Antigenic diversity of MASP gene family of Trypanosoma cruzi

Microbes Infect. 2022 Sep;24(6-7):104982. doi: 10.1016/j.micinf.2022.104982. Epub 2022 Apr 26.

Abstract

Trypanosoma cruzi, the etiological agent of Chagas disease (CD), is a heterogeneous species with high genetic and phenotypic diversity. MASP is the second largest multigene family of T. cruzi. The high degree of polymorphism of the family associated with its location at the surface of infective forms of T. cruzi suggests that MASP participates in mechanisms of host-parasite interaction. In this work, MASP members were divided into 7 subgroups based on protein sequence similarity, and one representative member from each subgroup was chosen to be expressed recombinantly. Immunogenicity of recombinant MASP proteins (rMASP) was investigated using different sera panels from T. cruzi infected mice. To mimic a natural condition in which different MASP members are expressed at the same time in the parasite population, a multiplex bead-based flow cytometry assay was also standardized. Results showed that rMASPs are poorly recognized by sera from mice infected with Colombiana strain, whereas sera from mice infected with CL Brener and Y display high reactivity against the majority of rMASPs tested. Flow cytometry showed that MASP recognition profile changes 10 days after infection. Also, multiplex assay suggests that MASP M1 and M2 are more immunogenic than the other MASP members evaluated that may play an immunodominant role during infection.

Keywords: Immunogenicity; MASP; Multigene; Multiplex assay; T. cruzi; Variability.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antigenic Variation
  • Chagas Disease* / parasitology
  • Mannose-Binding Protein-Associated Serine Proteases / genetics
  • Mannose-Binding Protein-Associated Serine Proteases / metabolism
  • Mice
  • Protozoan Proteins / metabolism
  • Trypanosoma cruzi* / genetics
  • Trypanosoma cruzi* / metabolism

Substances

  • Protozoan Proteins
  • Mannose-Binding Protein-Associated Serine Proteases