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Epitope Mapping of CCHFV Nucleoprotein

ABSTRACT: Mapping the binding site of mAb-9D5 on CCHFV Nucleoprotein as part of a larger study describing NP as an important target of protective mAb in mice

INSTRUMENT(S): Orbitrap Fusion Lumos, LTQ Orbitrap Elite

ORGANISM(S): Crimean-congo Hemorrhagic Fever Virus (ncbitaxon:11593) Mus Musculus (ncbitaxon:10090)

SUBMITTER: Aura Garrison

PROVIDER: MSV000092981 | MassIVE |

REPOSITORIES: MassIVE

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Epitope Mapping of CCHFV Nucleoprotein

Project description:Mapping the binding site of mAb-9D5 on CCHFV Nucleoprotein as part of a larger study describing NP as an important target of protective mAb in mice

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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.

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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.

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Hydrogen deuterium exchange epitope mapping of glycosylated epitopes enabled by online immobilized glycosidase

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Intact Transition Epitope Mapping – Serological Inspection by Epitope EXtraction (ITEM – SIX)

Project description:Precision medicine requests accurate serological inspections to precisely stratify patients for targeted treatment. Intact transition epitope mapping analysis proved seroconversion of a model organism's serum when spiked with a monoclonal murine anti-ovalbumin antibody with epitope-resolution. Isolation of the IgG fraction from blood serum applied two consecutive protein precipitation steps followed by ultrafiltration and resulted in an ESI-MS analysis-ready IgG preparation. For epitope mapping by epitope extraction, the ovalbumin antigen was digested with trypsin. After desalting, the peptide mixture was added to the ESI-MS-ready IgG preparation from converted serum and the solution was incubated to form an immune complex between the ovalbumin-derived epitope peptide and the anti-ovalbumin antibody. Then, the entire mixture of proteins and peptides was directly electrosprayed. Sorting of ions in the mass spectrometer's gas phase, dissociation of the immune complex ions by collision induced dissociation, and recording of the epitope peptide ion which had been released from the immune complex revealed the presence of the anti-ovalbumin antibody in converted serum. Mass determination of the complex-released epitope peptide ion with isotope resolution is highly accurate, guaranteeing high specificity of this novel seroconversion analysis approach which is termed Intact Transition Epitope Mapping – Serological Inspections by Epitope EXtraction (ITEM – SIX).

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Epitope Mapping of Human Polyclonal Antibodies to the fHbp Antigen of a Neisseria Meningitidis Vaccine by Hydrogen-Deuterium Exchange Mass Spectrometry (HDX-MS)

Project description:Antigen-antibody interactions play a key role in the immune response post vaccination and the mechanism of action of antibody-based biopharmaceuticals. 4CMenB is a multicomponent vaccine against Neisseria meningitidis serogroup B in which factor H binding protein (fHbp) is one of the key antigens. In this study, we use hydrogen/deuterium exchange mass spectrometry (HDX-MS) to identify epitopes in fHbp recognized by polyclonal antibodies (pAb) from two human donors (HDs) vaccinated with 4CMenB. Our HDX-MS data reveal several epitopes recognized by the complex mixture of human pAb. Furthermore, we show that the pAb from the two HDs recognize the same epitope regions. Epitope mapping of total pAb and purified fHbp-specific pAb from the same HD reveals that the two antibody samples recognize the same main epitopes, showing that HDX-MS based epitope mapping can, in this case at least, be performed directly using total IgG pAb samples that have not undergone Ab-selective purification. Two monoclonal antibodies (mAb) were previously produced from B-cell repertoire sequences from one of the HDs and used for epitope mapping of fHbp with HDX-MS. The epitopes identified for the pAb from the same HD in this study, overlap with the epitopes recognized by the two individual mAbs. Overall, HDX-MS epitope mapping appears highly suitable for simultaneous identification of epitopes recognized by pAb from human donors and to thus both guide vaccine development and study basic human immunity to pathogens, including viruses.

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Epitope Mapping of Human Polyclonal Antibodies to the fHbp Antigen of a Neisseria Meningitidis Vaccine by Hydrogen-Deuterium Exchange Mass Spectrometry (HDX-MS) - part 2

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Characterizing the interactions between a naturally-primed IgA and its conserved Bacteroides thetaiotaomicron species-specific epitope in gnotobiotic mice [RNA-Seq]

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