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Measles pp 163–191Cite as

Measles Virus Interaction with Host Cells and Impact on Innate Immunity

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Part of the book series: Current Topics in Microbiology and Immunology ((CT MICROBIOLOGY,volume 329))

Because viruses are obligate parasites, numerous partnerships between measles virus and cellular molecules can be expected. At the entry level, measles virus uses at least two cellular receptors, CD150 and a yet to be identified epithelial receptor to which the virus H protein binds. This dual receptor strategy illuminates the natural infection and inter-human propagation of this lymphotropic virus. The attenuated vaccine strains use CD46 as an additional receptor, which results in a tropism alteration. Surprisingly, the intracellular viral and cellular protein partnership leading to optimal virus life cycle remains mostly a black box, while the interactions between viral proteins that sustain the RNA-dependant RNA polymerase activity (i.e., transcription and replication), the particle assembly and the polarised virus budding are documented. Hsp72 is the only cellular protein that is known to regulate the virus transcription and replication through its interaction with the viral N protein. The viral P protein is phosphorylated by the casein kinase II with undetermined functional consequences. The cellular partnership that controls the intracellular trafficking of viral components, the assembly and/or the budding of measles virus, remains unknown. The virus to cell innate immunity war is better documented. The 5′ triphosphate-ended virus leader transcript is recognised by RIG-I, a cellular helicase, and induces the interferon response. Measles virus V protein binds to the MDA5 helicase and prevents the MDA5-mediated activation of interferon. By interacting with STAT1 and Jak1, the viral P and V proteins prevent the type I interferon receptor (IFNAR) signalling. The virus N protein interacts with eIF3-p40 to inhibit the translation of cellular mRNA. The H protein binds to TLR2, which then transduces an activation signal and CD150 expression in monocytes. The P protein activates the expression of the ubiquitin modifier A20, thus blocking the TLR4-mediated signalling. Few other partnerships between measles virus components and cellular proteins have been postulated or demonstrated, and they need further investigations to understand their physiopathological outcome.

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  1. Interactions virus cellule-hôte; CNRS, Université de Lyon 1, FRE3011, IFR 62, Laennec, Lyon Cedex 08, 69372, France

    D. Gerlier

  2. Interaction virus-système immunitaire; INSERM; U851, IFR128 BioSciences Lyon-Gerland, Université de Lyon 1, UCBL1 (Lyon, 69003); Hospices Civils de Lyon (Lyon, 69002) 21 Avenue Tony Garnier, Lyon Cedex 07, 69365, France

    H. Valentin

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  1. Department of Molecular Microbiology, Johns Hopkins University School of Hygiene and Public Health, 615 N. Wolfe Street, Baltimore, MD, 21205, USA

    Diane E. Griffin

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Gerlier, D., Valentin, H. (2009). Measles Virus Interaction with Host Cells and Impact on Innate Immunity. In: Griffin, D.E., Oldstone, M.B.A. (eds) Measles. Current Topics in Microbiology and Immunology, vol 329. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-70523-9_8

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