S18.11 Potential regulatory role of sialic acid modifications in cell adhesion mediated by murine sialo-adhesin as a macrophage-restricted cell adhesion molecule

1993 ◽  
Vol 10 (4) ◽  
pp. 330-330 ◽  
Author(s):  
S. Kelm ◽  
A. Pelz ◽  
R. Schauer ◽  
P. R. Crocker
Author(s):  
Kenji Hagimori ◽  
Hidenori Kato ◽  
Keiko Fukuda ◽  
Masaharu Kikuta ◽  
Yasuhiro Tsukamoto ◽  
...  

1998 ◽  
Vol 66 (7) ◽  
pp. 3420-3422 ◽  
Author(s):  
Renaud Jonquières ◽  
Hélène Bierne ◽  
Jérôme Mengaud ◽  
Pascale Cossart

ABSTRACT Internalin is a surface protein that mediates entry ofListeria 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.


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