Characterisation and immune responses to meningococcal recombinant porin complexes incorporated into liposomes.
We have analysed the structure of meningococcal outer membrane complexes and found that the main complexes are formed by different combinations of PorA and/or PorB molecules, associated to other proteins such as RmpM. In view of the growing knowledge of the importance of conformational epitopes in the immune responses to many pathogens, our aim in this study was to analyse the interactions of PorA and PorB by reconstitution of both recombinant porins into liposomes and determine the relevance of these interactions for the immune response. Recombinant PorA and PorB incorporated into liposomes associate forming complexes that are homomeric when only one of the porins is present, but heteromeric when both neisserial porins are present, mimicking those found previously in native outer membrane vesicles (OMVs). Association of PorA and PorB to form heterocomplexes modifies the immunogenicity of at least PorB, allowing the production of antibodies that recognise conformational epitopes, and produces new epitopes that react with a 50 kDa outer membrane protein not yet identified.
Sánchez
Sandra
S
Departamento de Microbiología y Parasitología, Facultade de Farmacia, Campus Sur, Universidad de Santiago de Compostela, 15782 Santiago de Compostela, Spain.
Abel
Ana
A
Marzoa
Juan
J
Gorringe
Andrew
A
Criado
Teresa
T
Ferreirós
Carlos M
CM
D000818:Animals; D001425:Bacterial Outer Membrane Proteins / Q000276:immunology*; D008081:Liposomes / Q000276:immunology*; D022401:Meningococcal Vaccines / Q000276:immunology*; D051379:Mice; D009345:Neisseria meningitidis / Q000276:immunology; D018272:Porins / Q000276:immunology*; D011994:Recombinant Proteins / Q000276:immunology
D001425:Bacterial Outer Membrane Proteins; D008081:Liposomes; D022401:Meningococcal Vaccines; D018272:Porins; D011994:Recombinant Proteins; C057699:porin protein, Neisseria