Characterisation and immune responses to meningococcal recombinant porin complexes incorporated into liposomes

Sandra Sánchez, Ana Abel, Juan Marzoa, Andrew Gorringe, Teresa Criado, Carlos M. Ferreirós*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)5338-5343
Number of pages6
Issue number39
Publication statusPublished - 27 Aug 2009

Bibliographical note

Funding Information:
This work was supported by grants PI050178 from the Fondo de Investigación Sanitaria (FIS, Ministerio de Sanidad y Consumo, Spain), and 2007/XA063-1 from the Consellería de Educación e Ordenación Universitaria (Xunta de Galicia, Spain).


  • Native electrophoresis
  • Neisseria meningitidis
  • Porin complexes


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