The virulence‐associated gonococcal H.8 gene encodes 14 tandemly repeated pentapeptides
- 1 January 1989
- journal article
- research article
- Published by Wiley in Molecular Microbiology
- Vol. 3 (1), 49-55
- https://doi.org/10.1111/j.1365-2958.1989.tb00103.x
Abstract
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.This publication has 43 references indexed in Scilit:
- Lounging in a lysosome: the intracellular lifestyle of Coxiella burnetiiCellular Microbiology, 2007
- Localization of a conserved epitope and an azurin‐like domain in the H.8 protein of pathogenic NeisseriaMolecular Microbiology, 1987
- Isolation and preliminary biochemical characterization of the gonococcal H.8 antigen.The Journal of Experimental Medicine, 1986
- Cloning of the structural genes of three H8 antigens and of protein III of Neisseria gonorrhoeae.The Journal of Experimental Medicine, 1986
- Analyses of gonococcal H8 antigen. Surface location, inter- and intrastrain electrophoretic heterogeneity, and unusual two-dimensional electrophoretic characteristics.The Journal of Experimental Medicine, 1985
- DNA sequences, gene regulation and modular protein evolution in the Drosophila 68C glue gene clusterJournal of Molecular Biology, 1983
- Aberrant Migration of Lipopolysaccharide in Sodium Dodecyl Sulfate/Poyacrylamide Gel ElectrophoresisEuropean Journal of Biochemistry, 1983
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Prediction of protein conformationBiochemistry, 1974