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Outer membrane vesicles of the VA‐MENGOC‐BC® vaccine against serogroup B of Neisseria meningitidis : Analysis of protein components by two‐dimensional gel electrophoresis and mass spectrometry
Author(s) -
Uli Liliam,
CastellanosSerra Lila,
Betancourt Lazaro,
Domínguez Francisco,
Barberá Ramón,
Sotolongo Franklin,
Guillén Gerardo,
Pajón Feyt Rolando
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200500502
Subject(s) - bacterial outer membrane , neisseria meningitidis , microbiology and biotechnology , membrane protein , biology , proteome , meningococcal disease , proteomics , bacteria , neisseriaceae , vesicle , neisseria , chemistry , virology , membrane , biochemistry , escherichia coli , gene , genetics , antibiotics
Neisseria meningitidis is a Gram‐negative bacterium responsible for significant mortality worldwide. While effective polysaccharides‐based vaccines exist against serogroups A, C, W135, and Y, no similar vaccine is suitable for children under 4 years against disease caused by serogroup B strains. Therefore, major vaccine efforts against this serogroup are based on outer membrane vesicles (OMVs), containing major outer membrane proteins. The OMV‐based vaccine produced by the Finlay Institute in Cuba (VA‐MENGOC‐BC®) contributed to the rapid decline of the epidemic in this Caribbean island. While the content of major proteins in this vaccine has been discussed, no detailed work of an outer membrane proteomic map of this, or any other, commercially available OMV‐derived product has been published so far. Since OMVs exhibit a large bias toward a few major proteins and usually contain a high content of lipids, establishing the adequate conditions for high resolution, 2‐DE of this kind of preparation was definitely a technical challenge. In this work, 2‐DE and MS have been used to generate a proteomic map of this product, detailing the presence of 31 different proteins, and it allows the identification of new putative protective protein components it contains.