N-Terminal Gly224–Gly411 Domain in Listeria Adhesion Protein Interacts with Host Receptor Hsp60
2011
Listeria Adhesion Protein Interacts with Host Receptor Hsp60
publication
Evidence: high
Author Information
Author(s): Jagadeesan Balamurugan, Fleishman Littlejohn Amy E., Amalaradjou Mary Anne Roshni, Singh Atul K., Mishra Krishna K., La David, Kihara Daisuke, Bhunia Arun K.
Primary Institution: Purdue University
Hypothesis
Which LAP subdomain(s) interact with Hsp60?
Conclusion
The N2 subdomain in the LAP ALDH domain is critical for initiating interaction with the mammalian cell receptor Hsp60.
Supporting Evidence
- The N2 subdomain showed significantly higher binding to Hsp60 compared to other subdomains.
- N2-coated microspheres had the highest adherence to HCT-8 cells.
- Pretreatment with anti-Hsp60 antibody reduced binding of N2-coated microspheres.
Takeaway
The study found that a specific part of a protein from Listeria bacteria helps it stick to human cells, which could help in preventing infections.
Methodology
LAP subdomains were cloned, expressed in E. coli, and their binding to Hsp60 was analyzed using ligand overlay, immunofluorescence, and bead-based adhesion assays.
Statistical Information
P-Value
p<0.05
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
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