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Epitope mapping of human antibodies directed against 4CmenB protein components

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Neisseria meningitidis serogroup B Homo sapiens Neisseria meningitidis

PROVIDER: GSE98883 | GEO | 2018/03/07

REPOSITORIES: GEO

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

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2018-03-07 | GSE98878 | GEO

Epitope mapping of human antibodies directed against 4CmenB protein components

Project description:Epitope mapping of human antibodies directed against 4CmenB protein components

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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 11 monoclonal antibodies directed against Neisserial adesin A by peptide microarray

Project description:The aim of the study was to determine the epitope targeted by four different HumAbs and the cross-reactivity to linear peptide epitopes of 5 different Neisserial adesin A (NadA) variants. the HumAbs were diluted at 1:200 and incubated on a custom PepStar Peptide Microarray platform printed with 348 different peptides.

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

Project description:The aim of the study was to determine the epitope targeted by four different HumAbs and the cross-reactivity to linear peptide epitopes of 10 different Neisserial Heparin Binding Antigen (NHBA) variants. the HumAbs were diluted at 1:60 and incubated on a custom PepStar Peptide Microarray platform printed with 561 different peptides.

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

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

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

Project description: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.

2016-05-27 | GSE81378 | GEO

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.

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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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Mapping the conformational epitope of a neutralizing antibody (AcV1) directed against the AcMNPV GP64 protein.

Project description:The envelope glycoprotein GP64 of Autographa californica nucleopolyhedrovirus (AcMNPV) is necessary and sufficient for the acid-induced membrane fusion activity that is required for fusion of the budded virus (BV) envelope and the endosome membrane during virus entry. Infectivity of the budded virus (BV) is neutralized by AcV1, a monoclonal antibody (MAb) directed against GP64. Prior studies indicated that AcV1 recognizes a conformational epitope and does not inhibit virus attachment to the cell, but instead inhibits entry at a step following virus attachment. We found that AcV1 recognition of GP64 was lost upon exposure of GP64 to low pH (pH 4.5) and restored by returning GP64 to pH 6.2. In addition, the AcV1 epitope was lost upon denaturation of GP64 in SDS, but the AcV1 epitope was restored by refolding the protein in the absence of SDS. Using truncated GP64 proteins expressed in insect cells, we mapped the AcV1 epitope to a 24 amino acid region in the central variable domain of GP64. When sequences within the mapped AcV1 epitope were substituted with a c-Myc epitope and the resulting construct was used to replace wt GP64 in recombinant AcMNPV viruses, the modified GP64 protein appeared to function normally. However, an anti-c-Myc monoclonal antibody did not neutralize infectivity of those viruses. Because binding of the c-Myc MAb to the same site in the GP64 sequence did not result in neutralization, these studies suggest that AcV1 neutralization may result from a specific structural constraint caused by AcV1 binding and not simply by steric hindrance caused by antibody binding at this position in GP64.

| S-EPMC3767133 | biostudies-literature

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