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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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