Commentary: Opportunities to decrease mortality and long-term sequellae associated with meningococcal disease in Africa

Rosenstein, Nancy E.

doi:10.1093/ije/30.6.1447

Cited by 4 publications

(4 citation statements)

References 7 publications

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“…An alternative approach is to improve low-cost diagnostics to limit the use of more costly but effective treatment to those who specifically need it. 6,7 Diagnostic confidence in clinical cases of meningitis is further complicated because of prior antibiotic therapy, which frequently renders cultures negative. 8 -10 In these cases, latex agglutination test (LAT) identifies the etiology in many cases; however, antibiotic susceptibility of these strains cannot be determined.…”

mentioning

confidence: 99%

Direct Detection of the Multidrug Resistance Genome of Haemophilus influenzae in Cerebrospinal Fluid of Children

Saha¹,

Baqui²,

Islam³

et al. 2008

Pediatric Infectious Disease Journal

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mentioning

confidence: 99%

Direct Detection of the Multidrug Resistance Genome of Haemophilus influenzae in Cerebrospinal Fluid of Children

Saha¹,

Baqui²,

Islam³

et al. 2008

Pediatric Infectious Disease Journal

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“…The structure revealed a large conformational epitope, featuring a dense network of salt bridges and hydrogen bonds, mainly localized at the N terminus of fHbp variant 3 that was not previously seen in other crystal structures of fHbp complexed with murine Fabs, nor with huFab 1A12, which targets a very different region on the C-terminal domain of fHbp (Figs. [3][4][5][6].…”

Section: Discussionmentioning

confidence: 99%

“…Bacterial strains have been classified in 12 serogroups based on the composition of their capsular polysaccharide (4, 5), but only serogroups A, B, C, W, X, and Y are responsible for almost all cases of invasive meningococcal disease (1, 2, 6). …”

mentioning

confidence: 99%

“…Neisseria meningitidis is an exclusively human pathogen, able to colonize the mucosal surfaces, proliferate, and (under some instances) invade the bloodstream, causing morbidity and mortality in infants, children, and young adults worldwide (1–3). Bacterial strains have been classified in 12 serogroups based on the composition of their capsular polysaccharide (4, 5), but only serogroups A, B, C, W, X, and Y are responsible for almost all cases of invasive meningococcal disease (1, 2, 6).…”

mentioning

confidence: 99%

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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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Estimates of the reproductive numbers and demographic reconstruction of outbreak associated with C:P1.5–1,10–8:F3–6:ST–11(cc11) Neisseria meningitidis strains

Presti

Vacca

Neri

et al. 2020

Infection, Genetics and Evolution

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Commentary: Opportunities to decrease mortality and long-term sequellae associated with meningococcal disease in Africa

Cited by 4 publications

References 7 publications

Direct Detection of the Multidrug Resistance Genome of Haemophilus influenzae in Cerebrospinal Fluid of Children

Direct Detection of the Multidrug Resistance Genome of Haemophilus influenzae in Cerebrospinal Fluid of Children

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

Estimates of the reproductive numbers and demographic reconstruction of outbreak associated with C:P1.5–1,10–8:F3–6:ST–11(cc11) Neisseria meningitidis strains

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