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Isolation and partial characterization of the reduction-modifiable protein of Neisseria gonorrhoeae
The Journal of Experimental Medicine
|November 1, 1986
Abstract:
We have isolated and purified the reduction-modifiable protein (protein III) from several strains of Neisseria gonorrhoeae. We have found them to be basic proteins (pI 8.6) and virtually identical. A similar but not identical protein was isolated from a meningococcal strain. Antibodies raised against this purified protein would absorb to whole bacteria, confirming that the protein is exposed on the surface of the organism.
Insights
Researchers isolated a surface protein, termed protein III, from Neisseria gonorrhoeae strains. This basic protein is nearly identical across strains and exposed on the bacterial surface.
Area of Science:
- Microbiology
- Bacterial Pathogenesis
Background:
- Neisseria gonorrhoeae is a significant human pathogen.
- Understanding bacterial surface structures is crucial for developing diagnostics and therapeutics.
Purpose of the Study:
- To isolate and characterize surface proteins from Neisseria gonorrhoeae.
- To investigate the presence of similar proteins in related species like Neisseria meningitidis.
Main Methods:
- Protein purification techniques were employed to isolate reduction-modifiable protein (protein III).
- Isoelectric focusing was used to determine protein properties (pI 8.6).
- Antibody-based assays were performed to confirm surface exposure.
Main Results:
- A basic protein (pI 8.6), designated protein III, was purified from multiple Neisseria gonorrhoeae strains and found to be highly conserved.
- A similar, though not identical, protein was identified in Neisseria meningitidis.
- Antibodies against purified protein III bound to whole bacteria, indicating surface localization.
Conclusions:
- Protein III is a conserved, surface-exposed protein in Neisseria gonorrhoeae.
- This protein represents a potential target for therapeutic and diagnostic strategies against gonorrhea.