@article{jonquières_bierne_mengaud_cossart_1998, 
  title={The inlA Gene of Listeria monocytogenesLO28 Harbors a  Nonsense Mutation Resulting in Release of Internalin}, 
  volume={66}, 
  DOI={10.1128/iai.66.7.3420-3422.1998}, 
  abstractNote={<jats:p>Internalin is a surface protein that mediates entry of<jats:italic>Listeria monocytogenes</jats:italic> 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 <jats:italic>L. monocytogenes</jats:italic> 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 <jats:italic>inlA</jats:italic> 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.</jats:p>}, 
  publisher={American Society for Microbiology}, 
  author={Jonquières, Renaud and Bierne, Hélène and Mengaud, Jérôme and Cossart, Pascale}, 
  year={1998}
  }