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Infection and Immunity, January 2003, p. 557-561, Vol. 71, No. 1
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.1.557-561.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Involvement of Trypanosoma cruzi Metacyclic Trypomastigote Surface Molecule gp82 in Adhesion to Gastric Mucin and Invasion of Epithelial Cells

Ivan Neira, Fernando A. Silva,{dagger} Mauro Cortez, and Nobuko Yoshida*

Departamento de Microbiologia, Imunologia e Parasitologia, Escola Paulista de Medicina, Universidade Federal de São Paulo, São Paulo, Brazil

Received 24 June 2002/ Returned for modification 26 August 2002/ Accepted 10 October 2002

Upon oral infection, Trypanosoma cruzi metacyclic trypomastigotes invade and replicate in the gastric mucosal epithelium, being apparently uniquely specialized for adhesion to mucin and mucosal invasion. Here we investigated the involvement of gp82, the metacyclic-stage-specific surface glycoprotein implicated in host cell entry, in both adhesion to gastric mucin and invasion of the mucosal epithelium upon oral challenge. Metacyclic forms, preincubated with a control monoclonal antibody (MAb) or with MAb 3F6 directed to gp82, were administered orally to BALB/c mice, and parasitemia was monitored. Mice that received parasites treated with MAb 3F6 had greatly reduced parasitemia, displaying at the peak a mean number of blood parasites more than 100-fold lower than that of the control group. MAbs directed to other T. cruzi surface glycoproteins had no such effect. gp82, as either a native or a recombinant molecule, but not the metacyclic trypomastigote surface molecule gp90 or gp35/50, bound to gastric mucin in enzyme-linked immunosorbent assays. MAb 3F6 significantly inhibited the penetration of cultured epithelial HeLa cells by metacyclic forms in the absence or in the presence of gastric mucin. Mucin alone did not affect parasite internalization. Parasite infectivity was not altered by treatment of metacyclic forms with pepsin, to which gp82 was resistant, or with proteinase K, which removed the N-terminal portion of gp82 but preserved its host cell binding site. Taken together, these findings suggest that gp82 mediates the interaction of metacyclic trypomastigotes with gastric mucin and the subsequent penetration of underlying epithelial cells.

* Corresponding author. Mailing address: Escola Paulista de Medicina, Universidade Federal de São Paulo, R. Botucatu, 862-60 Andar, 04023-062 São Paulo, SP, Brazil. Phone: 55-11-5576-4532. Fax: 55-11-5571-1095. E-mail: nyoshida{at}ecb.epm.br.

Editor: W. A. Petri, Jr.

{dagger} Present address: Universidade de São Paulo, Instituto de Ciências Biomédicas, Departamento de Farmacologia, São Paulo, SP, Brazil.

Infection and Immunity, January 2003, p. 557-561, Vol. 71, No. 1
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.1.557-561.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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