Surface antigens of virulent strains ofAeromonas hydrophila

Dooley, James; Lallier, R.; Trust, Trevor J.

doi:10.1016/0165-2427(86)90138-8

Cited by 44 publications

(29 citation statements)

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“…It is also reported that the outer membranes of Gram-nega tive bacteria may play vital role in virulence of bacteria (Aoki and Holland, 1985;Biosca and Amaro, 1991;Buchanan and Pearce, 1979;Dooley et al, 1986). It is capable to presume that the newly synthesized OMPs of A. hydrophila take part in its virulence.…”

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“…The S-layers are assembled externally to the outer membrane, by a noncovalent interaction between the OMP and S-layer protein (Messner and Sleytr, 1992;Smith,1986). It has been demonstrated that the cell surface proteins such as OMP and S-layer protein can be virulence factors of Gram-negative bacteria (Aoki and Holland, 1985;Belland and Trust, 1984;Biosca and Amaro, 1991;Buchanan and Pearce, 1979;Chakrabarti et al, 1996;Dooley et al, 1986;Ishiguro et al, 1981;Kay et al, 1985;Mittal et al, 1980). In the case of A. hydrophila, it has been re ported that the OMP and S-layer proteins are related to its virulence (Dooley and Trust, 1988).…”

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Changes of Outer Membrane and S-layer Protein Profiles of Aeromonas hydrophila by Stravation.

1998

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It was reported in our previous paper that the starved cells of Aeromonas hydrophila were more virulent compared to the cells cultured in a medium. In this study, differences in their protein profiles were compared between the starved and cultured cells of the bacterium. Total proteins, outer membrane proteins (OMP) and S-layer proteins prepared from starved and cultured cells were analysed by SDS-PAGE. A different pattern was shown in the OMPs between the cells. Major bands of OMPs, 39, 52 and 97 kDa, were detected in the starved cells, however they were not detected in the cultured cells. In S-layer fraction, major band estimated at 91 kDa was found only in the cultured cells. Experimental result on phagocytosis of crucian carp macrophages against those cells revealed that phagocytic rate of the starved cells was lower than that of the cultured cells. These results indicate that starvation induces shifts in OMP and S-layer proteins of A. hydrophila which may enhance the resistance of the bacterium against phagocytosis of macrophages.

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Changes of Outer Membrane and S-layer Protein Profiles of Aeromonas hydrophila by Stravation.

1998

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“…Aeromonas hydrophila is a gram-negative pathogen that expresses a tetragonally arranged surface protein array on its cell surface that is composed of a single species of protein with an apparent subunit M r of 52,000 (8,9). The gene for this AhsA protein has been cloned and sequenced, and structural analysis has shown that the protein contains posttranslationally modified tyrosine amino acid residues (41).…”

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A specific PulD homolog is required for the secretion of paracrystalline surface array subunits in Aeromonas hydrophila

Thomas

Trust

1995

J Bacteriol

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Aeromonas hydrophila is an important pathogen of fish, and its high-virulence strains display a twodimensional paracrystalline layer (S-layer) on their outermost surfaces. The nucleotide sequence of a 4.1-kb region located 700 bp upstream of the A. hydrophila TF7 S-layer protein gene (ahsA) has been determined. A sequence analysis of the region revealed the presence of three complete open reading frames ending in a gene encoding a 79.8-kDa polypeptide that shows high homology to the PulD family of secretion proteins. The sequenced region displays both organizational and sequence homology to the Xanthomonas campestris pv. campestris Xps secretory system. Insertional inactivation of the spsD (S-protein secretion D) gene showed that the loss of expression of the PulD homolog coincided with the localization of the S-protein in the periplasm and the loss of the S-layer from the surface of the bacterium. However, the secretion of the enzymes hemolysin, amylase, and protease was unaffected in the mutant with the nonfunctional spsD gene, as was the export of flagella and fimbrial proteins. Southern blot analysis showed that the spsD gene was not conserved among all strains of S-protein-producing A. hydrophila or Aeromonas veronii biotype sobria. Use of the promoterless chloramphenicol acetyltransferase gene showed that unlike pulD and its homologs, spsD contains its own promoter. A. hydrophila has been shown to contain the exe operon, which is responsible for the secretion of a number of extracellular enzymes in this bacterium. A fragment of DNA was generated from the exeD gene of A. hydrophila Ah65 by PCR and was subsequently used in hybridization studies to probe the chromosome of A. hydrophila TF7. The presence of an exeD homolog in A. hydrophila TF7 was found; therefore, the spsD gene encodes a second pulD homolog that displays a high specificity for the secretion of the S-protein. This gene appears to be part of a second terminal branch of the general secretory pathway in A. hydrophila.The secretion of bacterial products is of considerable interest because of the restrictions imposed on them during their passage across cell membranes. In the case of gram-negative bacteria, extracellular secreted proteins must cross two barriers, the cytoplasmic membrane and the outer membrane, prior to extracellular release. The system responsible for the transport of most secreted polypeptides in bacteria is the general secretory pathway (GSP), the first step of which is a signal peptide-dependent mechanism requiring products of the sec genes to enable the exported product to cross the cytoplasmic membrane and then undergo processing and release into the periplasm. The movement of the extracellular secreted protein across the outer membrane is then accomplished by a more specific terminal branch of the GSP that recognizes its particular substrate(s). Previously characterized two-step secretory systems in gram-negative bacteria have recently been reviewed (33).S-layers are two-dimensional paracrystalline arrays located on the outer...

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“…The surface location and high copy number of the S-layer protein subunits also mean that the S-layer subunit protein is a major surface antigen (11,13). While little is known concerning the antigenic structure of S-layers, two different antigenic strategies of S-layer-producing bacteria have been described.…”

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Antigenic diversity of the S-layer proteins from pathogenic strains of Aeromonas hydrophila and Aeromonas veronii biotype sobria

et al. 1992

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The antigenic relatedness of paracrystalline surface array proteins with subunit molecular weights of approximately 52,000 from isolates of Aeromonas hydrophila and Aeromonas veronii biotype sobria belonging to a single heat-stable serogroup was examined. Enzyme-linked immunosorbent assay and immunoblotting with two different polyclonal antisera against surface exposed and non-surface-exposed epitopes of the S-layer protein from A. hydrophila TF7 showed that the S-layer proteins of the mesophilic aeromonads were antigenically diverse. NH2-terminal amino acid sequence analysis of four antigenically different proteins showed that while the proteins were structurally related, they differed in primary sequence. Absorption experiments with heterologous live cells showed that cross-reactive epitopes were in non-surface-exposed regions of the S-layer proteins, while absorption with homologous live cells showed that the immunodominant epitopes of the S-layer protein of strain TF7 were strain specific and exposed on the surface of the native, tetragonal array produced by this strain. Proteolytic digestion of the TF7 S-layer protein with trypsin, chymotrypsin, or endoproteinase Glu-C produced an amino-terminal peptide of approximate Mr 38,000 which was refractile to further proteolytic cleavage under nondenaturing conditions. This peptide carried the immunodominant surface-exposed region of the protein, and chemical cleavage with cyanogen bromide further mapped the portion of these surface-exposed epitopes to a peptide of approximate Mr 26,000, part of which maps within the Mr 38,000 protease-resistant NH2-terminal peptide.

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Surface antigens of virulent strains ofAeromonas hydrophila

Cited by 44 publications

References 8 publications

Changes of Outer Membrane and S-layer Protein Profiles of Aeromonas hydrophila by Stravation.

Changes of Outer Membrane and S-layer Protein Profiles of Aeromonas hydrophila by Stravation.

A specific PulD homolog is required for the secretion of paracrystalline surface array subunits in Aeromonas hydrophila

Antigenic diversity of the S-layer proteins from pathogenic strains of Aeromonas hydrophila and Aeromonas veronii biotype sobria

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