Neuraminidase

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Template:STRUCTURE 3nss

Contents 1 Function 2 Relevance 3 3D structures of Neuraminidase 4 References

Function

Neuraminidase (NAN) cleaves the glycosidic bonds of neuraminic acid^[1].

• 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].
  

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^[4]. 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^[5].

3D structures of Neuraminidase

Updated on 08-May-2016

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. ↑ 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
5. ↑ 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