5nqx: Difference between revisions
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==Structure of a fHbp(V1.1):PorA(P1.16) chimera. Fusion at fHbp position 294.== | ==Structure of a fHbp(V1.1):PorA(P1.16) chimera. Fusion at fHbp position 294.== | ||
<StructureSection load='5nqx' size='340' side='right' caption='[[5nqx]], [[Resolution|resolution]] 3.66Å' scene=''> | <StructureSection load='5nqx' size='340' side='right'caption='[[5nqx]], [[Resolution|resolution]] 3.66Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5nqx]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NQX OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5nqx]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_MC58 Neisseria meningitidis MC58] 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=5NQX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NQX FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.66Å</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=5nqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nqx OCA], [https://pdbe.org/5nqx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nqx RCSB], [https://www.ebi.ac.uk/pdbsum/5nqx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nqx ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[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.[https://www.uniprot.org/uniprot/FHBP_NEIMB FHBP_NEIMB] A bacterial surface lipoprotein that binds host (human) complement factor H (fH, gene CFH), binding contributes to the avoidance of complement-mediated lysis by N.meningitidis. Binding of fH to the bacteria surface is independent of bacterial sialic acid moieties (PubMed:16751403). fH binding affinity is high enough that it may sequester plasma fH, depleting its circulating levels and de-regulating complement in the host (Probable). This protein induces high levels of bactericidal antibodies in mice (PubMed:12642606, PubMed:15039331, PubMed:15664958, PubMed:21753121, PubMed:23133374).<ref>PMID:12642606</ref> <ref>PMID:15039331</ref> <ref>PMID:15664958</ref> <ref>PMID:16751403</ref> <ref>PMID:21753121</ref> <ref>PMID:23133374</ref> <ref>PMID:19225461</ref> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5nqx" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Neisseria meningitidis MC58]] | |||
[[Category: | [[Category: Neisseria meningitidis serogroup C]] | ||
[[Category: | [[Category: Johnson S]] | ||
[[Category: | [[Category: Jongerius I]] | ||
[[Category: | [[Category: Lea SM]] | ||
[[Category: | [[Category: Tang CM]] | ||
[[Category: | |||