Hydrophobicity, Adhesion, and Surface-Exposed Proteins of Gliding Bacteria

AUTOR(ES)

Sorongon, Maria L.

RESUMO

The cell surface hydrophobicities of a variety of aquatic and terrestrial gliding bacteria were measured by an assay of bacterial adherence to hydrocarbons (BATH), hydrophobic interaction chromatography, and the salt aggregation test. The bacteria demonstrated a broad range of hydrophobicities. Results among the three hydrophobicity assays performed on very hydrophilic strains were quite consistent. Bacterial adhesion to glass did not correlate with any particular measure of surface hydrophobicity. Several adhesion-defective mutants of Cytophaga sp. strain U67 were found to be more hydrophilic than the wild type, particularly by the BATH assay and hydrophobic interaction chromatography. The very limited adhesion of these mutants correlated well with hydrophilicity as determined by the BATH assay. The hydrophobicities of several adhesion-competent revertants ranged between those of the wild type and the mutants. As measured by the BATH assay, starvation increased hydrophobicity of both the wild type and an adhesion-defective mutant. During filament fragmentation of Flexibacter sp. strain FS-1, marked changes in hydrophobicity and adhesion were accompanied by changes in the arrays of surface-exposed proteins as detected by an immobilized radioiodination procedure.

Documentos Relacionados

• Identification of surface-exposed B-cell epitopes on high molecular-weight adhesion proteins of nontypeable Haemophilus influenzae.
• Surface-exposed and antigenically conserved determinants of outer membrane proteins of Branhamella catarrhalis.
• Surface-exposed antigenic cleavage fragments of Neisseria gonorrhoeae proteins 1A and IB.
• Effect of proteolytic cleavage of surface-exposed proteins on infectivity of Chlamydia trachomatis.
• A family of surface-exposed proteins of 20 kilodaltons in the genus Borrelia.