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Review
. 2016 Jul;26(4):242-50.
doi: 10.1002/rmv.1879. Epub 2016 Apr 8.

A new role of neuraminidase (NA) in the influenza virus life cycle: implication for developing NA inhibitors with novel mechanism of action

Jie Yang  1   2 , Shuwen Liu  1 , Lanying Du  2 , Shibo Jiang  3   2
Affiliations
Review

A new role of neuraminidase (NA) in the influenza virus life cycle: implication for developing NA inhibitors with novel mechanism of action

Jie Yang et al. Rev Med Virol. 2016 Jul.

Abstract

The entire life cycle of influenza virus involves viral attachment, entry, replication, and release. Previous studies have demonstrated that neuraminidase (NA) is an essential glycoprotein on the surface of influenza virus and that it is responsible for release of progeny virions from the host cell to infect new cells. However, recent studies have also suggested that NA may play other roles in the early stages of the viral life cycle, that is, viral attachment and entry. This review focuses on the new role of NA in the early stages of influenza life cycle and the corresponding development of novel NA inhibitors. Copyright © 2016 John Wiley & Sons, Ltd.

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Conflict of interest statement

The authors have no competing interest.

Figures

Figure 1
Figure 1
The life cycle of an influenza A virus (IAV). (A) IAV binds to target cells through the interaction between sialylated receptors and HA or NA. (B) IAV envelope fuses with endosomal membrane under low pH, releasing viral genetic materials into cytosol. (C) Viral replication occurs in nucleus and Golgi apparatus. (D) Progeny virions are assembled, budded, and released from the infected host cell to infect neighbor cells
Figure 2
Figure 2
The roles of NA in the early and late stages of influenza A virus life cycle. (A) NA mediates attachment of the virus to receptors on host cells to facilitate viral entry. (B) NA mediates cleavage of sialic acid from receptors on host cells to allow release of progeny virions to infect neighbor cells
Figure 3
Figure 3
Chemical structures of four NA inhibitors currently used in clinics to treat influenza virus infection
Figure 4
Figure 4
Schematic representation of the structure of the complex between NA of influenza virus and sialic acid receptor (PDB code 2BAT). (A) Wild‐type NA protein in complex with sialic acid. The side chain of conserved catalytic sites of NA (R118, D151, R152, R224, E276, R292, R371, and Y406) was shown as green sticks. Location of residue 151 and the 150 loop was shown in marine. Sialic acid was shown as yellow sticks. The hydrogen bond was represented as red dot line (highlighted in red circle). (B) NA protein with D151G mutation in complex with sialic acid. All colors remain the same as shown in panel (A)
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