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Use of surface plasmon resonance for the measurement of low affinity binding interactions between HSP72 and measles virus nucleocapsid protein

Biological Procedures Online volume 5, pages 170–181 (2003)Cite this article

Abstract

The 72 kDa heat shock protein (HSP72) is a molecular chaperone that binds native protein with low affinity. These interactions can alter function of the substrate, a property known as HSP-mediated activity control. In the present work, BIAcore instrumentation was used to monitor binding reactions between HSP72 and naturally occurring sequence variants of the measles virus (MV) nucleocapsid protein (N), a structural protein regulating transcription/replication of the viral genome. Binding reactions employed synthetic peptides mimicking a putative HSP72 binding motif of N. Sequences were identified that bound HSP72 with affinities comparable to well-characterized activity control reactions. These sequences, but not those binding with lesser affinity, supported HSP72 activity control of MV transcription/replication. BIAcore instrumentation thus provides an effective way to measure biologically relevant low affinity interactions with structural variants of viral proteins.

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Authors and Affiliations

  1. Department of Veterinary Biosciences, The Ohio State University, 1925 Coffey Road, 43210, Columbus, OH

    Xinsheng Zhang & Michael Oglesbee

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  1. Xinsheng Zhang
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  2. Michael Oglesbee
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Correspondence to Michael Oglesbee.

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Published: September 5, 2003

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Zhang, X., Oglesbee, M. Use of surface plasmon resonance for the measurement of low affinity binding interactions between HSP72 and measles virus nucleocapsid protein. Biol. Proced. Online 5, 170–181 (2003). https://doi.org/10.1251/bpo59

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  • DOI: https://doi.org/10.1251/bpo59

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Biological Procedures Online

ISSN: 1480-9222

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