Function
Neuraminidase or sialidase (NAN) is a viral neuraminidase which cleaves the glycosidic bonds of neuraminic acid[1]. The non-viral neuraminidase is called Sialidase.
- endo-neuraminidase is a phage neuraminidase which cleaves α-2,8-polysialic acid[2].
- Pseudaminidase is a Pseudomonas aeruginosa neuraminidase.
- Trans-sialidase transfers sialic acid from Trypanosoma cruzi to a host cell[3]. This enzyme is a modified sialidase which has transglycosidase activity and transfers sialic acid from host glycoconjugates to β-galactose on a parasite surface[4].
- Anhydrosialidase catalyzes the elimination of sialyl group in N-acetylneuraminic acid glycosides to yield 2,7-anhydro-α-N-acetylneuraminate[5].
See also
For other inhibitors see
Relevance
The viral NAN is a drug target for prevention of influenza[6]. In Chagas disease trans-sialidase on the surface of Trypanosoma cruzi participate in host-parasite interactions and mediate the initial stages of the invasion of the host cell[7].
Structural highlights
The biological assembly of H5N1 avian influenza virus neuraminidase is homotetramer. The active site of NAN contains the influenza drug Tamiflu[8].
3D structures of Neuraminidase
Neuraminidase 3D structures
- ↑ Matrosovich MN, Matrosovich TY, Gray T, Roberts NA, Klenk HD. Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium. J Virol. 2004 Nov;78(22):12665-7. PMID:15507653 doi:https://dx.doi.org/10.1128/JVI.78.22.12665-12667.2004
- ↑ Rutishauser U, Watanabe M, Silver J, Troy FA, Vimr ER. Specific alteration of NCAM-mediated cell adhesion by an endoneuraminidase. J Cell Biol. 1985 Nov;101(5 Pt 1):1842-9. PMID:4055897
- ↑ Colli W. Trans-sialidase: a unique enzyme activity discovered in the protozoan Trypanosoma cruzi. FASEB J. 1993 Oct;7(13):1257-64. PMID:8405811
- ↑ Paris G, Ratier L, Amaya MF, Nguyen T, Alzari PM, Frasch AC. A sialidase mutant displaying trans-sialidase activity. J Mol Biol. 2005 Jan 28;345(4):923-34. PMID:15588836 doi:10.1016/j.jmb.2004.09.031
- ↑ Li YT, Nakagawa H, Ross SA, Hansson GC, Li SC. A novel sialidase which releases 2,7-anhydro-alpha-N-acetylneuraminic acid from sialoglycoconjugates. J Biol Chem. 1990 Dec 15;265(35):21629-33. PMID:2254319
- ↑ Sylte MJ, Suarez DL. Influenza neuraminidase as a vaccine antigen. Curr Top Microbiol Immunol. 2009;333:227-41. doi: 10.1007/978-3-540-92165-3_12. PMID:19768409 doi:https://dx.doi.org/10.1007/978-3-540-92165-3_12
- ↑ Schenkman S, Eichinger D, Pereira ME, Nussenzweig V. Structural and functional properties of Trypanosoma trans-sialidase. Annu Rev Microbiol. 1994;48:499-523. PMID:7826016 doi:https://dx.doi.org/10.1146/annurev.mi.48.100194.002435
- ↑ Russell RJ, Haire LF, Stevens DJ, Collins PJ, Lin YP, Blackburn GM, Hay AJ, Gamblin SJ, Skehel JJ. The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design. Nature. 2006 Sep 7;443(7107):45-9. Epub 2006 Aug 16. PMID:16915235 doi:https://dx.doi.org/10.1038/nature05114
