Structural comparison of Neisseria gonorrhoeae outer membrane proteins.

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Abstract
Outer membranes from opaque colonial variants of N. gonorrhoeae P9 contain a major outer membrane protein (protein I) together with 1 or more of a series of heat-modifiable proteins (proteins II). Proteins I, II and IIa were isolated by detergent extraction of outer membranes. Amino acid analysis showed proteins II and IIa to have a very similar composition. Cyanogen bromide cleavage of proteins II and IIa produced a pair of fragments with identical MW and a pair which differed by an amount (0.5K) equivalent to the difference between the intact proteins. Tryptic peptide maps of 125I-labeled proteins II, IIa and IIb showed many similarities, with only a few peptides unique to any 1 protein. Peptide maps of protein IIa from cells which were surface labeled showed that the unique peptides were exposed on the surface. The heat-modifiable proteins appear to form a family of proteins with closely related structure probably differing in that part which is exposed on the bacterial surface.