Lipoprotein NMB0928 from Neisseria meningitidis serogroup B as a novel vaccine candidate

Delgado, Maité; Yero, Daniel; Niebla, Olivia; González, Sonia; Climent, Yanet; Pérez, Yusleydis; Cobas, Karem; Caballero, Evelin; García, Duniesky Martinez; Pajón, Rolando

doi:10.1016/j.vaccine.2007.09.053

Cited by 30 publications

(23 citation statements)

References 52 publications

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“…Using the LC-MS/MS analysis, Aguilera et al, identified 18 different proteins that have been found to be strain specific and others are outer membrane vesicles of pathogens. These outer membrane vesicles shows binding with the host and increase the beneficial and positive effects on the host intestinal function [161]. Moreover, OMVs are known to be strong immunomodulatory, so they can also be used as potent pathogen-free vaccines after modifying its immunogenic contents.…”

Section: Significance Of Omv In the Development Of Probioticsmentioning

confidence: 99%

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Significances of OMV and Extracellular Vesicle Proteomics

Tiwari¹

2017

J Data Mining Genomics Proteomics

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Outer Membrane Vesicle (OMV) proteome has been involved into the pathogenesis of diseases and resistance of microorganisms against a number of antibiotics, mechanism of action of probiotics and host-pathogen interaction etc. We have enlightened the role played by extracellular vesicles proteomics in the pathogenesis of different diseases related to human. Isolation succeeded by purification of ample amount of OMV from biological samples, is one of the most important steps for further proteome related analysis. With the development of both labelled and label-free methods used in proteomics, significant progress has been made in previous years in membrane proteomics. Hence, it is important to review the biological significance of proteins found in the OMV fractions using membrane proteomics approach. We have also explained methods used for isolation, purification and quantification of OMV. In the present review, it can be concluded that proteomic study of outer membrane and extracellular vesicles has now gained priority for the detailed study of disease pathogenesis, drug resistance, vaccine development, cell signalling etc.

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Section: Significance Of Omv In the Development Of Probioticsmentioning

confidence: 99%

“…Proteomic analysis of OMV has enabled researchers to identify new vaccine targets against various pathogens by increasing host immune responses. This includes neonatal meningitis E. coli (NMEC) [136], group A Streptococcus [160] and Neisseria meningitidis serogroup B [161].…”

Section: Significance Of Omv In the Development Of Probioticsmentioning

confidence: 99%

Significances of OMV and Extracellular Vesicle Proteomics

Tiwari¹

2017

J Data Mining Genomics Proteomics

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“…Vaccines based on capsular polysaccharides confer protection against bacteria of the same serogroup, but, unfortunately, the serogroup B capsular polysaccharide cannot be used due to its poor immunogenicity in humans and the potential risk of autoimmunity (17). Subcapsular antigens, mainly outer membrane proteins (OMPs) (1,11,48), have been extensively examined as alternative candidates for the development of a vaccine against this serogroup.…”

Section: Meningococcal Disease Is a Systemic Infection Caused Bymentioning

confidence: 99%

Coincorporation of LpxL1 and PagL Mutant Lipopolysaccharides into Liposomes withNeisseria meningitidis Opacity Protein: Influence on Endotoxic and Adjuvant Activity

Arenas

Dijken²,

Kuipers³

et al. 2010

Clin Vaccine Immunol

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Wild-type lipopolysaccharide (LPS) of Neisseria meningitidis normally contains six acyl chains. Pentaacylated LPS forms were generated through inactivation of the lpxL1 gene or through the expression of the Bordetella bronchiseptica pagL gene in N. meningitidis. The resulting LPS species, designated LpxL1 LPS and PagL LPS, respectively, display reduced endotoxic activity compared to wild-type LPS. Here, we determined the adjuvant potential of PagL LPS by comparison with the broadly used LpxL1 LPS. We also investigated the potential benefit for adjuvanticity of coincorporating these LPS species, together with the meningococcal opacity-associated protein OpaJ as a model antigen, in a liposomal delivery system. PagL LPS showed a higher endotoxic activity than LpxL1 LPS, and their incorporation into liposomes significantly reduced their endotoxic activity as determined by measuring the induction of interleukin-6 (IL-6) production in a murine macrophage cell line. To determine the adjuvant effect, BALB/c mice were immunized with OpaJ-containing liposomes and either free LPS or LPS coincorporated into the proteoliposomes. OpaJ-containing liposomes adjuvanted with AlPO 4 or not adjuvanted at all were included as control groups. In the appropriate dose, PagL LPS showed a superior adjuvant effect compared with LpxL1 LPS, and for both LPS types, free LPS showed a higher adjuvant effect than when coincorporated into the liposomes, as evidenced by higher titers of IgG2a and IgG2b antibodies against OpaJ ؉ meningococci and higher bactericidal titers. In conclusion, PagL LPS is a better adjuvant than LpxL1 LPS, but coincorporation of either LPS into proteoliposomes did not improve their adjuvant activity.

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“…In parallel, techniques for proteomic and immunoproteomic analysis have been applied to characterize the antigen composition of commercial complex vaccines, and particularly some applications have arisen for the characterization of OMVs of pathogenic bacteria (Nally et al, 2005;Wheeler et al, 2007). For the meningococcus, such analytical approaches have recently identified new vaccine candidates (Delgado et al, 2007;Hsu et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

“…A set of these antigens that show promise as vaccine candidates is currently under preclinical evaluation (Delgado et al, 2007). One of these antigens is the protein NMB0088 with an apparent molecular mass of approximately 50 kDa.…”

Section: Introductionmentioning

confidence: 99%

Neisseria meningitidis antigen NMB0088: sequence variability, protein topology and vaccine potential

Sardiñas

Yero

Climent

et al. 2009

Journal of Medical Microbiology

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The significance of Neisseria meningitidis serogroup B membrane proteins as vaccine candidates is continually growing. Here, we studied different aspects of antigen NMB0088, a protein that is abundant in outer-membrane vesicle preparations and is thought to be a surface protein. The gene encoding protein NMB0088 was sequenced in a panel of 34 different meningococcal strains with clinical and epidemiological relevance. After this analysis, four variants of NMB0088 were identified; the variability was confined to three specific segments, designated VR1, VR2 and VR3. Secondary structure predictions, refined with alignment analysis and homology modelling using FadL of Escherichia coli, revealed that almost all the variable regions were located in extracellular loop domains. In addition, the NMB0088 antigen was expressed in E. coli and a procedure for obtaining purified recombinant NMB0088 is described. The humoral immune response elicited in BALB/c mice was measured by ELISA and Western blotting, while the functional activity of these antibodies was determined in a serum bactericidal assay and an animal protection model. After immunization in mice, the recombinant protein was capable of inducing a protective response when it was administered inserted into liposomes. According to our results, the recombinant NMB0088 protein may represent a novel antigen for a vaccine against meningococcal disease. However, results from the variability study should be considered for designing a cross-protective formulation in future studies.

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Lipoprotein NMB0928 from Neisseria meningitidis serogroup B as a novel vaccine candidate

Cited by 30 publications

References 52 publications

Significances of OMV and Extracellular Vesicle Proteomics

Significances of OMV and Extracellular Vesicle Proteomics

Coincorporation of LpxL1 and PagL Mutant Lipopolysaccharides into Liposomes withNeisseria meningitidis Opacity Protein: Influence on Endotoxic and Adjuvant Activity

Neisseria meningitidis antigen NMB0088: sequence variability, protein topology and vaccine potential

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