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Structure, Function, and Intracellular Processing of the Glycoproteins of Paramyxoviridae

  • Chapter
The Paramyxoviruses

Part of the book series: The Viruses ((VIRS))

Abstract

The membranes of Paramyxoviridae virions are studded with spike structures which can be readily visualized in electron micrographs. Biochemical characterization of these structures has shown that there are two different kinds of spikes on the surfaces of virions. One spike structure serves to attach the virus to the surfaces of the cells and is composed of a protein termed the hemagglutinin-neuraminidase (HN) in the case of the Paramyxovirus genus, the hemagglutinin (H) in the case of Morbillivirus, and the G protein in the case of Pneumovirus. As reflected in the nomenclature, the attachment protein of Paramyxovirus also contains a neuraminidase activity not demonstrated for the attachment proteins of the other genera (Scheid et al., 1972). The other spike is composed of the fusion protein and mediates the fusion of the viral membrane with that of the host cell, a step essential to the penetration and uncoating of the viral genetic information (Scheid and Choppin, 1974, 1977). This protein also mediates fusion between an infected cell and an adjacent cell, termed syncytium formation, a property that facilitates cell-to-cell spread of the viral genetic information.

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Authors and Affiliations

  1. Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, Massachusetts, 01655, USA

    Trudy Morrison

  2. Department of Virology and Molecular Biology, St. Jude Children’s Research Hospital, Memphis, Tennessee, 38101-0318, USA

    Allen Portner

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  1. Trudy Morrison
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  1. Howard Hughes Medical Institute, Bethesda, Maryland, USA

    David W. Kingsbury

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Morrison, T., Portner, A. (1991). Structure, Function, and Intracellular Processing of the Glycoproteins of Paramyxoviridae . In: Kingsbury, D.W. (eds) The Paramyxoviruses. The Viruses. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3790-8_13

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