Abstract
The protein IAs of serum-sensitive (FA635) and serum-resistant (FA638) transformants of Neisseria gonorrhoeae, which have identical pedigrees, have been shown to be different by the use of a monoclonal antibody and were also shown to be different by proteinase K cleavage and primary structural and surface peptide mapping. The difference in structure is within the surface-exposed region of the molecule. The only other difference observed between the two strains was a very slight difference in lipooligosaccharide silver staining in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. These data suggest that protein I alone or in combination with lipooligosaccharide may significantly contribute to serum resistance.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 273-276 |
| Number of pages | 4 |
| Journal | Infection and Immunity |
| Volume | 55 |
| Issue number | 1 |
| DOIs | |
| State | Published - 1987 |
| Externally published | Yes |
ASJC Scopus subject areas
- Parasitology
- Microbiology
- Immunology
- Infectious Diseases