Neuraminidase

From Proteopedia

spinqualitylabelsall models H5N1 avian influenza virus neuraminidase complex with Tamiflu (PDB entry 2ht7) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Relevance 3 Structural highlights 4 3D structures of Neuraminidase 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]. For Sialidase see Sialidase. See also Avian Influenza Neuraminidase, Tamiflu and Relenza Zanamivir (Relenza) Molecular Playground/Relenza Molecular Playground/Tamiflu Oseltamivir (Tamiflu) Treatments:Influenza User:Michael Strong/H1N1/NA for Influenza virus neuraminidase User:Michael Strong/H1N1/NA/MSA for multiple sequence alignment. For other inhibitors see Neuraminidase Inhibitor Pharmacokinetics Carbohydrate binding domain from Streptococcus pneumoniae NanA sialidase complexed with 3'-sialyllactose Treatments:Neuraminidase Inhibitor Pharmacokinetics References . Relevance The viral NAN is a drug target for prevention of influenza[5]. 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[6]. Structural highlights The biological assembly of H5N1 avian influenza virus neuraminidase is . The [7]. 3D structures of Neuraminidase Neuraminidase 3D structures

References

1. ↑ 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:http://dx.doi.org/10.1128/JVI.78.22.12665-12667.2004
2. ↑ 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
3. ↑ Colli W. Trans-sialidase: a unique enzyme activity discovered in the protozoan Trypanosoma cruzi. FASEB J. 1993 Oct;7(13):1257-64. PMID:8405811
4. ↑ 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
5. ↑ 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:http://dx.doi.org/10.1007/978-3-540-92165-3_12
6. ↑ 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:http://dx.doi.org/10.1146/annurev.mi.48.100194.002435
7. ↑ 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:http://dx.doi.org/10.1038/nature05114