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| - | [[Image:1uwx.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1uwx.png|left|200px]] |
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| | {{STRUCTURE_1uwx| PDB=1uwx | SCENE= }} | | {{STRUCTURE_1uwx| PDB=1uwx | SCENE= }} |
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| - | '''P1.2 SEROSUBTYPE ANTIGEN DERIVED FROM N. MENINGITIDIS PORA IN COMPLEX WITH FAB FRAGMENT'''
| + | ===P1.2 SEROSUBTYPE ANTIGEN DERIVED FROM N. MENINGITIDIS PORA IN COMPLEX WITH FAB FRAGMENT=== |
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| - | ==Overview==
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| - | Neisseria meningitidis is a globally important cause of bacterial meningitis and septicemia. No comprehensive antimeningococcal vaccine is available, largely as a consequence of the high sequence diversity of those surface proteins that could function as components of a vaccine. One such component is the protein PorA, a major surface porin of this Gram-negative organism that has been used in a number of experimental and licensed vaccines. Here we describe a series of experiments designed to investigate the consequences for antibody recognition of sequence diversity within a PorA antigen. The binding of a 14-residue peptide, corresponding to the P1.2 subtype antigen, to the MN16C13F4 monoclonal antibody was sensitive to mutation of five out of the six residues within the epitope sequence. The crystal structure of the antibody Fab fragment, determined in complex with the peptide antigen, shows a remarkably hydrophobic binding site and interactions between the antigen and antibody are dominated by apolar residues. Nine intrachain hydrogen bonds are formed within the antigen which maintain the beta-hairpin conformation of the peptide. These hydrogen bonds involve residues that are highly conserved amongst different P1.2 sequence variants, suggesting that some positions may be conserved for structural reasons in these highly polymorphic regions. The sensitivity of antibody recognition of the antigen towards mutation provides a structural explanation for the widespread sequence variation seen in different PorA sequences in this region. Single point mutations are sufficient to remove binding capability, providing a rationale for the manner in which different meningococcal PorA escape variants arise.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16470851}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16470851 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16470851}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Pora]] | | [[Category: Pora]] |
| | [[Category: Protein g]] | | [[Category: Protein g]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:47:51 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:28:21 2008'' |
Revision as of 21:28, 28 July 2008
Template:STRUCTURE 1uwx
P1.2 SEROSUBTYPE ANTIGEN DERIVED FROM N. MENINGITIDIS PORA IN COMPLEX WITH FAB FRAGMENT
Template:ABSTRACT PUBMED 16470851
About this Structure
1UWX is a Protein complex structure of sequences from Mus musculus, Neisseria meningitidis and Streptococcus sp.. Full crystallographic information is available from OCA.
Reference
Structural variation and immune recognition of the P1.2 subtype meningococcal antigen., Tzitzilonis C, Prince SM, Collins RF, Achtman M, Feavers IM, Maiden MC, Derrick JP, Proteins. 2006 Mar 1;62(4):947-55. PMID:16470851
Page seeded by OCA on Tue Jul 29 00:28:21 2008
