• Publication Date: 2021-07
• Subjects: Classical pathway -- Alternative pathway -- Lectin pathway -- Dog -- Cat -- Leishmania infantum; Immunology -- Periodicals; Developmental immunology -- Periodicals; 616.079
• DOI: 10.1016/j.dci.2021.104061
• Languages: English
• ISSNs: 0145-305X

Abstract

Abstract: Visceral Leishmaniasis is an infectious disease that affects mainly humans and dogs, with the latter being important reservoirs of the parasite. Conversely, cats are naturally resistant. The immune system can offer important explanation to this problematic as there is no evidence on the role that the complement system plays in cats. In this context, effect of the complement system from human, dog and cat sera on Leishmania infantum was evaluated. Activation of the classical, alternative and lectin pathways was assessed through hemolytic and ELISA assays. Lytic activity of the complement on the parasite's viability was investigated by Transmission Electron Microscopy and Flow Cytometry. Complement proteins were more consumed in dog serum on the classical and alternative pathways, leading to less hemolytic activity, and only in cat serum they were consumed on the lectin pathway when incubated with L. infantum . Lytic activity on the parasite's surface was more accentuated in human serum, and varied throughout the parasite's developmental stages. Highlights: Complement system pathways are differently activated by L. infantum between hosts. Dog proteins are more consumed by L. infantum in classical and alternative pathways. L. infantum was able to consume the lectin complement proteins only in cat serum. Human serum presented the highest complement-mediated lysis.