Neuraminidase
From Proteopedia
(Difference between revisions)
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{{STRUCTURE_3nss| PDB=3nss | SIZE=350| SCENE= |right|CAPTION=Glycosylated Influenza virus neuraminidase complex with Ca+2 (green) and acetate, [[3nss]] }} | {{STRUCTURE_3nss| PDB=3nss | SIZE=350| SCENE= |right|CAPTION=Glycosylated Influenza virus neuraminidase complex with Ca+2 (green) and acetate, [[3nss]] }} | ||
- | + | == Function == | |
- | '''Neuraminidase''' (NAN) cleaves the glycosidic bonds of neuraminic acid. | + | '''Neuraminidase''' (NAN) cleaves the glycosidic bonds of neuraminic acid<ref>PMID:15507653</ref>. <br /> |
+ | *'''endo-neuraminidase''' is a phage neuraminidase which cleaves α-2,8-polysialic acid<ref>PMID:4055897</ref>. <br /> | ||
+ | *'''Pseudaminidase''' is a ''Pseudomonas aeruginosa'' neuraminidase. <br /> | ||
+ | *'''Trans-sialidase''' transfers sialic acid from ''Trypanosoma cruzi'' to a host cell<ref>PMID:8405811</ref>. <br /> | ||
See also<br /> | See also<br /> | ||
*[[Avian Influenza Neuraminidase, Tamiflu and Relenza]]<br /> | *[[Avian Influenza Neuraminidase, Tamiflu and Relenza]]<br /> | ||
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*[[Carbohydrate binding domain from Streptococcus pneumoniae NanA sialidase complexed with 3'-sialyllactose]]<br /> | *[[Carbohydrate binding domain from Streptococcus pneumoniae NanA sialidase complexed with 3'-sialyllactose]]<br /> | ||
*[[Treatments:Neuraminidase Inhibitor Pharmacokinetics References]]<br />. | *[[Treatments:Neuraminidase Inhibitor Pharmacokinetics References]]<br />. | ||
+ | |||
+ | == Relevance == | ||
+ | The viral NAN is a drug target for prevention of influenza<ref>PMID:19768409</ref>. 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<ref>PMID:7826016</ref>. | ||
==3D structures of Neuraminidase== | ==3D structures of Neuraminidase== | ||
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}} | }} | ||
+ | == References == | ||
+ | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Revision as of 09:32, 8 May 2016
Contents |
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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
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