Investigation of the Binding Mechanism between Internalin B and Heparin using Surface Plasmon Resonance

Authors
Hrtska, Sybil C.Lang
Kemp, Melissa M.
Muñoz, Eva M.
Azizad, Omaira
Banerjee, Mani
Raposo, Catarina
Kumaran, Jyothi
Ghosh, Partho
Linhardt, Robert J.
ORCID
https://orcid.org/0000-0003-2219-5833
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Issue Date
2007-03-13
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
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Full Citation
Investigation of the Binding Mechanism between Internalin B and Heparin using Surface Plasmon Resonance, S. Lang, M. M. Kemp, E. M. Muñoz, O. Azizad, M. Banerjee, J. Kumaran, P. Ghosh, R. J. Linhardt, Biochemistry, 46, 2697 -2706, 2007.
Abstract
Listeria monocytogenes, a food-borne pathogen that infects immunocompromised patients, enters and proliferates within mammalian cells by taking advantage of host cell machinery. While entry into macrophages and other phagocytic cells occurs constitutively, intracellular invasion of nonphagocytic cells, such as epithelial and endothelial cells, occurs through induced phagocytosis. Invasion of these nonphagocytic cell types is under the control of the secreted L. monocytogenes protein internalin B (InlB), which directly associates with and activates the receptor tyrosine kinase Met. Activation of Met by InlB has previously been shown to be potentiated by binding of glycosaminoglycans to the GW domains of this protein. We studied the interaction between heparin and full-length InlB as well as a truncated, functional form of InlB to understand the mode of interaction between these two molecules. InlB preferred long-chain (>or=dp14) heparin oligosaccharides, and the interaction with heparin fit a complicated binding model with a dissociation constant in the nanomolar range. While there are various explanations for this complicated binding model, one supported by our data involves binding and rebinding of InlB to multiple binding sites on heparin in a positive and weakly cooperative manner. This mode is consistent with enhancement of interaction of InlB with glycosaminoglycans for activation of Met.
Description
Biochemistry, 46, 2697-2706
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Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
Publisher
American Chemical Society (ACS)
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
Biochemistry
https://harc.rpi.edu/
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A full text version is available in DSpace@RPI