8ib1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:43, 17 October 2024) (edit) (undo)
 
Line 7: Line 7:
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8ib1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ib1 OCA], [https://pdbe.org/8ib1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ib1 RCSB], [https://www.ebi.ac.uk/pdbsum/8ib1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ib1 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=8ib1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ib1 OCA], [https://pdbe.org/8ib1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ib1 RCSB], [https://www.ebi.ac.uk/pdbsum/8ib1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ib1 ProSAT]</span></td></tr>
</table>
</table>
-
== Function ==
+
<div style="background-color:#fffaf0;">
-
[https://www.uniprot.org/uniprot/HEMA_I89A7 HEMA_I89A7] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore (By similarity).
+
== Publication Abstract from PubMed ==
 +
Plasticity of influenza virus hemagglutinin (HA) conformation increases an opportunity to generate conserved non-native epitopes with unknown functionality. Here, we have performed an in-depth analysis of human monoclonal antibodies against a stem-helix region that is occluded in native prefusion yet exposed in postfusion HA. A stem-helix antibody, LAH31, provided IgG Fc-dependent cross-group protection by targeting a stem-helix kinked loop epitope, with a unique structure emerging in the postfusion state. The structural analysis and molecular modeling revealed key contact sites responsible for the epitope specificity and cross-group breadth that relies on somatically mutated light chain. LAH31 was inaccessible to the native prefusion HA expressed on cell surface; however, it bound to the HA structure present on infected cells with functional linkage to the Fc-mediated clearance. Our study uncovers a novel non-native epitope that emerges in the postfusion HA state, highlighting the utility of this epitope for a broadly protective antigen design.
 +
 
 +
Structural basis for cross-group recognition of an influenza virus hemagglutinin antibody that targets postfusion stabilized epitope.,Tonouchi K, Adachi Y, Suzuki T, Kuroda D, Nishiyama A, Yumoto K, Takeyama H, Suzuki T, Hashiguchi T, Takahashi Y PLoS Pathog. 2023 Aug 9;19(8):e1011554. doi: 10.1371/journal.ppat.1011554. , eCollection 2023 Aug. PMID:37556494<ref>PMID:37556494</ref>
 +
 
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 8ib1" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Structure of the LAH31 Fab bound to an influenza virus HA epitope peptide

PDB ID 8ib1

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/8ib1"
Personal tools