Prevalence and sequence variations of the genes encoding the five antigens included in the novel 5CVMB vaccine covering group B meningococcal disease

Jacobsson, Susanne; Hedberg, Sara Thulin; Mölling, Paula; Unemo, Magnus; Comanducci, Maurizio; Rappuoli, Rino; Olcén, Per

doi:10.1016/j.vaccine.2008.12.052

Cited by 47 publications

(33 citation statements)

References 24 publications

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“…We demonstrate here that this lipoprotein is localized at the periplasmic side of the OM. This conclusion is corroborated by the amino acid sequence of GNA2091, which is highly conserved among N. meningitidis strains (25). N. meningitidis is notorious for its ability to vary the amino acid sequence of surface-exposed proteins to avoid immune recognition by the host.…”

Section: Discussionmentioning

confidence: 75%

Involvement of Neisseria meningitidis Lipoprotein GNA2091 in the Assembly of a Subset of Outer Membrane Proteins

Bos

Grijpstra

Boxtel

et al. 2014

Journal of Biological Chemistry

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Background: Outer membrane protein assembly is an incompletely understood process in Gram-negative bacteria. Results: A Neisseria meningitidis mutant lacking the lipoprotein GNA2091 is affected in growth and accumulates unassembled outer membrane proteins. Conclusion:We identified a novel component involved in outer membrane biogenesis. Significance: Our findings contribute to the understanding of a fundamental process occurring in Gram-negative bacteria.

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Section: Discussionmentioning

confidence: 75%

Involvement of Neisseria meningitidis Lipoprotein GNA2091 in the Assembly of a Subset of Outer Membrane Proteins

Bos

Grijpstra

Boxtel

et al. 2014

Journal of Biological Chemistry

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“…Several epidemiology studies have been conducted to asses the presence and conservation of genes coding for the antigens included in the recombinant MenB vaccine (17)(18)(19)(20). Considering that the nhba gene is present in all of the strains analyzed so far and that, despite amino acid sequence variations, it showed cross-protective activity for most of the strains tested in preclinical studies (5), we believe NHBA is an important antigen to be included in a meningococcal vaccine.…”

Section: Mc58mentioning

confidence: 99%

Neisseria meningitidis GNA2132, a heparin-binding protein that induces protective immunity in humans

Serruto

Spadafina

Ciucchi

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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188

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GNA2132 is a Neisseria meningitidis antigen of unknown function, discovered by reverse vaccinology, which has been shown to induce bactericidal antibodies in animal models. Here we show that this antigen induces protective immunity in humans and it is recognized by sera of patients after meningococcal disease. The protein binds heparin in vitro through an Arg-rich region and this property correlates with increased survival of the unencapsulated bacterium in human serum. Furthermore, two proteases, the meningococcal NalP and human lactoferrin, cleave the protein upstream and downstream from the Arg-rich region, respectively. We conclude that GNA2132 is an important protective antigen of N. meningitidis and we propose to rename it, N eisserial H eparin B inding A ntigen (NHBA).

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“…However, within a single bacterial species, AT-1 coding genes can be in single or multiple copies, and display allelic and phase variation (Pallen et al, 2003;van der Woude & Henderson, 2008). For these reasons, besides immunological studies, a genomic comparison among virulent strains is necessary to further consider these proteins as potential vaccine candidates (Jacobsson et al, 2009). …”

Section: Introductionmentioning

confidence: 99%

Genomic and antigenic characterization of monomeric autotransporters of Haemophilus parasuis: an ongoing process of reductive evolution

et al. 2012

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The genome of the highly pathogenic Haemophilus parasuis Nagasaki strain (serovar 5) was sequenced to 99 % completion. A genomic comparison with two other pathogenic serovar 5 H. parasuis strains identified six genes per genome (bmaA1-bmaA6) encoding b-barrel monomeric autotransporters, bmaA2 and bmaA3 being pseudogenes in at least one strain. The remaining encoded proteins were predicted to belong to the subtilisin (BmaA1 and BmaA4) and cysteine (BmaA5 and BmaA6) protease families. Allelic polymorphism was detected in other H. parasuis strains by comparative genomic hybridization using microarrays. Recombination events were observed, some of them leading to gene disruption in one of the three strains, although synteny around bmaA genes was conserved. These results suggest that bmaA genes are undergoing a process of reductive evolution. To evaluate their use as potential vaccine antigens, the products of the passenger domains of bmaA1, bmaA4, bmaA5 and bmaA6 were produced in Escherichia coli as recombinant proteins. They were detected by immunoblotting using sera of colostrum-deprived piglets recovering from a sublethal infection with H. parasuis (Nagasaki). The existence of specific antibodies after infection with H. parasuis also demonstrated in vivo expression. Using proteomics, only BmaA6 was detected in the in vitro-grown Nagasaki strain. Interestingly, the translocator domain was found in the outer membrane, while the passenger domain was located in supernatants. These results indicate that BmaA proteins could be considered as immunogen candidates to improve H. parasuis vaccines. However, their capacity to confer protective immunity needs to be studied further.

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Prevalence and sequence variations of the genes encoding the five antigens included in the novel 5CVMB vaccine covering group B meningococcal disease

Cited by 47 publications

References 24 publications

Involvement of Neisseria meningitidis Lipoprotein GNA2091 in the Assembly of a Subset of Outer Membrane Proteins

Involvement of Neisseria meningitidis Lipoprotein GNA2091 in the Assembly of a Subset of Outer Membrane Proteins

Neisseria meningitidis GNA2132, a heparin-binding protein that induces protective immunity in humans

Genomic and antigenic characterization of monomeric autotransporters of Haemophilus parasuis: an ongoing process of reductive evolution

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