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On The Role of Viral Envelope Proteins in Pathogenesis

  • Chapter
Mechanisms of Viral Pathogenesis

Part of the book series: Developments in Molecular Virology ((DMVI,volume 3))

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Summary

The paramyxovirus envelope contains two surface glycoproteins (HN and F) and an internal non-glycosylated protein (M). The F protein is involved in viral pathogenesis in three different ways, each related to its ability to cause membrane fusion, which mediates virus penetration, cell fusion, and hemolysis. 1. Membrane fusion is activated by a specific proteolytic cleavage yielding two polypeptides (F1 and F2), and because this is accomplished by a host enzyme, the tropism and virulence of the virus is significantly determined by the F protein and its susceptibility to cleavage by a protease available in the host tissue. 2. In some virus- cell systems cell death has been shown to be due to the membrane-damaging effects of the F protein. 3. Lack of antibodies to F has been implicated in an immune pathological response in patients receiving formalin-inactivated measles virus vaccine. The membrane fusion reaction has been characterized using intact cells and liposomes as target membranes, and both intact virus and membranes reconstituted with purified F protein as the fusogenic agents. Requirements for fusion have been determined, including a conformational change in the F protein upon cleavage, the lipid composition of the target membrane, and the effect of pH. Extensive evidence has been obtained indicating that the N-terminus on F generated by the activating cleavage is involved in membrane fusion reaction, probably through a hydrophobic interaction with the target membrane. Synthetic oligopeptides with sequences that mimic this N-terminal region specifically inhibit membrane fusion, and thereby virus infectivity at the level of penetration. The oligopeptides have been found to act at the cell membrane, presumably competing with the F1 polypeptide for sites on the cell membrane.

Lack of the expression of the M protein of measles virus is involved in the persistent leading to the chronic neurological disease subacute scelorosing panencephalitis (SSPE), and evidence has been obtained which suggests that there is a host restriction in the expression of this protein in brain cells. In vitro studies have provided structural evidence supporting the role of the M protein in virus assembly at the cell membrane.

A new protein has been identified in cells infected with influenza B of a protein unique for influenza B. The protein (NB) is glycosylated and is encoded in the same viral genome RNA segment as the viral neuraminidase (NA). A single mRNA codes for both proteins, with NB translated from the first initiation codon and NA translated from the second.

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  1. The Rockefeller University, New York, New York, 10021, USA

    Purnell W. Choppin

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  1. Israel Institute for Biological Research, Ness-Ziona, Israel

    A. Kohn  & P. Fuchs  & 

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© 1984 Martinus Nijhoff Publishing, Boston

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Choppin, P.W. (1984). On The Role of Viral Envelope Proteins in Pathogenesis. In: Kohn, A., Fuchs, P. (eds) Mechanisms of Viral Pathogenesis. Developments in Molecular Virology, vol 3. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-3894-9_19

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  • DOI: https://doi.org/10.1007/978-1-4613-3894-9_19

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