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5nqp

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Current revision

Structure of a fHbp(V1.4):PorA(P1.16) chimera. Fusion at fHbp position 151.

Structural highlights

5nqp is a 3 chain structure with sequence from Neisseria meningitidis and Neisseria meningitidis serogroup C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.86Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q6VS06_NEIME 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.

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^[1]

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

References

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5nqp"

@@ Line 1: / Line 1: @@
 ==Structure of a fHbp(V1.4):PorA(P1.16) chimera. Fusion at fHbp position 151.==
-<StructureSection load='5nqp' size='340' side='right' caption='[[5nqp]], [[Resolution|resolution]] 2.86&Aring;' scene=''>
+<StructureSection load='5nqp' size='340' side='right'caption='[[5nqp]], [[Resolution|resolution]] 2.86&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5nqp]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"diplokokkus_intracellularis_meningitidis"_(sic)_weichselbaum_1887 "diplokokkus intracellularis meningitidis" (sic) weichselbaum 1887]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NQP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NQP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5nqp]] is a 3 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=5NQP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NQP FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.86&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fhbp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=487 "Diplokokkus intracellularis meningitidis" (sic) Weichselbaum 1887])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5nqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nqp OCA], [http://pdbe.org/5nqp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nqp RCSB], [http://www.ebi.ac.uk/pdbsum/5nqp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nqp ProSAT]</span></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=5nqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nqp OCA], [https://pdbe.org/5nqp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nqp RCSB], [https://www.ebi.ac.uk/pdbsum/5nqp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nqp 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 ==
@@ Line 21: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Hollingshead, S]]
+[[Category: Large Structures]]
-[[Category: Johnson, S]]
+[[Category: Neisseria meningitidis]]
-[[Category: Lea, S M]]
+[[Category: Neisseria meningitidis serogroup C]]
-[[Category: Tang, C M]]
+[[Category: Hollingshead S]]
-[[Category: Chimeric]]
+[[Category: Johnson S]]
-[[Category: Complement]]
+[[Category: Lea SM]]
-[[Category: Immune system]]
+[[Category: Tang CM]]
-[[Category: Meningitis]]
-[[Category: Vaccine]]

5nqp

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Current revision

Structure of a fHbp(V1.4):PorA(P1.16) chimera. Fusion at fHbp position 151.

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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