n-terminal gly224–gly411 domain in listeria adhesion protein interacts with host receptor hsp60氨基端gly224-gly411域在李斯特菌粘附蛋白与宿主相互作用受体hsp60.pdfVIP

N-Terminal Gly224–Gly411 Domain in Listeria Adhesion Protein Interacts with Host Receptor Hsp60 1 1,2 1 Balamurugan Jagadeesan , Amy E. Fleishman Littlejohn , Mary Anne Roshni Amalaradjou , Atul K. 1 1 3 2,3,4 1,2,5 Singh , Krishna K. Mishra , David La , Daisuke Kihara , Arun K. Bhunia * 1 Molecular Food Microbiology Laboratory, Department of Food Science, Purdue University, West Lafayette, Indiana, United States of America, 2 Purdue University Interdisciplinary Life Sciences Program, Purdue University, West Lafayette, Indiana, United States of America, 3 Department of Biological Sciences, Purdue University, West Lafayette, Indiana, United States of America, 4 Department of Computer Science, Purdue University, West Lafayette, Indiana, United States of America, 5 Department of Comparative Pathobiology, Purdue University, West Lafayette, Indiana, United States of America 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