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  • 1
    Electronic Resource
    Electronic Resource
    Cloning and Molecular Analysis of the galE Gene of Neisseria meningitidis and Its Role in Lipopolysaccharide Biosynthesis (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 730 (1994), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1994.tb44256.x
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  • 2
    Electronic Resource
    Electronic Resource
    Identification of a locus involved in meningococcal lipopolysaccharide biosynthesis by deletion mutagenesis (1996)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 19 (1996), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: A novel method for insertion/deletion mutagenesis in meningococci was devised. This consisted of ligating a digest of total chromosomal DNA to a 1.1 kb restriction fragment containing an erythromycin-resistance marker (ermC), and subsequent transformation of the ligation mixture into the homologous meningococcal strain H44/76. Southern blotting of a number of the resulting erythromycin-resistant transformants demonstrated that all carried the ermC gene inserted at different positions in the chromosome. Mutants with a specific phenotype were identified by screening with the anti-lipopolysaccharide (LPS) monoclonal antibody MN4A8B2, which is specific for immunotype L3. In this way, two independent L3-negative mutant strains were isolated. In transformation experiments with chromosomal DNA from these mutants, erythromycin-resistance and lack of MN4A8B2 reactivity were always linked, showing that the insertion/deletion was in a locus involved in LPS biosynthesis. On SDS–PAGE, the mutant LPS displayed an electrophoretic mobility intermediate between that produced by the previously isolated galE and rfaF mutant strains. Chemical analysis of the mutant LPS revealed that the structure was probably lipid A–(KDO)2–(Hep)2. Chromosomal DNA flanking the ermC insertion in these two mutant strains was cloned, and used as probe for the isolation of the corresponding region of the wild-type strain. From hybridization and polymerase chain reaction (PCR) analysis, it could be concluded that both mutations map to the same locus. The affected gene probably encodes the glycosyltransferase necessary for adding N-acetylglucosamine to heptose.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1996.464992.x
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  • 3
    Electronic Resource
    Electronic Resource
    Cloning and molecular analysis of the galE gene of Neisseria meningitidls and its role in lipopolysaccharide biosynthesis (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 10 (1993), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The galE gene from Haemophilus influenzae was used as a hybridization probe for the galE gene of Neisseria meningitidis Group B, identifying two different homologous loci. Each of the loci was cloned and nucleotide sequence analysis revealed that both loci contained sequences similar to galE. One contained a functional galE gene and mapped to the capsule biosynthetic locus. The second contained only a partial galE-coding sequence, which did not express a functional gene product. A galE mutant meningococcal strain was constructed by transformation with an inactivated galE gene. Analysis of the LPS from the galE mutant strain revealed an apparent reduction in molecular weight and a loss of reactivity with monoclonal antibodies specific for structures known to contain galactose. These results are consistent with an essential role for galE in the incorporation of galactose into meningococcal lipopolysaccharide.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1993.tb01962.x
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  • 4
    Electronic Resource
    Electronic Resource
    Epitope specificity of murine and human bactericidal antibodies against PorA P1.7,16 induced with experimental meningococcal group B vaccines (1997)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS immunology and medical microbiology 17 (1997), S. 0 
    Details
    ISSN: 1574-695X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Synthetic peptides derived from the predicted loops 1 and 4 of meningococcal PorA, sero-subtype P1.7,16, were used to study the epitope specificity of murine and human PorA P1.7,16 bactericidal antibodies. The predicted loops 1 and 4 are surface exposed and carry in their apices the sero-subtype epitopes P1.7 (loop 1) or P1.16 (loop 4), respectively. Peptides were synthesized as mono- and multimeric peptides. Murine monoclonal and polyclonal antibodies were induced with meningococcal whole cell preparations. Polyclonal antibodies were evoked in volunteers after one immunization with 50 μg or 100 μg protein of a hexavalent meningococcal PorA vesicle vaccine. The induction of PorA antibodies was determined in ELISA using purified PorA P1.7,16. The epitope specificity of anti-PorA antibodies for both murine and human antibodies could be demonstrated by direct peptide ELISA using overlapping multimeric peptides almost spanning the entire loops 1 or 4 of the protein. The capacity of peptides to inhibit the bactericidal activity of murine and human antibodies was investigated using meningococcal strain H44/76 (B:15:P1.7,16) as a target strain. Bactericidal activities could be inhibited with both monomeric and multimeric peptides derived from epitopes P1.7 and P1.16.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-695X.1997.tb01006.x
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  • 5
    Electronic Resource
    Electronic Resource
    Analysis of the icsBA locus required for biosynthesis of the inner core region from Neisseria meningitidis lipopolysaccharide (1997)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 146 (1997), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: By deletion mutagenesis in the entire meningococcal chromosome, we have previously identified the icsA gene, which encodes the glycosyltransferase required for adding GlcNAc to Hep-II in the inner core of meningococcal LPS. This gene has homology to several LPS glycosyltransferases, notably to rfaK from Salmonella typhimurium and bplH from Bordetella pertussis, both of which encode GlcNAc transferases. Directly upstream of icsA is an ORF showing significant homology to the hypothetical protein HI0653 from the Haemophilus influenzae genome sequence, and to a lesser degree to putative glycosyltransferases from Streptococcus thermophilus and Yersinia enterocolitica. Insertional inactivation of this ORF resulted in a meningococcal strain with truncated LPS. We have named this new LPS-involved gene icsB. Differences in binding of monoclonal antibodies and in mobility on Tricine-SDS-PAGE showed that LPS from icsA and icsB mutants is similar but not identical. On the basis of these results, we postulated that the new gene encodes the glycosyltransferase required for adding Glc to Hep-I. Structural analysis of purified mutant LPS by electrospray mass spectrometry was used to verify this hypothesis. The composition determined for icsA and icsB is lipidA-(KDO)2-(Hep)2.PEA and lipidA-(KDO)2-(Hep)2.PEA-GlcNAc, respectively. The icsA and icsB genes thus form an operon encoding the glycosyltransferases required for chain elongation from the lipidA-(KDO)2-(Hep)2 basal structure, with IcsA first adding GlcNAc to Hep-II and IcsB subsequently adding Glc to Hep-I. Only then is completion of the lacto-N-neotetraose structure possible through the action of the lgtA–E genes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1997.tb10201.x
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  • 6
    Electronic Resource
    Electronic Resource
    Definition of meningococcal class 1 OMP subtyping antigens by monoclonal antibodies (1988)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 47 (1988), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The subtypes of meningococci are defined by antigenic determinants on the class 1 outer membrane proteins. The established subtypes, designated by P1 and a number according to the prototype reference strain on which they were first recognized by monoclonal antibodies, includes P1.2, P1.9, P1.15 and P1.16.We have investigated more prototype reference strains, using new monoclonal antibodies, and identified the new subtypes P1.1, P1.6 and P1.1,16. The P1.1,16 epitope is found on both the P1.1 and the P1.16 reference strains, but not on all P1.1 and P1.16 strains and can occur independently from the P1.1 and the P1.16 epitopes. It appears that class 1 outer membrane proteins contain at least two independent subtype-specific epitopes. For clarity, we now redefine P1.1,16 as P1.7, permitting thus the identification of strains of P1.1, P1.1,7, P1.7, P1.7,16 and P1.16 subtypes. It can clearly be expected that more class 1 outer membrane protein determinants will be recognized as more monoclonal typing antibodies are produced. The monoclonal antibodies now available to us can subtype 80–90% of group B and C meningococci; they also react with group A meningococci, but not with other Neisseriae. The immunological dissection of these subtyping antigens will improve our understanding of the relationship between components of the bacteria and the induction or prevention of disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1988.tb02366.x
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  • 7
    Electronic Resource
    Electronic Resource
    Whole-cell ELISA for typing Neisseria meningitidis with monoclonal antibodies (1987)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 48 (1987), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Large-scale screening of Neisseria meningitidis strains is necessary for epidemiological studies as well as for identifying immunologically important antigens. We have developed a new and simpler type of ELISA for this purpose. Whole bacteria from the strains being studied are coated onto PVC plates; the type and subtype are then determined by the binding of monoclonal antibodies with known specificities, detected with a protein A-conjugate. This technique is rapid and easy but still sensitive and reproducible and is thus highly suitable for screening for antigens in a relatively native state on large numbers of strains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1987.tb02626.x
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  • 8
    Electronic Resource
    Electronic Resource
    In vitro antibody response of human lymphocytes to the Haemophilus influenzae type b capsular polysaccharide (1993)
    Springer
    Springer seminars in immunopathology 15 (1993), S. 247-258 
    Details
    ISSN: 1432-2196
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00201105
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  • 9
    Electronic Resource
    Electronic Resource
    Editorial (1987)
    Springer
    Antonie van Leeuwenhoek 53 (1987), S. iii 
    Details
    ISSN: 1572-9699
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00415489
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  • 10
    Electronic Resource
    Electronic Resource
    Response of Neisseria meningitidis to iron limitation (1997)
    Springer
    Antonie van Leeuwenhoek 71 (1997), S. 129-136 
    Details
    ISSN: 1572-9699
    Keywords: iron-limitation ; lactoferrin ; meningococci ; outer membrane proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In the human body, the concentration of free iron is limiting for bacterial growth, since iron is bound to transport and storage proteins such as transferrin and lactoferrin. When grown under iron starvation, Neisseria meningitidis produces receptors for these proteins in the outer membrane. These receptors are presently being characterized at the molecular level. Here, we summarize our current knowledge of these receptors, with special emphasis on the LbpA and FrpB proteins, which are studied in our laboratories. Furthermore, the genetic and antigenic variability of these proteins and their vaccine potential are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1000179301748
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