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Immunological fingerprint of 4CMenB recombinant antigens via protein microarray

ABSTRACT: Immunological fingerprint of 4CMenB recombinant antigens via protein microarray

PROVIDER: PRJNA640397 | ENA |

REPOSITORIES: ENA

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Immunological fingerprint of 4CMenB recombinant antigens via protein microarray

Project description:In this study, we describe the development and use of an ad hoc protein microarray to study the immune response induced by the three major 4CMenB antigenic components (fHbp, NHBA and NadA) in individual sera from vaccinated infants, adolescents and adults.

2020-08-28 | GSE152785 | GEO

Immunological fingerprint of 4CMenB recombinant antigens via protein microarray reveals key immunosignatures correlating with bactericidal activity.

Project description:Serogroup B meningococcus (MenB) is a leading cause of meningitis and sepsis across the world and vaccination is the most effective way to protect against this disease. 4CMenB is a multi-component vaccine against MenB, which is now licensed for use in subjects >2 months of age in several countries. In this study, we describe the development and use of an ad hoc protein microarray to study the immune response induced by the three major 4CMenB antigenic components (fHbp, NHBA and NadA) in individual sera from vaccinated infants, adolescents and adults. The resulting 4CMenB protein antigen fingerprinting allowed the identification of specific human antibody repertoire correlating with the bactericidal response elicited in each subject. This work represents an example of epitope mapping of the immune response induced by a multicomponent vaccine in different age groups with the identification of protective signatures. It shows the high flexibility of this microarray based methodology in terms of high-throughput information and minimal volume of biological samples needed.

| S-EPMC7536418 | biostudies-literature

OpcA and PorB are novel bactericidal antigens of the 4CMenB vaccine in mice and humans

Project description:In this study, we describe the development and use of an ad hoc protein microarray to study the immune response induced by the OMV component of 4CMenB vaccine in infant sera before and after vaccination

2023-04-15 | GSE224340 | GEO

ARTICLE OPEN OpcA and PorB are novel bactericidal antigens of the 4CMenB vaccine in mice and humans

2023-04-12 | GSE224291 | GEO

OpcA and PorB are novel bactericidal antigens of the 4CMenB vaccine in mice and humans

Project description:OpcA and PorB are novel bactericidal antigens of the 4CMenB vaccine in mice and humans

| PRJNA930682 | ENA

OpcA and PorB are novel bactericidal antigens of the 4CMenB vaccine in mice and humans

Project description:OpcA and PorB are novel bactericidal antigens of the 4CMenB vaccine in mice and humans

| PRJNA930686 | ENA

Isolation of human monoclonal antibodies from 4CMenB vaccinees reveals PorB and LOS as the main OMV components inducing cross-strain protection [ Recombinant Chip]

Project description:In this study, we describe the development and use of an ad hoc protein microarray to characterize the target of HumAbs isolated from 4CMenB vaccinated subjects and induced by the OMV component of the vaccine

2025-04-09 | GSE291739 | GEO

ARTICLE OPEN OpcA and PorB are novel bactericidal antigens of the 4CMenB vaccine in mice and humans

Project description:ARTICLE OPEN OpcA and PorB are novel bactericidal antigens of the 4CMenB vaccine in mice and humans

| PRJNA930472 | ENA

Structural dynamics and immunogenicity of the recombinant and outer membrane vesicle-embedded Meningococcal antigen NadA

Project description:The structure and conformation adopted by protein vaccine antigens significantly influence the exposure of their antigenic determinants. Structural knowledge of antigens in native state could drive the design of recombinant vaccines that resemble their cognate native forms, although such information is often difficult to obtain, particularly for membrane proteins. Here, we assessed the structural and functional features of the native Neisseria Adhesin A (NadA), a meningococcal trimeric outer membrane protein included as soluble recombinant antigen in the 4CMenB vaccine. We used hydrogen-deuterium exchange mass spectrometry (HDX-MS) to generate a structural model of NadA and to compare the fold and structural dynamics of the recombinant NadA as soluble vaccine form, and the native NadA in situ, as embedded in meningococcal outer membrane vesicles (OMVs), complementing the HDX data with electron microscopy imaging. While their overall structures are similar, conformational differences between the two forms were observed. Especially, OMV- embedded NadA appears more susceptible to trimer opening than its cognate soluble antigen, suggesting that NadA in its native membrane could display a larger antigenic surface. Accordingly, we show that mice immunized with OMV-embedded NadA elicited antibodies with superior bactericidal activity and capable of better preventing bacterial adhesion compared to the soluble antigen. Collectively, these data support the hypothesis that protein vaccine antigens presented in native-like environments can elicit a more potent immune response than recombinant forms.

2025-09-15 | PXD058197 | Pride

Safety and Immunogenicity of the Recombinant BCG Vaccine AERAS-422 in Healthy BCG-naïve Adults: A Randomized, Active-controlled, First-in-human Phase 1 Trial

Project description:We report a first-in-human trial evaluating safety and immunogenicity of a recombinant BCG, AERAS-422, over-expressing TB antigens Ag85A, Ag85B, and Rv3407 and expressing mutant perfringolysin. Interpretation: The unexpected development of VZV in two of eight healthy adult vaccine recipients resulted in discontinuation of AERAS-422 vaccine development. Immunological and transcriptomal data identified correlations with the development of TB immunity and VZV that require further investigation.

2016-09-22 | GSE87186 | GEO

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