Multivalent meningococcal serogroup B vaccines: challenges in predicting protection and measuring effectiveness

Poolman, Jan; Richmond, Peter

doi:10.1586/14760584.2015.1071670

Cited by 17 publications

(13 citation statements)

References 109 publications

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“…17 The Meningococcal Antigen Typing System predicts that 4CMenB will protect against 91% of U.S. meningococcal B strains. 18 Although the system is designed to quantify the expression of antigen-using polyclonal antibodies against the fHbp, NHBA, and NadA components of 4CMenB and to determine whether bacterial expression is sufficient to elicit a vaccine response, the system cannot determine the degree to which heterogeneity in vaccine-induced immunity can be expected within populations.…”

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confidence: 99%

Immunogenicity of a Meningococcal B Vaccine during a University Outbreak

et al. 2016

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confidence: 99%

Immunogenicity of a Meningococcal B Vaccine during a University Outbreak

et al. 2016

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“…To our knowledge, this study was the first to assess coverage with licensed meningococcal vaccines. Since the 1980s, three monovalent OMV-based MenB vaccines have been licensed for IMD epidemics but they demonstrated clinical efficacy only against homologous meningococci [12]. Although a nonavalent OMV-based MenB vaccine has been evaluated [18], we found low prevalence of its homologous variants among Chinese MenB meningococci based on PorA data in this study (<5%) and from 27 provinces of China (<11%) [26].…”

Section: Discussionmentioning

confidence: 65%

“…To address this deficit, two protein-based vaccines, Bexsero® (4CMenB) and Trumenba® (bivalent rLP2086), were developed and licensed in Europe and the USA [10, 11]. Bexsero® is composed of factor H binding protein (fHbp), Neisserial heparin-binding antigen (NHBA), Neisseria adhesin A (NadA), and PorA, while Trumenba® contains two fHbp-subfamily variants [12]. Both Bexsero® and Trumenba® may elicit protective responses across serogroups [13].…”

Section: Introductionmentioning

confidence: 99%

Characterisation of carried and invasive Neisseria meningitidis isolates in Shanghai, China from 1950 to 2016: implications for serogroup B vaccine implementation

Chen

Rodrigues

Harrison

et al. 2018

Preprint

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vaccine approaches evaluated. Since 1950, MenA:cc5 shifted to MenC:cc4821 then MenB:cc4821, with MenB dominating since 2009. Distinct antigens potentially beyond coverage with licensed OMV-and protein-based MenB vaccines were found. AbstractBackground Serogroup B invasive meningococcal disease (IMD) is increasing in China, little is known however, about these meningococci. This study characterises a collection of isolates associated with IMD and carriage in Shanghai and assesses current vaccine strategies.

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“…SBA is a functional serological surrogate of vaccine efficacy (14, 58, 59). When tested in human SBA (with human complement source) against strains carrying 1 of the 3 fHbp variants, the mAb 1E6 alone failed in eliciting positive titers (<4).…”

Section: Resultsmentioning

confidence: 99%

Cocrystal structure of meningococcal factor H binding protein variant 3 reveals a new crossprotective epitope recognized by human mAb 1E6

et al. 2019

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The 4 component meningococcus B vaccine (4CMenB) vaccine is the first vaccine containing recombinant proteins licensed for the prevention of invasive meningococcal disease caused by meningococcal serogroup B strains. 4CMenB contains 3 main recombinant proteins, including the Neisseria meningitidis factor H binding protein (fHbp), a lipoprotein able to bind the human factor H. To date, over 1000 aa sequences of fHbp have been identified, and they can be divided into variant groups 1, 2, and 3, which are usually not crossprotective. Nevertheless, previous characterizations of a small set (n = 10) of mAbs generated in humans after 4CMenB immunization revealed 2 human Fabs (huFabs) (1A12, 1G3) with some crossreactivity for variants 1, 2, and 3. This unexpected result prompted us to examine a much larger set of human mAbs (n = 110), with the aim of better understanding the extent and nature of crossreactive anti-fHbp antibodies. In this study, we report an analysis of the human antibody response to fHbp, by the characterization of 110 huFabs collected from 3 adult vaccinees during a 6-mo study. Although the 4CMenB vaccine contains fHbp variant 1, 13 huFabs were also found to be crossreactive with variants 2 and 3. The crystal structure of the crossreactive huFab 1E6 in complex with fHbp variant 3 was determined, revealing a novel, highly conserved epitope distinct from the epitopes recognized by 1A12 or 1G3. Further, functional characterization shows that human mAb 1E6 is able to elicit rabbit, but not human, complement-mediated bactericidal activity against meningococci displaying fHbp from any of the 3 different variant groups. This functional and structural information about the human antibody response upon 4CMenB immunization contributes to further unraveling the immunogenic properties of fHbp. Knowledge gained about the epitope profile recognized by the human antibody repertoire could guide future vaccine design.—Bianchi, F., Veggi, D., Santini, L., Buricchi, F., Bartolini, E., Lo Surdo, P., Martinelli, M., Finco, O., Masignani, V., Bottomley, M. J., Maione, D., Cozzi, R. Cocrystal structure of meningococcal factor H binding protein variant 3 reveals a new crossprotective epitope recognized by human mAb 1E6.

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Multivalent meningococcal serogroup B vaccines: challenges in predicting protection and measuring effectiveness

Cited by 17 publications

References 109 publications

Immunogenicity of a Meningococcal B Vaccine during a University Outbreak

Immunogenicity of a Meningococcal B Vaccine during a University Outbreak

Characterisation of carried and invasive Neisseria meningitidis isolates in Shanghai, China from 1950 to 2016: implications for serogroup B vaccine implementation

Cocrystal structure of meningococcal factor H binding protein variant 3 reveals a new crossprotective epitope recognized by human mAb 1E6

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