Opacity genes in Neisseria gonorrhoeae: Control of phase and antigenic variation

  title={Opacity genes in Neisseria gonorrhoeae: Control of phase and antigenic variation},
  author={Anne Stern and Melissa Brown and Peter Nickel and Thomas F. Meyer},

The control mechanism of opacity protein expression in the pathogenic Neisseriae

The expression of Neisseria gonorrhoeae opacity protein shows frequent phase transitions and part of the leader peptide of all Op's is encoded by repetitive CTTCT pentameric units, the so-called coding repeat (CR).

Common mechanism controlling phase and antigenic variation in pathogenic Neisseriae

Using opa‐specific oligonucleotides as probes in genomic blots, Op‐related gene sequences (opr) in N. meninglitidis and N. lactamica are detected, suggesting a translational control mechanism identical to that of the opa genes in gonococci.

Genome plasticity in Neisseria gonorrhoeae.

An analysis of the chromosomal structure of a defined lineage of Neisseria gonorrhoeae strain MSl1 pilin variants reveals the occurrence of large rearrangements, including the amplification of a 26 kb region and an inversion involving more than a third of the chromosome.

Promoter strength influences phase variation of neisserial opa genes

Transcription of the opa gene family of N. gonorrhoeae MS11mk is analysed to provide an explanation for the favoured expression of specific Opa proteins and indicate that expression of opa genes may be regulated at the level of transcription.

Variable expression of the Opc outer membrane protein in Neisseria meningitidis is caused by size variation of a promoter containing poly‐cytidine

Opa proteins of Neisseria meningitidis exhibit translational phase variation via addition or deletion of repetitive coding repeat units within the DNA encoding the protein leader sequence, which may have evolved because the Opc protein enables meningococcal invasion and is immunogenic.

Recombination among Protein II genes of Neisseria gonorrhoeae generates new coding sequences and increases structural variability in the Protein II family

The DNA sequences of three P.II genes showed that they shared a conserved framework, with two short hypervariable (HV) regions being responsible for most of the differences among them, and it was demonstrated that unique epitopes recognized by the MAbs were at least partially encoded by one of the HV regions.

Genetic locus for the biosynthesis of the variable portion of Neisseria gonorrhoeae lipooligosaccharide

Three of the LOS biosynthetic enzymes are potentially susceptible to premature termination by reading frame changes and it is likely that these structural features are responsible for the high-frequency genetic variation of gonococcal LOS.

Genetics of surface protein variation in Neisseria gonorrhoeae

  • G. MurphyJ. Cannon
  • Biology, Medicine
    BioEssays : news and reviews in molecular, cellular and developmental biology
  • 1988
Recent studies have shown that the gonococcus uses novel and complex mechanisms, of types not described previously, to store different versions of genetic information for surface proteins, and to regulate expression of those genes.

Cloning and characterisation of the Neisseria gonorrhoeaearoB gene

The 3-dehydroquinate synthetase (aroB) of Neisseria gonorrhoeae has been cloned by functional complementation of an Escherichia coli aroB mutant, indicating that the gene is responsible for the auxotrophic phenotype.



Variations in surface protein composition associated with virulence properties in opacity types of Neisseria gonorrhoeae.

The results show that the heat-modifiable surface proteins are important virulence attributes of the gonococcus: this must be considered in the selection of strains for vaccine trials.

Pilus genes of Neisseria gonorrheae: chromosomal organization and DNA sequence.

Two regions of the Neisseria gonorrheae genome, pilE1 and pilE2, which are involved in pilus expression, are mapped, which indicate that these two loci carry sequences necessary for pilin production when cells are in the piliated P+ state.

Purification and partial characterization of the opacity-associated proteins of Neisseria gonorrhoeae

A method is described to isolate and purify the opacity-associated proteins from Neisseria gonorrhoeae, which are very basic with isoelectric points varying between 9.0 to 10.0.

Antigenic variation of outer membrane protein II in colonial variants of Neisseria gonorrhoeae P9.

Despite their considerable structural homology, different protein II species from colonial variants of the same strain showed little cross-reactivity with specific anti-protein II sera, thus demonstrating the considerable variation in that part of the antigen which is exposed on the surface of the gonococcus and is closely involved in pathogenic mechanisms.

Comparative virulence of opacity variants of Neisseria gonorrhoeae strain P9

Evaluated invasive properties of nine variants of Neisseria gonorrhoeae strain P9 showed increased ability to kill the target cells compared with the prototype P9-1, and enhanced attachment was exhibited by both piliated and some nonpiliated variants.

Structural comparison of Neisseria gonorrhoeae outer membrane proteins

Outer membranes from opaque colonia variants of Neisseria gonorrhoeae P9 contain a major outer membrane protein (protein I) together with one or more of a series of heat-modifiable proteins (proteins

Effects of proteolytic enzymes on the outer membrane proteins of Neisseria gonorrhoeae

The data suggested the presence of an endogenous gonococcal enzyme that appeared to degrade proteins I and II into fragments resembling the fragments resulting from the action of chymotrypsin, and suggests how these proteins may be arranged in intact membranes.