8e6k
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8e6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8e6k OCA], [https://pdbe.org/8e6k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8e6k RCSB], [https://www.ebi.ac.uk/pdbsum/8e6k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8e6k ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8e6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8e6k OCA], [https://pdbe.org/8e6k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8e6k RCSB], [https://www.ebi.ac.uk/pdbsum/8e6k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8e6k ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == Function == | ||
| - | [https://www.uniprot.org/uniprot/NRAM_I18A0 NRAM_I18A0] Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication (By similarity). Unlike other strains, A/WSN/33 neuraminidase binds and activates plasminogen into plasmin in the vicinity of HA so that activated plasmin cleaves HA rendering the virus infectious (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Neuraminidase (NA) is one of the two influenza virus surface glycoproteins, and antibodies that target it are an independent correlate of protection. However, our current understanding of NA antigenicity is incomplete. Here, we describe human monoclonal antibodies (mAbs) from a patient with a pandemic H1N1 virus infection in 2009. Two mAbs exhibited broad reactivity and inhibited NA enzyme activity of seasonal H1N1 viruses circulating before and after 2009, as well as viruses with avian or swine N1s. The mAbs provided robust protection from lethal challenge with human H1N1 and avian H5N1 viruses in mice, and both target an epitope on the lateral face of NA. In summary, we identified two broadly protective NA antibodies that share a novel epitope, inhibited NA activity, and provide protection against virus challenge in mice. Our work reaffirms that NA should be included as a target in future broadly protective or universal influenza virus vaccines. | Neuraminidase (NA) is one of the two influenza virus surface glycoproteins, and antibodies that target it are an independent correlate of protection. However, our current understanding of NA antigenicity is incomplete. Here, we describe human monoclonal antibodies (mAbs) from a patient with a pandemic H1N1 virus infection in 2009. Two mAbs exhibited broad reactivity and inhibited NA enzyme activity of seasonal H1N1 viruses circulating before and after 2009, as well as viruses with avian or swine N1s. The mAbs provided robust protection from lethal challenge with human H1N1 and avian H5N1 viruses in mice, and both target an epitope on the lateral face of NA. In summary, we identified two broadly protective NA antibodies that share a novel epitope, inhibited NA activity, and provide protection against virus challenge in mice. Our work reaffirms that NA should be included as a target in future broadly protective or universal influenza virus vaccines. | ||
| - | Human anti-N1 monoclonal antibodies elicited by pandemic H1N1 virus infection broadly inhibit HxN1 viruses in vitro and in vivo.,Hansen L, McMahon M, Turner HL, Zhu X, Turner JS, Ozorowski G, Stadlbauer D, Vahokoski J, Schmitz AJ, Rizk AA, Alsoussi WB, Strohmeier S, Yu W, Choreno-Parra JA, Jimenez-Alvarez L, Cruz-Lagunas A, Zuniga J, Mudd PA, Cox RJ, Wilson IA, Ward AB, Ellebedy AH, Krammer F Immunity. 2023 | + | Human anti-N1 monoclonal antibodies elicited by pandemic H1N1 virus infection broadly inhibit HxN1 viruses in vitro and in vivo.,Hansen L, McMahon M, Turner HL, Zhu X, Turner JS, Ozorowski G, Stadlbauer D, Vahokoski J, Schmitz AJ, Rizk AA, Alsoussi WB, Strohmeier S, Yu W, Choreno-Parra JA, Jimenez-Alvarez L, Cruz-Lagunas A, Zuniga J, Mudd PA, Cox RJ, Wilson IA, Ward AB, Ellebedy AH, Krammer F Immunity. 2023 Aug 8;56(8):1927-1938.e8. doi: 10.1016/j.immuni.2023.07.004. Epub , 2023 Jul 27. PMID:37506693<ref>PMID:37506693</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Current revision
2H08 Fab in complex with influenza virus neuraminidase from A/Brevig Mission/1/1918 (H1N1)
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