Influenza: A case study
Influenza: A case study

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Influenza: A case study

2.1 Structure of influenza

The structure of influenza A is shown schematically in Figure 4. The viral genomic RNA, which consists of eight separate strands (see Section 2.3), is enclosed by its associated nucleoproteins to make a ribonucleoprotein complex (RNP), and this is contained in the central core of the virus (the capsid).

The nucleoproteins are required for viral replication and packing of the genome into the new capsid, which is formed by M1-protein (or matrix protein). The M1-protein is the most abundant component of the virus, constituting about 40% of the viral mass; it is essential for the structural integrity of the virus and to control assembly of the virus.

Influenza virus structure.
Figure 4 Structure of an influenza A virus. The capsid, formed by M1-protein, also contains the viral genome and a number of enzymes required for viral replication. The viral envelope is a lipid bilayer formed from the plasma membrane of the host cell, which contains two virus-encoded proteins, haemagglutinin and neuraminidase.

Orthomyxoviruses have a capsid surrounded by a phospholipid bilayer derived from the plasma membrane of the cell that produced the virus. This layer is shown in Figure 4 as the virus’s envelope.

Two proteins, haemagglutinin and neuraminidase, are found on the viral envelope. These proteins are encoded by the viral HA and NA genes (Section 2.3), respectively and are inserted into the plasma membrane of the infected cell before the newly-produced viruses bud off from the cell surface.

The haemagglutinin can bind to glycophorin, a type of polysaccharide that contains sialic acid residues, and which is present on the surface of a variety of host cells. The virus uses the haemagglutinin to attach to the host cells that it will infect. Antibodies and drugs against haemagglutinin are therefore particularly important in limiting the spread of the virus, since they prevent it from attaching to new host cells.

Neuraminidase is an enzyme that cleaves sialic acid residues from polysaccharides. It has a role in clearing a path to the surface of the target cell before infection, namely, digesting the components of mucus surrounding epithelial cells in the respiratory system. Similarly, neuraminidase also promotes release of the budding virus from the cell surface after infection.

The structures of influenza B and influenza C are broadly similar to that of Type A, although in influenza C the functions of the haemagglutinin and the neuraminidase are combined in a single molecule, haemagglutinin esterase. This molecule binds and cleaves a less common type of sialic acid. Influenza C does not normally cause clinical disease or epidemics, so the following discussion is confined to influenza A and B.


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