Proteomic Analysis of Outer Membranes and Vesicles from Wild-Type Serogroup B Neisseria meningitidis and a Lipopolysaccharide-Deficient Mutant

• DOI: 10.1128/iai.01424-06
• Publication Date: 2006-12-12T10:40:04Z
• Authors: Jeannette N. Will...; Paul J. Skipp; Holly E. Humphries; Myron Christodoul...; C. David O'Connor; John E. Heckels
• Keywords: Proteome; Neisseria

ABSTRACT Current experimental vaccines against serogroup B Neisseria meningitidis are based on meningococcal outer membrane (OM) proteins present in vesicles (OMV) which toxic lipopolysaccharide is depleted by detergent extraction. Knowledge of the composition OM and OMV essential for developing new defined antigens. In current study, sodium dodecyl sulfate-polyacrylamide gel electrophoresis nanocapillary liquid chromatography-tandem mass spectrometry were used to investigate proteomes from strain MC58 a lipopolysaccharide-deficient mutant. The analysis revealed that was much more complex than has been reported previously; total 236 identified, only 6.4% predicted be located membrane. most abundant included not well-established major (PorA, PorB, Opc, Rmp, Opa) but also other proteins, such as pilus-associated protein Q (PilQ) putative macrophage infectivity protein. All these obtained extraction with deoxycholate. There markedly increased levels some additional mutant, including enzymes contribute tricarboxylic acid cycle. all preparations, have an location predominantly periplasmic or cytoplasmic had unknown location, relatively few detected. However, several previously identified potential vaccine candidates detected either preparations OMV. These results important implications development use proteins.