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Aeromonas Salmonicida W JOURNAL OF BACTERIOLOGY, Dec. 1985, p. 1332-1336 Vol. 164, No. 3 0021-9193/85/121332-05$02.00/0 Copyright ©D 1985, American Society for Microbiology Porphyrin Binding by the Surface Array Virulence Protein of Aeromonas salmonicida W. W. KAY,* B. M. PHIPPS, E. E. ISHIGURO, AND T. J. TRUST Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8W 2 Y2, Canada Received 5 June 1985/Accepted 26 September 1985 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 ,uM) which was absent in A- isogenic strains. Purified A-layer protein ("A protein") protein A also bound Congo red with similar affinity (Kd, 0.40 ,IM). Congo red binding was structurally specific; it was not influenced by a wide variety of compounds including amino acids and nucleotides and only weakly inhibited by structurally similar dyes. However, protoporphyrin IX and hemin were strong competitive inhibitors of Congo red binding. Protoporphyrin and hemin were bound only by A' strains (Kds of 0.41 and 0.63 ,uM, respectively). Furthermore, binding of these porphyrins was strongly inhibited by Congo red but weakly inhibited by hematoporphyrin. Purified A protein also bound protoporphyrin IX and hemin with affinities similar to those of A' cells (Kds of 0.94 and 0.41 ,uM, respectively). Aeromonas salmonicida is a pathogen of a wide variety of used as complete media. Cells were grown at 20°C to late log fish and is the causative agent of the systemic disease phase on a reciprocating shaker. Cultures were routinely furunculosis, a commercially important disease in cultured harvested by centrifugation at 10,000 x g and washed once salmonids (6). Virulent strains possess a cell surface protein with 100 mM Tris hydrochloride buffer, pH 7.0 (TB). array designated as the A-layer (23), the principal compo- CR and porphyrin binding to whole cells. Cells were nent of which is a 49,000Mr protein arranged tetragonally resuspended to an optical density at 650 nm of 1 ml-' (6 x and contiguously over the cell surface (4, 11). Isogenic 108 cells ml-') in TB in 1.5-ml Eppendorf tubes. Various strains devoid of A-layer protein ("A protein") (A-) are concentrations of CR were added and allowed to bind for 10 avirulent (8, 11), and the role of the A-layer as a virulence min at room temperature. Cells were pelleted on an Ep- factor stems at least partly from the protection if affords pendorf centrifuge by centrifugation for 1 min. CR binding to against the bactericidal activity of serum (14). However, the cells was determined subtractively by assaying the residual A-layer also endows the cell with an enhanced ability to dye in the supernatant spectrophotometrically at 480 nm. In associate with macrophages (22) and to resist the effects of a competition experiments with interfering chromogenic com- variety of proteases (unpublished data), thus potentially pounds, the chromogen was first allowed to bind to the cells facilitating the spread of the infection. for 10 min; the cells were then centrifuged for 45 s, washed Virulent A-layer-containing strains of A. salmonicida can once with TB, pelleted once more, resuspended in TB, and be detected by resistance to bacteriophage whose receptors assayed for residual chromogen contamination of the super- reside beneath the A-layer (8), or, more conveniently, by the natant. In separate tubes the cells were resuspended in TB ability of A' cells to hydrophobically bind the aromatic containing the various amounts of CR, incubated for 10 min, sulfonated diazo dye, Congo red (CR), during growth on and pelleted for 1 min as before. solid media (7). CR media have been used for some time to CR and porphyrin binding to A protein. A Protein was permit differentiation of virulent and avirulent strains of a purified from outer membrane preparations as previously variety of gram-negative bacteria (13, 15, 20), but the mo- described (16) except that it was solubilized using 2 M lecular basis of CR binding is unknown. guanidine-hydrochloride in the presence of 0.1 mM The ability of Yersinia species and Shigella flexneri to phenylmethylsulfonyl fluoride. Various concentrations of absorb CR as well as hemin has been correlated with CR or porphyrins were mixed with 70 ,ug (1.4 nmol) of pure virulence (9, 15, 17), and it has been suggested that the A protein in 0.1 M TB (pH 7.0) at a total volume of 1 ml. ability to bind CR is related to the ability to sequester iron After 5 min, duplicate 0.5-ml samples were applied to (17). In this study we expand on these observations by Sephadex G-25 columns of 0.5-ml bed volume made from a demonstrating that CR and porphyrins are both bound by the 1-ml Eppendorf pipettor tip. The pipettor tip was inserted same site on the A protein of A. salmonicida. into the lid of a precut 1.5-ml Eppendorf tube into which a separate small hole had been drilled to prevent an air-tight MATERIALS AND METHODS seal. This column plus tube was then centrifuged for 10 s at Bacterial strains. A. salmonicida A451 is an A' virulent maximum speed on an IEC clinical bench top centrifuge strain. Isogenic A- derivatives A451-3 and A451-25 are stock equipped with a swing-out head. The contents of the tube laboratory strains. A451-3 is an A- strain containing normal containing A protein plus bound ligand (700 RI) were then lipopolysaccharide, and A451-25 is a strain deficient in both assayed for ligand concentration spectrophotometrically at A protein and the lipopolysaccharide o-oligosaccharide. 480 nm for CR, 460 nm for protoporphyrin IX, and 400 nm Media and growth conditions. L broth and L agar were for hemin. All samples were run in duplicate with duplicate protein-free controls at each ligand concentration tested. * Corresponding author. Chemicals. CR dye was obtained from MCB Manufactur- 1332 VOL. 164, 1985 PORPHYRIN BINDING BY PROTEIN OF A. SALMONICIDA 1333 I_ 1.0 E 4 4' Z75 o0 0 '0 0 5 0 b\\0 0.5 {) 025 , . In 1 0 . 0 2 Z co gx _ 0~~~- 0fD LF C'g25 10 20 ~~~~~0 Ia- 1- 2 N , 0 1 2 3 4 0 5 10 15 20 -2 -1 CR (ug ml ) CR FREE (mM) FIG. 1. Effect of (NH4)2SO4 on the concentration-dependent FIG. 3. Kinetics of CR binding by purified A protein from A. binding of CR by A451 cells. Washed cells of A451 in TB were salmonicida. A protein was purified by a modification of the method incubated with CR in the presence (0) or absence (0) of 2 M of Phipps et al. (16). A protein-bound CR was separated from free (NH4)2SO4 for 10 min. Cells were collected by centrifugation, and CR by rapid centrifugation through Sephadex G-25. Inset: a the residual CR left in the supernatant was measured. Controls were Scatchard plot of the binding data where N is the stoichiometric run without cells at each CR concentration. Inset: a ieplot of the ratio of bound ligand to total protein and LF is the free-ligand same data but the total CR bound was plotted as a function of CR concentration. concentration. we examined further the binding of CR at low CR levels in ing Chemists, Inc., Cincinnati, Ohio. Protoporphyrin IX, the absence of salt. hemin, and hematoporphyrin were from Sigma Chemical Kinetics of CR binding to A' cells. A. salmonicida A451 Co., St. Louis, Mo. All other reagents were commercially (A') cells possess a kinetically distinct high-affinity binding available. of CR with an apparent Kd of 0.25 ,uM (Fig. 2). At higher CR concentrations no saturation was observed (Fig. 2, inset), RESULTS suggesting some nonspecific binding of CR to the cells at these ligand concentrations. Furthermore, A- cells of Effect of (NH4)2SO4 on CR binding to A' cells. At higher A451-3 had no high-affinity CR binding at low dye concen- CR levels, the binding of CR to A' cells was strongly trations, suggesting that A protein is responsible for binding. enhanced by the presence of 2 M (NH4)2SO4, whereas at 2 ,ug ml-' CR the added salt had little effect. At low dye Kinetics of CR binding to purified A protein. We developed a rapid dye-binding assay for CR to A protein since technical concentrations there was an apparent salt-independent bind- ing of CR which also suggested saturation kinetics (Fig. 1, problems such as dye precipitation hindered accurate bind- inset). Since salt enhances nonspecific hydrophobic binding, ing kinetics by more traditional binding assay methods such TABLE 1. Effect of various hydrophobic compounds and dyes on /0.4 0 CR binding to A. salmonicida A451 2.0 CR CR w- Compounda binding Compound" binding (%)b (%) E VI /0.2 J Phenylalanine 83.3 Bromcresol green 108.8 0 1.5 Tryptophan 97.1 Bromcresol purple 79.4 0 0 Tyrosine 97.1 Bromthymol blue 87.3 E Methionine 92.7 Nitroblue tetrazolium 117.3 c Leucine 91.3 Methylthiazole 131.8 1.0 00 "-i / °~~~0.2 0.4 0.6 tetrazolium 9 Isoleucine 79.7 Fast violet 108.0 z 00 Valine 75.4 Fast garnet 100.0 00 ATP 102.6 Fast blue 108.0 0 0.5 oo NAD 102.6 Ruthenium red 120.0 Imidazole 83.3 Evans blue 79.5 , Methylxanthine 77.3 Trypan blue 69.2 I 110.6 Procion red MXSB 63.1 - Benzidine n Ia,-2 3 Aminoacridine 131.8 Procion red HE38 69.0 v Jr__ FREE (NM) Aminonaphthylsulfonate 72.7 Coomassie brilliant blue 55.7 FIG.
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