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Peptides ¹⁴VIDLL¹⁸ and ⁹⁶FEAAAL¹⁰¹ defined as epitopes of antibodies raised against amino acid sequences of enterotoxigenic Escherichia coli colonization factor antigen I fused to Salmonella flagellin

Maria G. Luna^1,,1

Instituto de Biofísica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro, Cidade Universitária, Rio de Janeiro, 21949-900, RJ, Brazil
Department of Medical Microbiology and Immunology, Göteborg University, S-413 46 Göteborg, Sweden

¹ Author for correspondence: Maria G. Luna. Tel: +55 21 5876380. Fax: +55 21 5876476. e-mail: luna@uerj.br

ABSTRACT

Antibodies raised against four hybrid Salmonella flagellins carrying amino acid sequences derived from the fimbrial subunit of the colonization factor I antigen (CFA/I) of enterotoxigenic Escherichia coli (ETEC), i.e. hybrid flagellins Fla I (aa 1-15), Fla II (aa 11-25), Fla III (aa 32-45) and Fla IV (aa 88-102), were not able to inhibit the in vitro binding of CFA/I-expressing ETEC bacteria to enterocyte-like Caco-2 cells. However, one of the hybrid flagellins (Fla II) was recognized by a previously described anti-CFA/I subunit mAb (S-CFA/I 17:8) which was able to block adhesion of CFA/l-expressing bacteria to Caco-2 cells and to bind to the amino acid sequence ¹⁵IDLLQ¹⁹ of the CFA/I fimbrial subunit. Pepscan analysis of antibodies raised against the hybrid flagellins Fla II and Fla IV showed that they were specific for the sequences ¹⁴VIDLL¹⁸ and ⁹⁶FEAAAL¹⁰¹, respectively, of the CFA/I fimbrial subunit. Thus, the discrepancy in the abilities of the anti-Fla II serum and the mAb S-CFA/I 17:8 to block binding might be ascribed to their slightly different fine specificity for epitopes.

Present address: Disciplina de Microbiologia e imunologia, Faculdade de Ciências Médicas, Universidade do Estado do Rio de Janeiro, Av. 28 de Setembro 87 fundos - 3° andar, 20551-030, Rio de Janeiro, RJ, Brazil.

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