6tou: Difference between revisions

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== Function ==

[https://www.uniprot.org/uniprot/Q8JUA9_9RHAB Q8JUA9_9RHAB]

== Publication Abstract from PubMed ==

Rabies virus (RABV) causes fatal encephalitis in more than 59,000 people yearly. Upon the bite of an infected animal, the development of clinical disease can be prevented with post-exposure prophylaxis (PEP), which includes the administration of Rabies immunoglobulin (RIG). However, the high cost and limited availability of serum-derived RIG severely hamper its wide use in resource-limited countries. A safe low-cost alternative is provided by using broadly neutralizing monoclonal antibodies (bnAbs). Here we report the X-ray structure of one of the most potent and most broadly reactive human bnAbs, RVC20, in complex with its target domain III of the RABV glycoprotein (G). The structure reveals that the RVC20 binding determinants reside in a highly conserved surface of G, rationalizing its broad reactivity. We further show that RVC20 blocks the acid-induced conformational change required for membrane fusion. Our results may guide the future development of direct antiviral small molecules for Rabies treatment.

Structure of the prefusion-locking broadly neutralizing antibody RVC20 bound to the rabies virus glycoprotein.,Hellert J, Buchrieser J, Larrous F, Minola A, de Melo GD, Soriaga L, England P, Haouz A, Telenti A, Schwartz O, Corti D, Bourhy H, Rey FA Nat Commun. 2020 Jan 30;11(1):596. doi: 10.1038/s41467-020-14398-7. PMID:32001700<ref>PMID:32001700</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

==See Also==

*[[Antibody 3D structures|Antibody 3D structures]]

*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]

== References ==

__TOC__

</StructureSection>

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@@ Line 10: / Line 10: @@
 == Function ==
 [https://www.uniprot.org/uniprot/Q8JUA9_9RHAB Q8JUA9_9RHAB]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Rabies virus (RABV) causes fatal encephalitis in more than 59,000 people yearly. Upon the bite of an infected animal, the development of clinical disease can be prevented with post-exposure prophylaxis (PEP), which includes the administration of Rabies immunoglobulin (RIG). However, the high cost and limited availability of serum-derived RIG severely hamper its wide use in resource-limited countries. A safe low-cost alternative is provided by using broadly neutralizing monoclonal antibodies (bnAbs). Here we report the X-ray structure of one of the most potent and most broadly reactive human bnAbs, RVC20, in complex with its target domain III of the RABV glycoprotein (G). The structure reveals that the RVC20 binding determinants reside in a highly conserved surface of G, rationalizing its broad reactivity. We further show that RVC20 blocks the acid-induced conformational change required for membrane fusion. Our results may guide the future development of direct antiviral small molecules for Rabies treatment.
+Structure of the prefusion-locking broadly neutralizing antibody RVC20 bound to the rabies virus glycoprotein.,Hellert J, Buchrieser J, Larrous F, Minola A, de Melo GD, Soriaga L, England P, Haouz A, Telenti A, Schwartz O, Corti D, Bourhy H, Rey FA Nat Commun. 2020 Jan 30;11(1):596. doi: 10.1038/s41467-020-14398-7. PMID:32001700<ref>PMID:32001700</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 6tou" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Antibody 3D structures|Antibody 3D structures]]
 *[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>