Increased cell surface hydrophobicity associated with possession of an additional surface protein by Aeromonas salmonicida
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چکیده
منابع مشابه
Immunoglobulin binding by the regular surface array of Aeromonas salmonicida.
The cell surface of Aeromonas salmonicida is covered by a regular surface array composed of a single species of protein, the A-protein (Phipps, B. M., Trust, T. J., Ishiguro, E. E., and Kay, W. W. (1983) Biochemistry 22, 2934-2939). The array, known as the A-layer, is the key virulence factor for this organism. Cells containing the A-layer specifically bound rabbit IgG and human IgM with high a...
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Congo red binding by virulent A-layer-containing (A+) and avirulent A-layer-deficient (A-) strains of Aeromonas salmonicida was examined. Congo red binding to A+ cells was enhanced by salt and thus hydrophobically driven, but at low Congo red concentrations binding was salt independent. Congo red was bound by A+ cells by a kinetically distinct mechanism (Kd, 0.25 microM) which was absent in A- ...
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Some properties of compounds in degrading bacteria are required for biodegradation of contaminants to higher performance. Those strains which have a high percentage of these features are more effective at biodegradation. The present experiments were designed to measure these parameters. In this study, measurement of cell surface hydrophobic-degrading bacteria was designed which oil was separate...
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Some properties of compounds in degrading bacteria are required for biodegradation of contaminants to higher performance. Those strains which have a high percentage of these features are more effective at biodegradation. The present experiments were designed to measure these parameters. In this study, measurement of cell surface hydrophobic-degrading bacteria was designed which oil was separate...
متن کاملStructure of the tetragonal surface virulence array protein and gene of Aeromonas salmonicida.
The paracrystalline surface protein array of the pathogenic bacterium Aeromonas salmonicida is a primary virulence factor with novel binding capabilities. The species-specific structural gene (vapA) for this array protein (A-protein) was cloned into lambda gt11 but was unstable when expressed in Escherichia coli, undergoing an 816-base pair deletion due to a 21-base pair direct repeat within th...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 1984
ISSN: 0378-1097
DOI: 10.1016/0378-1097(84)90300-8