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Gonococcal protein III. Purification and chemical characterization of the protein, and the DNA sequence of the structural gene

✍ Scribed by E. C. Gotschlich; M. S. Blake; E. J. Lytton; M. Seiff

Publisher
Springer Netherlands
Year
1987
Tongue
English
Weight
240 KB
Volume
53
Category
Article
ISSN
0003-6072

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✦ Synopsis

We have purified protein III (PIII) from several strains of gonococcus by extractions with Zwittergent 3,14 followed by cation exchange chromatography and gel filtration. The pl of 8.6 determined by isoeleetric focusing was in keeping with the high content of basic amino acids found. PIII from two strains had identical N-terminal sequence. In contrast to PIII in vivo, purified PIII was highly susceptible to proteolysis. Rabit antibodies raised with purified antigen reacted with PIII of all strains tested as well as meningococcal protein 4. Furthermore, intact gonococci or meningococci could absorb 80% of antibodies raised by immunization with the purified PIII. The structural gene of PIII was cloned and the DNA sequenced. The predicted primary structure is strongly homologous to the OmpA proteins of Enterobacteria.

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