Genetic Structure and Expression of the Surface Glycoprotein GP82, the Main Adhesin ofTrypanosoma cruziMetacyclic Trypomastigotes

Author:

Correa Paulo Roberto Ceridorio1,Cordero Esteban Mauricio1,Gentil Luciana Girotto1,Bayer-Santos Ethel1ORCID,Silveira José Franco da1

Affiliation:

1. Departamento de Microbiologia, Imunologia e Parasitologia, Escola Paulista de Medicina, Universidade Federal de São Paulo, Rua Botucatu 862, 04023-062 São Paulo, SP, Brazil

Abstract

T. cruziimproves the likelihood of invading or adapting to the host through its capacity to present a large repertoire of surface molecules. The metacyclic stage-specific surface glycoprotein GP82 has been implicated in host cell invasion. GP82 is encoded by multiple genes from the trans-sialidase superfamily. GP82 shows a modular organization, with some variation of N-terminal region flanking a conserved central core where the binding sites to the mammalian cell and gastric mucin are located. The function of GP82 as adhesin in host cell invasion process could expose the protein to an intense conservative and selective pressure. GP82 is a GPI-anchored surface protein, synthesized as a 70 kDa precursor devoid ofN-linked sugars. GPI-minus variants accumulate in the ER indicating that GPI anchor acts as a forward transport signal for progressing along the secretory pathway as suggested forT. cruzimucins. It has been demonstrated that the expression of GP82 is constitutive and may be regulated at post-transcriptional level, for instance, at translational level and/or mRNA stabilization. GP82 mRNAs are mobilized to polysomes and consequently translated, but only in metacyclic trypomastigotes. Analysis of transgenic parasites indicates that the mechanism regulating GP82 expression involves multiple elements in the 3′UTR.

Funder

FAPESP

Publisher

Hindawi Limited

Subject

General Environmental Science,General Biochemistry, Genetics and Molecular Biology,General Medicine

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