Author
Carlson, Steven | |
WILSON, R - UNIVERSITY OF IOWA | |
OMARY, M - VA PALO ALTO HLTH CARE | |
JONES, B - UNIVERSITY OF IOWA |
Submitted to: Meeting Abstract
Publication Type: Abstract Only Publication Acceptance Date: 9/15/1999 Publication Date: N/A Citation: N/A Interpretive Summary: Technical Abstract: Pathogenic Salmonella species initiate infection of a host by inducing their own uptake into intestinal M-cells. During the uptake process, the bacteria utilize an intrinsic secretion system to release proteins that enter host cells. The secreted invasion-mediating proteins subsequently interact with host cell components that induce alterations in the actin cytoskeleton. To identify potential cellular determinants of invasion, we employed a yeast two-hybrid system using the secreted Salmonella invasion protein SipC as the bait protein. This system identified the family of cytokeratins, supportive components of the cytoskeletal matrix, as proteins that may physically interact with SipC. Dominant negative transfection-based studies revealed a mild inhibition of Salmonella invasion when endogenous cytokeratin-18 expression was perturbed. Immunofluorescent microscopy studies identified a co-condensation of actin and cytokeratins at the site of Salmonella entry into HEp-2 cells. These results indirectly suggest that a component of Salmonella invasion may occur as part of an interaction between SipC and cytokeratin-18. In addition, these experiments suggest the presence of a pathway from a cytokeratin to an actin rearrangement process that may participate in homeostatic cytoskeletal functions. |