Five structural classes of major outer membrane proteins in Neisseria meningitidis

Tsai, Chao-Ming; Frasch, Carl E.; Mocca, L F

doi:10.1128/jb.146.1.69-78.1981

Cited by 160 publications

(66 citation statements)

References 20 publications

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“…Each member of the genus Neisseria has at least one major outer membrane protein which is a porin. The meningococcus has two, a class 1 OMP and either a class 2 or 30MP [15], the gonococcus N. gonorrhoeae has either a PIA or PIB porin. In meningococci these major surface proteins are antigenically variable and have been used as targets for serological typing reagents and as candidate antigens in novel anti-meningococcal vaccines.…”

Section: Neisseria Outer Membrane Proteins (Omps)mentioning

confidence: 99%

Population genetics of a transformable bacterium: The influence of horizontal genetic exchange on the biology of Neisseria meningitidis

Maiden

1993

FEMS Microbiology Letters

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Information of the biochemistry and genetics of bacterial species, usually obtained by the study of single isolates, is enhanced by studies of populations of bacteria. Recent advances in molecular technology, particularly polymerase chain reaction-based nucleotide sequence analysis, provide powerful tools for the study of population genetics. Data obtained by such techniques indicate that, while some bacterial species have a clonal population structure, others are non-clonal or panmictic. Clonal populations are a consequence of asexual reproduction by binary fission; panmictic population structures result from 'horizontal' exchange of genetic material between clones. A consequence of horizontal genetic exchange is mosaic gene structures, recognisable by comparisons of nucleotide sequences. In transformable bacteria, for example the human pathogen Neisseria meningitidis, several different genes, including the gene encoding the class 1 outer membrane protein, a major surface antigen, are mosaics. This genetic process has implications both for vaccine design and in the interpretation of epidemiological data.

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Section: Neisseria Outer Membrane Proteins (Omps)mentioning

confidence: 99%

Population genetics of a transformable bacterium: The influence of horizontal genetic exchange on the biology of Neisseria meningitidis

Maiden

1993

FEMS Microbiology Letters

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“…When cultured in vitro each meningococcal strain has representatives of four of the five classes (1-5) of major outer membrane proteins in one of a number of combinations (Tsai et al, 1981). The differences in outer membrane protein composition are used in the classification of isolates into serotypes (class 2 and class 3 proteins; Mocca and Frasch, 1982;Frasch et a!., 1985) and subtypes (class 1 proteins; Abdillahi and Poolman, 1987).…”

Section: Introductionmentioning

confidence: 99%

Comparison of the class 1 outer membrane proteins of eight serological reference strains of Neisseria meningitidis

Maiden

Suker

McKenna

et al. 1991

Molecular Microbiology

113

117

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Primers suitable for the amplification of the gene encoding the class 1 outer membrane protein of Neisseria meningitidis by the polymerase chain reaction (PCR) were designed from published DNA sequences and used to study the gene in eight meningococcal strains of different serogroup, serotype and subtype. At high annealing stringency one product, shown to correspond to the class 1 protein gene, was amplified from each strain. For three strains an additional smaller product, provisionally identified as the gene encoding the class 3 outer membrane protein, was amplified at lower annealing stringencies. Nucleotide sequence analysis of the PCR products corresponding to the class 1 proteins established the differences in the primary structure of the proteins between each of the subtypes and other outer-membrane proteins from Neisseria spp. These differences impose constraints on possible structural models of these proteins. Most amino acid sequence variation occurred in two domains of between 8 and 17 amino acids; there was an additional region which varied mainly between classes of outer membrane protein and there were nine conserved regions. Using appropriate primers it was possible to distinguish between class 1 outer membrane protein genes from strains of different subtypes by the PCR.

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“…Thus, non-ionic detergents were effective in restoring the antigenicity of the E. coli porin protein, but not amphoteric detergents. The opposite was the case with meningococcal class 2 OM proteins (19), which function as porins in the meningococci (33). Data from the literature and those of the present study, including the observation that detection in immunoblotting of the 7.5 kD E. coli 055 OM protein was also variously affected by detergents, emphasize the importance of scrutiny to find optimal conditions when using Western blotting in the analysis of outer membrane proteins.…”

Section: Discussionmentioning

confidence: 49%

THE PORIN PROTEIN OF THE OUTER MEMBRANE OF ESCHERICHIA COLI: REACTIVITY IN IMMUNOBLOTTING, ANTIBODY‐BINDING BY THE NATIVE PROTEIN, AND CROSS‐REACTIVITY WITH OTHER ENTERIC BACTERIA

Henriksen

Mæland

1987

Acta Pathologica Microbiologica Scandinavica Series B: Microbio

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The experimental conditions for antibody‐binding by the 38.5 kD porin protein of an E. coli 055 strain in immunoblotting were investigated. A non‐ionic detergent in the buffer which contained the primary antibody was required for antibody‐binding by electroblots of the SDS‐denatured protein. Immunobloting, using antiserum absorbed with bacteria or the outer membrane (OM) of the E. coli 055 strain, showed results concordant with inaccessibility to antibodies of the 38.5 kD porin protein in its native configuration in the bacterial cells, but immunoreactivity when contained in the OM. OM from strains of different genera of the Enterobacteriaceae and antisera against these strains when used in immunoblot analyses showed that the E. coli 055 porin protein harboured antigenic determinants which are common to the various genera of the enteric bacilli. Cross‐reactivity with non‐enteric Gram‐negative bacteria was not observed.

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Five structural classes of major outer membrane proteins in Neisseria meningitidis

Cited by 160 publications

References 20 publications

Population genetics of a transformable bacterium: The influence of horizontal genetic exchange on the biology of Neisseria meningitidis

Population genetics of a transformable bacterium: The influence of horizontal genetic exchange on the biology of Neisseria meningitidis

Comparison of the class 1 outer membrane proteins of eight serological reference strains of Neisseria meningitidis

THE PORIN PROTEIN OF THE OUTER MEMBRANE OF ESCHERICHIA COLI: REACTIVITY IN IMMUNOBLOTTING, ANTIBODY‐BINDING BY THE NATIVE PROTEIN, AND CROSS‐REACTIVITY WITH OTHER ENTERIC BACTERIA

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