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Infect Immun, July 1998, p. 3420-3422, Vol. 66, No. 7
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

The inlA Gene of Listeria monocytogenes LO28 Harbors a Nonsense Mutation Resulting in Release of Internalin

Renaud Jonquières, Hélène Bierne, Jérôme Mengaud, and Pascale Cossart*

Unité des Interactions Bactéries-Cellules, Institut Pasteur, Paris, France

Received 4 February 1998/Returned for modification 6 March 1998/Accepted 2 April 1998

Internalin is a surface protein that mediates entry of Listeria monocytogenes EGD into epithelial cells expressing the cell adhesion molecule human E-cadherin or its chicken homolog, L-CAM, which act as receptors for internalin. After observing that entry of L. monocytogenes LO28 into S180 fibroblasts, in contrast to that of EGD, did not increase after transfection with L-CAM, we examined both the expression and the structure of internalin in strain LO28. We discovered a nonsense mutation in inlA which results in a truncated protein released in the culture medium. Mutations leading to release of internalin were also detected in clinical and food isolates. These results question the role of internalin as a virulence factor in murine listeriosis.

* Corresponding author. Mailing address: Unité des Interactions Bactéries-Cellules, Institut Pasteur, 28 Rue du Docteur Roux, 75724 Paris Cedex 15, France. Phone: 33 1 45 68 88 41. Fax: 33 1 45 68 87 06. E-mail: pcossart{at}pasteur.fr.

Infect Immun, July 1998, p. 3420-3422, Vol. 66, No. 7
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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Copyright © 1998 by the American Society for Microbiology. All rights reserved.