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Infection and Immunity, July 2002, p. 3611-3620, Vol. 70, No. 7
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.7.3611-3620.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Expression of the Plasmodium falciparum Immunodominant Epitope (NANP)4 on the Surface of Salmonella enterica Using the Autotransporter MisL

Fernando Ruiz-Pérez,1,2 Rocío León-Kempis,1 Araceli Santiago-Machuca,1 Guadalupe Ortega-Pierres,2 Eileen Barry,3 Myron Levine,3 and César González-Bonilla1*

Unidad de Investigación Médica en Inmunología e Infectología, Hospital de Infectología "Dr. Daniel Méndez Hernández," Centro Médico "La Raza," Instituto Mexicano del Seguro Social,,1 Biomedicina Molecular, Genética y Biología Molecular, Centro de Investigación y Estudios Avanzados del IPN, Mexico D.F., Mexico,2 Center for Vaccine Development, University of Maryland School of Medicine, Baltimore, Maryland3

Received 19 November 2001/ Returned for modification 11 February 2002/ Accepted 27 March 2002

Gram-negative bacterial proteins which are exported from the cytosol to the external environment by the type V secretion system are also known as autotransporters. Once translocated to the periplasmic compartment by the sec-dependent general secretory pathway, their C-terminal domain forms a pore through which the N-terminal domain travels to the outer membrane without the need of other accessory proteins. MisL (protein of membrane insertion and secretion) is a protein of unknown function located in the pathogenicity island SPI-3 of Salmonella enterica and classified as an autotransporter due to its high homology to Escherichia coli AIDA-I. In the present work, the MisL C-terminal translocator domain was used to display the immunodominant B-cell epitope of the circumsporozoite protein (CSP) from Plasmodium falciparum on the surface of Salmonella enterica serovar Typhimurium (serovar Typhimurium SL3261) and serovar Typhi (serovar Typhi CVD 908). The MisL ß domain was predicted by alignment with AIDA-I, amplified from serovar Typhimurium SL3261, cloned in a plasmid fused to four repeats of the tetrapeptide NANP behind the Escherichia coli heat-labile enterotoxin B subunit signal peptide to ensure periplasmic traffic, and expressed under the control of the anaerobically inducible nirB promoter. The fusion protein was translocated to the outer membrane of both bacterial strains, although the foreign epitope was displayed more efficiently in serovar Typhimurium SL3261, which elicited a better specific antibody response in BALB/c mice. More importantly, antibodies were able to recognize the native CSP in P. falciparum sporozoites. These results confirm that MisL is indeed an autotransporter and that it can be used to express foreign immunogenic epitopes on the surface of gram-negative bacteria.

* Corresponding author. Mailing address: Hospital de Infectología "Dr. Daniel Méndez Hernández," Centro Médico "La Raza," IMSS, Apartado Postal 15-095, Mexico D.F., Mexico. Phone: (052) 55 5724 5900, ext. 5201. Fax: (052) 55 5583 0626. E-mail: bonilla{at}conacyt.mx.

Editor: A. D. O'Brien

Infection and Immunity, July 2002, p. 3611-3620, Vol. 70, No. 7
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.7.3611-3620.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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