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The Unusual Attachment Glycoprotein of the Respiratory Syncytial Viruses

Structure, Maturation, and Role in Immunity

  • Chapter
The Paramyxoviruses

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

Abstract

Human respiratory syncytial (RS) virus, a pneumovirus in the paramyxovirus family, differs from other members of this family in several ways: (1) it has additional genes, which include two independent genes for nonstructural proteins and a gene for a second matrixlike protein, (2) the organization of the genome differs from that of other paramyxoviruses, and (3) the major glycoprotein, G, is unique among paramyxovirus proteins (Collins and Wertz, 1986; Wertz et al., 1985; see also Chapter 4). The G protein is characterized as the attachment protein of RS virus (Levine et al., 1987). However, whereas the attachment proteins of the other paramyxoviruses possess hemagglutinin (HA) or hemagglutinin-neuraminidase (HN) activities, respectively, the G protein of RS virus lacks such activities (Richman et al., 1971). Furthermore, analysis of the sequence of the G gene shows no similarity between the G protein of RS virus and the attachment proteins of the other paramyxoviruses, or indeed with any known RNA virus protein described to date (Wertz et al., 1985). Instead, the structural features of G resemble those of a class of cellular proteins called the mucinous proteins. The purpose of this chapter is to describe the structure and function of the G protein and to discuss its role in infection and immunity to RS virus disease (see also Chapters 18 and 19).

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  1. Department of Microbiology, University of Alabama School of Medicine, Birmingham, Alabama, 35294, USA

    Wayne M. Sullender & Gail W. Wertz

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  1. Wayne M. Sullender
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  1. Howard Hughes Medical Institute, Bethesda, Maryland, USA

    David W. Kingsbury

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Sullender, W.M., Wertz, G.W. (1991). The Unusual Attachment Glycoprotein of the Respiratory Syncytial Viruses. In: Kingsbury, D.W. (eds) The Paramyxoviruses. The Viruses. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3790-8_14

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  • DOI: https://doi.org/10.1007/978-1-4615-3790-8_14

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