View source for 7uvq


==Pfs230 domain 1 bound by RUPA-97 and 15C5 Fabs==
<StructureSection load='7uvq' size='340' side='right'caption='[[7uvq]], [[Resolution|resolution]] 3.29&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7uvq]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UVQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UVQ 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]] 3.29&#8491;</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=7uvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uvq OCA], [https://pdbe.org/7uvq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uvq RCSB], [https://www.ebi.ac.uk/pdbsum/7uvq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uvq ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pfs230 is essential for Plasmodium falciparum transmission to mosquitoes and is the protein targeted by the most advanced malaria-transmission-blocking vaccine candidate. Prior understanding of functional epitopes on Pfs230 is based on two monoclonal antibodies (mAbs) with moderate transmission-reducing activity (TRA), elicited from subunit immunization. Here, we screened the B cell repertoire of two naturally exposed individuals possessing serum TRA and identified five potent mAbs from sixteen Pfs230 domain-1-specific mAbs. Structures of three potent and three low-activity antibodies bound to Pfs230 domain 1 revealed four distinct epitopes. Highly potent mAbs from natural infection recognized a common conformational epitope that is highly conserved across P. falciparum field isolates, while antibodies with negligible TRA derived from natural infection or immunization recognized three distinct sites. Our study provides molecular blueprints describing P. falciparum TRA, informed by contrasting potent and non-functional epitopes elicited by natural exposure and vaccination.

Potent transmission-blocking monoclonal antibodies from naturally exposed individuals target a conserved epitope on Plasmodium falciparum Pfs230.,Ivanochko D, Fabra-Garcia A, Teelen K, van de Vegte-Bolmer M, van Gemert GJ, Newton J, Semesi A, de Bruijni M, Bolscher J, Ramjith J, Szabat M, Vogt S, Kraft L, Duncan S, Lee SM, Kamya MR, Feeney ME, Jagannathan P, Greenhouse B, Sauerwein RW, Richter King C, MacGill RS, Bousema T, Jore MM, Julien JP Immunity. 2023 Feb 14;56(2):420-432.e7. doi: 10.1016/j.immuni.2023.01.013. PMID:36792575<ref>PMID:36792575</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7uvq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Plasmodium falciparum]]
[[Category: Ivanochko D]]
[[Category: Julien JP]]