View source for 9ish


==Crystal structure of nanobody 32 in complex with HSV-2 gD==
<StructureSection load='9ish' size='340' side='right'caption='[[9ish]], [[Resolution|resolution]] 2.88&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9ish]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_2 Human alphaherpesvirus 2] and [https://en.wikipedia.org/wiki/Vicugna_pacos Vicugna pacos]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9ISH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9ISH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.88&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=9ish FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ish OCA], [https://pdbe.org/9ish PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ish RCSB], [https://www.ebi.ac.uk/pdbsum/9ish PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ish ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1W6QD44_HHV2 A0A1W6QD44_HHV2] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Herpes simplex virus (HSV) causes significant health burden worldwide. Currently used antiviral drugs are effective but resistance can occur. Here, we report two high-affinity neutralizing nanobodies, namely Nb14 and Nb32, that target non-overlapping epitopes in HSV gD. Nb14 binds a neutralization epitope located in the N-A' interloop, which prevents the interaction between gD and gH/gL during the second step of conformational changes during membrane fusion after virus attachment. The bispecific nanobody dimer (Nb14-32-Fc) exhibits high potency in vitro and in vivo. Mechanistically, Nb14-32-Fc neutralizes HSVs at both the pre-and post-attachment stages and prevents cell-to-cell spread in vitro. Administration of Nb14-32-Fc at low dosage of 1 mg/kg provides 100% protection in an HSV-1 infection male mouse model and an HSV-2 infection female mouse model. Our results demonstrate that Nb14-32-Fc could serve as a promising drug candidate for treatment of HSV infection, especially in the cases of antiviral drug resistance and severe herpes encephalitis.

A potent protective bispecific nanobody targeting Herpes simplex virus gD reveals vulnerable epitope for neutralizing.,Hu J, Tan H, Wang M, Deng S, Liu M, Zheng P, Wang A, Guo M, Wang J, Li J, Qiu H, Yao C, Zhu Z, Hasi C, Pan D, He H, Huang C, Shang Y, Zhu S, Jin T Nat Commun. 2025 May 6;16(1):4196. doi: 10.1038/s41467-025-58669-7. PMID:40328740<ref>PMID:40328740</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9ish" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human alphaherpesvirus 2]]
[[Category: Large Structures]]
[[Category: Vicugna pacos]]
[[Category: Hu J]]
[[Category: Jin TC]]