Baehr W, Gotschlich E C, Hitchcock P J
Laboratory of Microbial Structure and Function, National Institutes of Allergy and Infectious Diseases.
Mol Microbiol. 1989 Jan;3(1):49-55. doi: 10.1111/j.1365-2958.1989.tb00103.x.
H.8 is a virulence-associated, surface-exposed immunogenic macromolecule composed of lipid and protein, common to Neisseria gonorrhoeae and Neisseria meningitidis. The H.8 DNA sequence predicted a 6.9 kD peptide comprising 14 tandemly repeated pentameric sequences. Ten were identical: Pro, Ala, Ala, Glu, Ala. Also predicted was a lipoprotein leader consensus sequence which probably specified acylation since the Escherichia coli-expressed protein was tightly associated with lipid. Lipid appeared to contribute significantly to H.8 antigen's electrophoretic mobility. This is the first description of a prokaryotic outer membrane protein composed solely of tandem repeats. Furthermore, DNA encoding this repeat appears to have been duplicated and translocated into another neisserial gene encoding an azurin.