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- Title
N-Terminal Gly<sub>224</sub>-Gly<sub>411</sub> Domain in Listeria Adhesion Protein Interacts with Host Receptor Hsp60.
- Authors
Jagadeesan, Balamurugan; Littlejohn, Amy E. Fleishman; Amalaradjou, Mary Anne Roshni; Singh, Atul K.; Mishra, Krishna K.; La, David; Kihara, Daisuke; Bhunia, Arun K.
- Abstract
Background: Listeria adhesion protein (LAP) is a housekeeping bifunctional enzyme consisting of N-terminal acetaldehyde dehydrogenase (ALDH) and C-terminal alcohol dehydrogenase (ADH). It aids Listeria monocytogenes in crossing the epithelial barrier through a paracellular route by interacting with its host receptor, heat shock protein 60 (Hsp60). To gain insight into the binding interaction between LAP and Hsp60, LAP subdomain(s) participating in the Hsp60 interaction were investigated. Methods: Using a ModBase structural model, LAP was divided into 4 putative subdomains: the ALDH region contains N1 (Met1-Pro223) and N2 (Gly224-Gly411), and the ADH region contains C1 (Gly412-Val648) and C2 (Pro649-Val866). Each subdomain was cloned and overexpressed in Escherichia coli and purified. Purified subdomains were used in ligand overlay, immunofluorescence, and bead-based epithelial cell adhesion assays to analyze each domain's affinity toward Hsp60 protein or human ileocecal epithelial HCT-8 cells. Conclusion: These data indicate that the N2 subdomain in the LAP ALDH domain is critical in initiating interaction with mammalian cell receptor Hsp60 providing insight into the molecular mechanism of pathogenesis for the development of potential anti-listerial control strategies.
- Publication
PLoS ONE, 2011, Vol 6, Issue 6, p1
- ISSN
1932-6203
- Publication type
Academic Journal
- DOI
10.1371/journal.pone.0020694