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Epitope mapping of a monoclonal antibody directed against Neisserial Heparin Binding Antigen by protein microarray

ABSTRACT: The aim of the study was to determine the epitope targeted by 31E10/E7 mouse monoclonal antibody (mAb). mAb 31E10/E7 was diluted at 1:2000 and incubated on a non-commercial Protein Microarray platform printed with NHBA specific recombinant protein fragments and full length NHBA of different variants.

ORGANISM(S): Mus musculus Neisseria meningitidis

PROVIDER: GSE81378 | GEO | 2016/05/27

SECONDARY ACCESSION(S): PRJNA321417

REPOSITORIES: GEO

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Epitope mapping of a monoclonal antibody directed against Neisserial Heparin Binding Antigen by peptide microarray

Project description:The aim of the study was to determine the epitope targeted by 31E10/E7 mouse monoclonal antibody (mAb) and the cross-reactivity to linear peptide epitopes of 10 different Neisserial Heparin Binding Antigen (NHBA) variants. mAb 31E10/E7 was diluted at 1:200 and incubated on a custom PepStar Peptide Microarray platform printed with 560 different peptides in three independent experiments.

2016-05-27 | GSE81377 | GEO

Epitope mapping of 4 monoclonal antibodies directed against Neisserial Heparin Binding Antigen by peptide microarray

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Protein microarray epitope mapping of monoclonal antibody 5H2 raised by human immunization with the 4CMenB vaccine formulation containing the fusion antigen NHBA-NMB1030.

Project description:The aim of the study was to determine the epitope targeted by 5H2 human Fab directed against NHBA and the crossreactivity aginst a panel of nine different NHBA long and short peptide variants (p2, p3, p5, p10, p17, p20, p21, p24, p29). 5H2 were diluted at 1:2000 and incubated on a non-commercial Protein Microarray platform printed with NHBAp2 specific recombinant protein fragments and full length NHBA of different variants.

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Epitope mapping of human Fabs directed against 4CmenB protein components by protein microarray

Project description:The aim of the study was to determine the epitope targeted by a panel of Human Fabs. Fabs were diluted at 1:50 and incubated on a non-commercial Protein Microarray platform printed with fHbp, NHBA and NadA specific recombinant protein fragments and full length fHbp, NHBA and NadA of different variants.

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Epitope mapping of 5 monoclonal antibodies directed against meningococcal factor H binding protein by peptide microarray

Project description:The aim of the study was to determine the epitope targeted by 5 different HumAbs and the cross-reactivity to linear peptide epitopes of 12 different factor H binding protein (fHbp) variants. The HumAbs were diluted at 1:200 and incubated on a custom PepStar Peptide Microarray platform printed with 363 different peptides.

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Epitope mapping of a monoclonal antibody directed against Neisserial Heparin Binding Antigen

Project description:Epitope mapping of a monoclonal antibody directed against Neisserial Heparin Binding Antigen

| PRJNA321411 | ENA

Epitope mapping of a monoclonal antibody directed against Neisserial Heparin Binding Antigen

Project description:This SuperSeries is composed of the SubSeries listed below.

2016-05-27 | GSE81379 | GEO

Epitope Mapping of a Monoclonal Antibody Directed against Neisserial Heparin Binding Antigen Using Next Generation Sequencing of Antigen-Specific Libraries.

Project description:We explore here the potential of a newly described technology, which is named PROFILER and is based on next generation sequencing of gene-specific lambda phage-displayed libraries, to rapidly and accurately map monoclonal antibody (mAb) epitopes. For this purpose, we used a novel mAb (designated 31E10/E7) directed against Neisserial Heparin-Binding Antigen (NHBA), a component of the anti-group B meningococcus Bexsero® vaccine. An NHBA phage-displayed library was affinity-selected with mAb 31E10/E7, followed by massive sequencing of the inserts present in antibody-selected phage pools. Insert analysis identified an amino acid stretch (D91-A128) in the N-terminal domain, which was shared by all of the mAb-enriched fragments. Moreover, a recombinant fragment encompassing this sequence could recapitulate the immunoreactivity of the entire NHBA molecule against mAb 31E10/E7. These results were confirmed using a panel of overlapping recombinant fragments derived from the NHBA vaccine variant and a set of chemically synthetized peptides covering the 10 most frequent antigenic variants. Furthermore, hydrogen-deuterium exchange mass-spectrometry analysis of the NHBA-mAb 31E10/E7 complex was also compatible with mapping of the epitope to the D91-A128 region. Collectively, these results indicate that the PROFILER technology can reliably identify epitope-containing antigenic fragments and requires considerably less work, time and reagents than other epitope mapping methods.

| S-EPMC4980009 | biostudies-literature

Autoimmune peptide antigen reactivity in BXD2 mice with spontaneous systemic autoimmune disease

Project description:The aim of the study was to determine autoimmune BXD2 mouse sera reactivity to linear peptide epitopes from the Immune Epitope Database. Pooled sera from six 8-10 month old BXD2 mice was diluted at 1:1000 and incubated on a PEPperPRINT peptide microarray platform printed with peptide autoantigens.

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