The C-terminal region of Trypanosoma cruzi MASPs is antigenic and secreted via exovesicles.
Trypanosoma cruzi is the etiological agent of Chagas disease, a neglected and emerging tropical disease, endemic to South America and present in non-endemic regions due to human migration. The MASP multigene family is specific to T. cruzi, accounting for 6% of the parasite's genome and plays a key role in immune evasion. A common feature of MASPs is the presence of two conserved regions: an N-terminal region codifying for signal peptide and a C-terminal (C-term) region, which potentially acts as GPI-addition signal peptide. Our aim was the analysis of the presence of an immune response against the MASP C-term region. We found that this region is highly conserved, released via exovesicles (EVs) and has an associated immune response as revealed by epitope affinity mapping, IFA and inhibition of the complement lysis assays. We also demonstrate the presence of a fast IgM response in Balb/c mice infected with T. cruzi. Our results reveal the presence of non-canonical secreted peptides in EVs, which can subsequently be exposed to the immune system with a potential role in evading immune system targets in the parasite.
Departamento de Parasitología, Grupo de Bioquímica y Parasitología Molecular, Campus de Fuentenueva, Universidad de Granada, 18071 Granada, Spain.|Center for Immunology and Infection (CII), Biology Department, University of York, York, UK.
Luis Miguel
LM
De Pablos
Departamento de Parasitología, Grupo de Bioquímica y Parasitología Molecular, Campus de Fuentenueva, Universidad de Granada, 18071 Granada, Spain.
Isabel María
IM
Díaz Lozano
Parasitology Reference Laboratory, Instituto de Salud Pública de Chile, Avenida Marathon 1000, 7780050 Santiago, Chile.
Maria Isabel
MI
Jercic
Departamento de Microbiología y Parasitología, Facultad de Medicina, Universidad de Panamá, República de Panamá
Markela
M
Quinzada
Servicio de Microbiología Hospital Universitario y Politécnico La Fe, Valencia, Spain.
Maria José
MJ
Giménez
Servicio de Microbiología Hospital Universitario y Politécnico La Fe, Valencia, Spain.
Eva
E
Calabuig
Laboratory of Immunology and Molecular Parasitology, Department of Microbiology, University of Puerto Rico, School of Medicine. PO BOX 365067, San Juan, 00936-5067, Puerto Rico.
Ana Margarita
AM
Espino
Laboratorio de Biología Molecular de la Enfermedad de Chagas, INGEBI-CONICET, Buenos Aires, Argentina.
Alejandro Gabriel
AG
Schijman
Laboratorio de Parasitología Básico-Clínico, Instituto de Ciencias Biomédicas, Facultad de Medicina, Universidad de Chile, Santiago, Chile.
Inés
I
Zulantay
Laboratorio de Parasitología Básico-Clínico, Instituto de Ciencias Biomédicas, Facultad de Medicina, Universidad de Chile, Santiago, Chile.
Werner
W
Apt
Departamento de Parasitología, Grupo de Bioquímica y Parasitología Molecular, Campus de Fuentenueva, Universidad de Granada, 18071 Granada, Spain.
Antonio
A
Osuna
D000818:Animals; D000913:Antibodies, Protozoan / Q000097:blood; D000953:Antigens, Protozoan / Q000737:chemistry* / Q000378:metabolism; D014355:Chagas Disease / Q000097:blood / Q000276:immunology*; D004195:Disease Models, Animal; D018604:Epitope Mapping; D000067128:Extracellular Vesicles / Q000378:metabolism*; D006801:Humans; D007075:Immunoglobulin M / Q000097:blood; D050606:Mannose-Binding Protein-Associated Serine Proteases / Q000737:chemistry* / Q000378:metabolism; D051379:Mice; D008807:Mice, Inbred BALB C; D005810:Multigene Family; D014349:Trypanosoma cruzi / Q000276:immunology* / Q000378:metabolism
D000913:Antibodies, Protozoan; D000953:Antigens, Protozoan; D007075:Immunoglobulin M; D050606:Mannose-Binding Protein-Associated Serine Proteases