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تسجيل

Structure and Function of Neuraminidase

المؤلف:  Stefan Riedel, Jeffery A. Hobden, Steve Miller, Stephen A. Morse, Timothy A. Mietzner, Barbara Detrick, Thomas G. Mitchell, Judy A. Sakanari, Peter Hotez, Rojelio Mejia

المصدر:  Jawetz, Melnick, & Adelberg’s Medical Microbiology

الجزء والصفحة:  28e , p583-584

2025-12-27

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The antigenicity of NA, the other glycoprotein on the surface of influenza virus particles, is also important in determining the subtype of influenza virus isolates.

The NA spike on the virus particle is a tetramer com posed of four identical monomers (Figure 1D). A slender stalk is topped with a box-shaped head. There is a catalytic site for NA on the top of each head, so that each NA spike contains four active sites.

Fig1. Influenza virus hemagglutinin (HA) and neuraminidase (NA) surface glycoproteins. A: Primary structures of HA and NA polypeptides. The cleavage of HA into HA1 and HA2 is necessary for virus to be infectious. HA1 and HA2 remain linked by a disulfide bond (S–S). No posttranslational cleavage occurs with NA. Carbohydrate attachment sites • are shown. The hydrophobic amino acids that anchor the proteins in the viral membrane are located near the carboxyl terminal of HA and the amino terminal of NA. B: Folding of the HA1 and HA2 polypeptides in an HA monomer. Five major antigenic sites (sites A–E) that undergo change are shown as shaded areas. The amino terminal of HA2 provides fusion activity (fusion peptide). The fusion particle is buried in the molecule until it is exposed by a conformational change induced by a low pH. C: Structure of the HA trimer as it occurs on a virus particle or the surface of infected cells. Some of the sites involved in antigenic variation are shown (A). Carboxyl terminal residues (C) protrude through the membrane. D: Structure of the NA tetramer. Each NA molecule has an active site on its upper surface. The amino terminal region (N) of the polypeptides anchors the complex in the membrane. (Redrawn with permission from [A, B] Murphy BR, Webster RG: Influenza viruses, pp. 1185 and 1186, and [C, D] Kingsbury DW: Orthomyxo-and paramyxoviruses and their replication, pp. 1163 and 1172. In Fields BN [editor-in-chief] Virology. Raven Press, 1985.)

The NA functions at the end of the viral replication cycle. It is a sialidase enzyme that removes sialic acid from glycoconjugates. It facilitates release of virus particles from infected cell surfaces during the budding process and helps prevent self-aggregation of virions by removing sialic acid residues from viral glycoproteins. It is possible that NA helps the virus negotiate through the mucin layer in the respiratory tract to reach the target epithelial cells.