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Isolation and Identification of Dengue Virus Interactome with Human Plasma Proteins by Affinity Purification-Mass Spectrometry

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Dengue Virus

Part of the book series: Methods in Molecular Biology ((MIMB,volume 2409))

Abstract

Viral proteins evolve to benefit the interaction with host proteins during the infection and replication processes. A comprehensive understanding of virus interactome with host proteins may thus lead to the identification of molecular targets for infection inhibition. We present a procedure for isolating and identifying the dengue virus interactome with human plasma proteins. It comprises the fractionation of human plasma by anion exchange chromatography, followed by affinity purification and mass spectrometry identification of the captured proteins. This procedure was applied to the characterization of the interactions of the four serotypes of dengue virus with human plasma proteins, mediated by the domain III of the envelope protein of the virus. The resulting interactome comprises 62 proteins, six of which were validated as new direct interactions of the virus with its human host.

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Authors and Affiliations

  1. Division of System Biology, Center for Genetic Engineering and Biotechnology, Havana, Cuba

    Vivian Huerta & Yassel Ramos

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  1. Vivian Huerta
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  2. Yassel Ramos
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Correspondence to Vivian Huerta .

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Editors and Affiliations

  1. Biophysics Institute Carlos Chagas Filho, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil

    Ronaldo Mohana-Borges

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Huerta, V., Ramos, Y. (2022). Isolation and Identification of Dengue Virus Interactome with Human Plasma Proteins by Affinity Purification-Mass Spectrometry. In: Mohana-Borges, R. (eds) Dengue Virus. Methods in Molecular Biology, vol 2409. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-1879-0_10

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  • DOI: https://doi.org/10.1007/978-1-0716-1879-0_10

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  • Publisher Name: Humana, New York, NY

  • Print ISBN: 978-1-0716-1878-3

  • Online ISBN: 978-1-0716-1879-0

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