The periplasm of Neisseria gonorrhoeae should be similar to other Gram
-negative bacteria, but no published reports confirm this assumption.
We used a periplasmic isolation procedure developed in Escherichia col
i to release the periplasmic contents of N. gonorrhoeae. The resultant
periplasmic extract lacked lipopolysaccharide, protein markers of inn
er or outer membranes, surface-radiolabelled protein components, or ri
bosomal proteins. The periplasmic extract contained a single haem prot
ein believed to be a c-type cytochrome known to exist in the periplasm
of other Gram-negative species, and retained significant alkaline pho
sphatase activity. The dominant protein species released in the peripl
asmic extract was the gonococcal homologue of elongation factor Tu, a
major component released in similar periplasmic extracts of E. coli. T
hese data showed that the extraction procedure selectively released pe
riplasmic components and that the gonococcal periplasm was comparable
to that of E. coli. Further analysis of the gonococcal periplasm may p
rovide important insights into the physiology of this pathogen of huma
ns.