View source for 5nqy


==Structure of a fHbp(V1.4):PorA(P1.16) chimera. Fusion at fHbp position 309.==
<StructureSection load='5nqy' size='340' side='right'caption='[[5nqy]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5nqy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis] and [https://en.wikipedia.org/wiki/Neisseria_meningitidis_serogroup_C Neisseria meningitidis serogroup C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NQY 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]] 2.6&#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=5nqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nqy OCA], [https://pdbe.org/5nqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nqy RCSB], [https://www.ebi.ac.uk/pdbsum/5nqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nqy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6VS06_NEIME Q6VS06_NEIME] [https://www.uniprot.org/uniprot/OMPA1_NEIMC OMPA1_NEIMC] Serves as a slightly cation selective porin. Major antigen on the gonococcal cell surface and it may have pathogenic properties in addition to its porin activity.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
There is an urgent need to develop vaccines against pathogenic bacteria. However, this is often hindered by antigenic diversity and difficulties encountered manufacturing membrane proteins. Here we show how to use structure-based design to develop chimeric antigens (ChAs) for subunit vaccines. ChAs are generated against serogroup B Neisseria meningitidis (MenB), the predominant cause of meningococcal disease in wealthy countries. MenB ChAs exploit factor H binding protein (fHbp) as a molecular scaffold to display the immunogenic VR2 epitope from the integral membrane protein PorA. Structural analyses demonstrate fHbp is correctly folded and the PorA VR2 epitope adopts an immunogenic conformation. In mice, immunisation with ChAs generates fHbp and PorA antibodies that recognise the antigens expressed by clinical MenB isolates; these antibody responses correlate with protection against meningococcal disease. Application of ChAs is therefore a potentially powerful approach to develop multivalent subunit vaccines, which can be tailored to circumvent pathogen diversity.

Structure-based design of chimeric antigens for multivalent protein vaccines.,Hollingshead S, Jongerius I, Exley RM, Johnson S, Lea SM, Tang CM Nat Commun. 2018 Mar 13;9(1):1051. doi: 10.1038/s41467-018-03146-7. PMID:29535307<ref>PMID:29535307</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5nqy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Neisseria meningitidis]]
[[Category: Neisseria meningitidis serogroup C]]
[[Category: Hollingshead S]]
[[Category: Johnson S]]
[[Category: Lea SM]]
[[Category: Tang CM]]