%0 Journal Article %1 ferrari_outer_2006 %A Ferrari, Germano %A Garaguso, Ignazio %A Adu-Bobie, Jeannette %A Doro, Francesco %A Taddei, Anna Rita %A Biolchi, Alessia %A Brunelli, Brunella %A Giuliani, Marzia Monica %A Pizza, Mariagrazia %A Norais, Nathalie %A Grandi, Guido %D 2006 %J Proteomics %K B, Bacterial Biology, Chromatography, Computational Cytometry, Deletion, Detergents, Electrophoresis, Flow Gel, Gene Mass Membrane Neisseria Outer Proteins, Proteomics, Serogroup Serotyping Spectrometry, meningitidis, {Two-Dimensional,} %N 6 %P 1856--66 %R 10.1002/pmic.200500164 %T Outer membrane vesicles from group B Neisseria meningitidis delta gna33 mutant: proteomic and immunological comparison with detergent-derived outer membrane vesicles %U http://www.ncbi.nlm.nih.gov/pubmed/16456881 %V 6 %X We compared the proteome of detergent-derived group B Neisseria meningitidis (MenB) outer membrane vesicles (DOMVs) with the proteome of outer membrane vesicles (m-OMVs) spontaneously released into culture supernatant by MenB delta gna33, a mutant in which the gene coding for a lytic transglycosylase homologous to the E. coli MltA was deleted. In total, 138 proteins were identified in DOMVs by 1- and 2-DE coupled with MS; 64\% of these proteins belonged to the inner membrane and cytoplasmic compartments. By contrast, most of the 60 proteins of m-OMVs were classified by PSORT as outer membrane proteins. When tested for their capacity to elicit bactericidal antibodies, m-OMVs elicited a broad protective activity against a large panel of MenB strains. Therefore, the identification of mutations capable of conferring an OMV-releasing phenotype in bacteria may represent an attractive approach to study bacterial membrane composition and organization, and to design new efficacious vaccine formulations.

@article{ferrari_outer_2006, abstract = {We compared the proteome of detergent-derived group B Neisseria meningitidis {(MenB)} outer membrane vesicles {(DOMVs)} with the proteome of outer membrane vesicles {(m-OMVs)} spontaneously released into culture supernatant by {MenB} delta gna33, a mutant in which the gene coding for a lytic transglycosylase homologous to the E. coli {MltA} was deleted. In total, 138 proteins were identified in {DOMVs} by 1- and {2-DE} coupled with {MS;} 64\% of these proteins belonged to the inner membrane and cytoplasmic compartments. By contrast, most of the 60 proteins of {m-OMVs} were classified by {PSORT} as outer membrane proteins. When tested for their capacity to elicit bactericidal antibodies, {m-OMVs} elicited a broad protective activity against a large panel of {MenB} strains. Therefore, the identification of mutations capable of conferring an {OMV-releasing} phenotype in bacteria may represent an attractive approach to study bacterial membrane composition and organization, and to design new efficacious vaccine formulations.}, added-at = {2011-03-11T10:05:34.000+0100}, author = {Ferrari, Germano and Garaguso, Ignazio and {Adu-Bobie}, Jeannette and Doro, Francesco and Taddei, Anna Rita and Biolchi, Alessia and Brunelli, Brunella and Giuliani, Marzia Monica and Pizza, Mariagrazia and Norais, Nathalie and Grandi, Guido}, biburl = {https://www.bibsonomy.org/bibtex/2d4b624042e36b62e71cadb7c94ad5ab6/jelias}, doi = {10.1002/pmic.200500164}, interhash = {c8c717b75b7417fa90d25d878e75800f}, intrahash = {d4b624042e36b62e71cadb7c94ad5ab6}, issn = {1615-9853}, journal = {Proteomics}, keywords = {B, Bacterial Biology, Chromatography, Computational Cytometry, Deletion, Detergents, Electrophoresis, Flow Gel, Gene Mass Membrane Neisseria Outer Proteins, Proteomics, Serogroup Serotyping Spectrometry, meningitidis, {Two-Dimensional,}}, month = mar, note = {{PMID:} 16456881}, number = 6, pages = {1856--66}, shorttitle = {Outer membrane vesicles from group B Neisseria meningitidis delta gna33 mutant}, timestamp = {2011-03-11T10:05:43.000+0100}, title = {Outer membrane vesicles from group B Neisseria meningitidis delta gna33 mutant: proteomic and immunological comparison with detergent-derived outer membrane vesicles}, url = {http://www.ncbi.nlm.nih.gov/pubmed/16456881}, volume = 6, year = 2006 }