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PubMed2002

Structure of the O-polysaccharide of Aeromonas hydrophila O:34; a case of random O-acetylation of 6-deoxy-L-talose.

The O-polysaccharide of Aeromonas hydrophila O:34 was obtained by mild-acid degradation of the lipopolysaccharide and studied by chemical methods and NMR spectroscopy before and after O-deacetylation. The polysaccharide was found to contain D-Man, D-GalNAc and 6-deoxy-L-talose (L-6dTal), and the following structure of the tetrasaccharide repeating unit was established [carbohydrate structure see text] where 6dTal(I) is O-acetylated stoichiometrically at position-2 and 6dTal(II) carries no, one or two O-acetyl groups at any positions.

Acetylation↗
PubMed1996

Structural studies of the O-antigenic polysaccharide from an Aeromonas caviae strain.

The structure of the O-antigenic polysaccharide from a strain of Aeromonas caviae, isolated from the stools of a patient with diarrhoea, has been investigated. Sugar analysis, methylation analyses, and a uronic acid degradation together with NMR spectroscopy were the principal methods used. The sequence of the sugar residues could be determined by NOESY and HMBC experiments. It is concluded that the polysaccharide is composed of pentasaccharide repeating units with the following structure: [sequence: see text]

Aeromonas↗
PubMed2000

Kinetic and spectroscopic characterization of native and metal-substituted beta-lactamase from Aeromonas hydrophila AE036.

Two metal ion binding sites are conserved in metallo-beta-lactamase from Aeromonas hydrophila. The ligands of a first zinc ion bound with picomolar dissociation constant were identified by EXAFS spectroscopy as one Cys, two His and one additional N/O donor. Sulfur-to-metal charge transfer bands are observed for all mono- and di-metal species substituted with Cu(II) or Co(II) due to ligation of the single conserved cysteine residue. Binding of a second metal ion results in non-competitive inhibition which might be explained by an alternative kinetic mechanism. A possible partition of metal ions between the two binding sites is discussed.

Aeromonas hydrophila↗
PubMed1995

Molecular analysis of an A-protein secretion mutant of Aeromonas salmonicida reveals a surface layer-specific protein secretion pathway.

The Aeromonas salmonicida Tn5 mutant, A449-TM1, is unable to secrete the surface layer protein (A-protein) through the outer membrane. Immunogold labeling of thin sections of A449-TM1, with polyclonal antisera against the A-protein, showed the accumulation of large quantities of A-protein in an enlarged periplasm. The majority of the labeled A-protein could be seen at the poles of the cells. The ability of A449-TM1 to secrete other extracellular proteins such as hemolysin and protease was not impaired by the Tn5 insertion, which indicates that the mutation in A449-TM1 interferes with a secretion pathway specifically for the translocation of the A-protein through the outer membrane. The mutant, A449-TM1, was shown to be avirulent for fish. A cosmid clone from a gene library of A449-TM1, which contains the Tn5 insertion from the chromosome, was used to identify a 1.4 kb SaII/ClaI fragment from immediately adjacent to the Tn5 insertion. This fragment was used to identify and clone a 4 kb HindIII fragment from a chromosomal DNA digest from the wild-type strain, A449. DNA sequence analysis of this clone identified an open reading frame (ORF) of 1656 bp. The deduced product of this ORF showed sequence similarity to a family of ATP-binding secretion proteins, but appeared to be phylogenetically distinct from these proteins, consistent with its participation in a secretory pathway specific for surface layer protein.

Aeromonas↗
PubMed2002

Survival of an Aeromonas hydrophila in an artificial mineral water microcosm.

The survival capacity of an Aeromonas hydrophila strain (named SB14) isolated from mineral water was investigated in an artificial mineral water microcosm. The bacterial count of this microorganism was compared with two strains of other species from aquatic environments (Pseudomonas fluorescens SSD and Pseudomonas putida SSC) and a bacterium indicative of faecal pollution (Escherichia coli ATCC 25922). Among the strains, all added to sterile Pyrex glass flasks (1 l) to yield a final bacterial count of about 5 x 10(6) CFU/ml, A. hydrophila SB14 showed a quite strong survival capacity (150 days), even though the Pseudomonas strains were better adapted to this habitat (more than 240 days). E. coli ATCC 25922 was the least well fitted to survive and was no longer detected after 70 days. When A. hydrophila SB14 was inoculated together with one or two of the above strains, its survival appeared to be dependent on interaction with other organisms. A marked decrease in survival by 30 days, possibly due to antagonistic interaction, was observed when this microorganism was associated with E. coli ATCC 25922, and an increase by 30 and 60 days, possibly due to commensalic interaction, was obtained when A. hydrophila SB14 was inoculated with P. fluorescens SSD or P. putida SSC, respectively.

Aeromonas hydrophila↗
PubMed1997

Expression and characterization of the recombinant gene encoding chitinase from Aeromonas caviae.

The gene encoding a chitinase from Aeromonas caviae was cloned by PCR techniques. Its recombinant gene expression was performed using pET20b(+) in Escherichia coli BL21 (DE3). The recombinant chitinase with the extra 33 and 13 amino acids in its N- and C-termini, respectively, was purified to near homogeneity using His-Tag affinity chromatography. The recombinant chitinase was found to be present in both the culture medium and the cytoplasm. A single protein band on the native polyacrylamide gel was confirmed by both the activity staining and protein staining. The optimum pH and temperature of the recombinant chitinase were determined to be 6.25-6.5 and 42.5 degrees C, respectively. It was stable within the pH range of 5-7. Significant activity stimulation by Cu2+ and inhibition by Fe3+ and Hg2+ were observed. Detergents such as SDS and Triton X-100 strongly inhibited the enzyme activity. Substrates such as 4-methylumbelliferyl-N,N'-diacetylchitobioside and 4-methylumbelliferyl-N,N',N"-triacetylchitotriose were hydrolyzed by the recombinant chitinase; however, 4-methylumbelliferyl-N-acetylglucosaminide was not cleaved during the activity assay periods. When chitin power was suspended in buffer with the chitinase (pH 6.5 and 42.5 degrees C), N-acetylchitooligosaccharides [(GlcNAc)n, n = 1-4] were detected at 24 h.

Aeromonas↗
PubMed2003

The effect of intraperitoneally administered recombinant IL-1beta on immune parameters and resistance to Aeromonas salmonicida in the rainbow trout (Oncorhynchus mykiss).

The present work provides the first information concerning the immunostimulatory activity of trout recombinant interleukin-1 beta (rIL-1beta) in vivo. The predicted rainbow trout mature IL-1beta peptide was produced as a recombinant protein in Escherichia coli. Optimal migration of peritoneal leucocytes and rIL-1beta induced phagocytosis occurred following intraperitoneal injection of 1 microg of the recombinant protein. Moreover, systemic IL-1beta, COX-2 and lysozyme II gene expression was enhanced following >or=1 microg rIL-1beta administration. Finally, resistance to Aeromonas salmonicida, the causative agent of furunculosis, was augmented at early times (2 days) post-injection of 1 microg rIL-1beta.

Adjuvants, Immunologic↗
PubMed2002

A global non-conjugative Tet C plasmid, pRAS3, from Aeromonas salmonicida.

Two 11.8 kb non-conjugative, but mobilizable R plasmids designated pRAS3.1 and pRAS3.2 were isolated from Aeromonas salmonicida subspecies salmonicida and atypical A. salmonicida, respectively. Differences between the plasmids were of minor extent and they are considered as being variants of the same plasmid, pRAS3. The genes repA, repB, mobA, mobC, mobD, and mobE were organized similar to corresponding genes in the small, mobilizable plasmid pTF-FC2 isolated from Acidithiobacillus ferrooxidans (previously Thiobacillus ferrooxidans). The nucleotide identity between these genes from pRAS3.1 and pTF-FC2 ranged from 89.5 to 98.2%. The tetA(C), tetR(C), and approximately 960 base pairs adjacent to tetR(C) were highly similar to the nucleotide sequence in pSC101. Plasmid pRAS3 was also found in a Scottish A. salmonicida strain, and appears to be identical to the R plasmid pJA8102-2 isolated from A. salmonicida in Japan.

Aeromonas↗
PubMed2003

Three small, cryptic plasmids from Aeromonas salmonicida subsp. salmonicida A449.

The nucleotide sequences of three small (5.2-5.6 kb) plasmids from Aeromonas salmonicida subsp. salmonicida A449 are described. Two of the plasmids (pAsa1 and pAsa3) use a ColE2-type replication mechanism while the third (pAsa2) is a ColE1-type replicon. Insertions in the Rep protein and oriV region of the ColE2-type plasmids provide subtle differences that allow them to be maintained compatibly. All three plasmids carry genes for mobilization (mobABCD), but transfer genes are absent and are presumably provided in trans. Two of the plasmids, pAsa1 and pAsa3, carry toxin-antitoxin gene pairs, most probably to ensure plasmid stability. One open reading frame (ORF), orf1, is conserved in all three plasmids, while other ORFs are plasmid-specific. A survey of A. salmonicida strains indicates that pAsa1 and pAsa2 are present in all 12 strains investigated, while pAsa3 is present in 11 and a fourth plasmid, pAsal1, is present in 7.

Aeromonas↗
PubMed1997

Enhancement of the resistance of tilapia and grass carp to experimental Aeromonas hydrophila and Edwardsiella tarda infections by several polysaccharides.

Efficacies of eleven polysaccharides including Bar (glycan extracted from Barley), curdlan, Dex (dextran sulfate), inulin, krestin, laminaran, levan, PO (glycan extracted from Pleurotus ostreatus), scleroglucan, YG (yeast glucan), and zymosan, in the protection of tilapia, Tilapia aureus P., and grass carp, Ctenopharyngodon idellus, against bacterial infections in vivo were examined. Four glycans. namely, Bar, krestin, scleroglucan, and zymosan were observed to significantly increase the survival rates of tilapia (80, 60, 70, and 60%) and grass carp (60, 70, 90, and 60%) (p < 0.05) after injection with Aeromonas hydrophila. The above mentioned four glycans were also found to raise the survival rates of tilapia (70, 60, 80, and 50%) and grass carp (50, 50, 70, and 50%) (p < 0.05) significantly after infection with Edwardsiella tarda. Moreover, Bar, curdlan, krestin, scleroglucan, and zymosan were also found to significantly increase the number of NBT-positive staining cells (p < 0.05), which might indicate that to activate non-specific phagocytes in fish is one of the antibacterial mechanisms of polysaccharides.

Adjuvants, Immunologic↗
PubMed2000

Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinethiol: kinetic and spectroscopic characterization of a slow, tight-binding inhibitor-enzyme complex.

The peptide inhibitor L-leucinethiol (LeuSH) was found to be a potent, slow-binding inhibitor of the aminopeptidase from Aeromonas proteolytica (AAP). The overall potency (K(I)*) of LeuSH was 7 nM while the corresponding alcohol L-leucinol (LeuOH) was a simple competitive inhibitor of much lower potency (K(I) = 17 microM). These data suggest that the free thiol is likely involved in the formation of the E x I and E x I* complexes, presumably providing a metal ligand. In order to probe the nature of the interaction of LeuSH and LeuOH with the dinuclear active site of AAP, we have recorded both the electronic absorption and EPR spectra of [CoCo(AAP)], [CoZn(AAP)], and [ZnCo(AAP)] in the presence of both inhibitors. In the presence of LeuSH, all three Co(II)-substituted AAP enzymes exhibited an absorption band centered at 295 nm, characteristic of a S --> Co(II) ligand-metal charge-transfer band. In addition, absorption spectra recorded in the 450 to 700 nm region all showed changes characteristic of LeuSH and LeuOH interacting with both metal ions. EPR spectra recorded at high temperature (19 K) and low power (2.5 mW) indicated that, in a given enzyme molecule, LeuSH interacts weakly with one of the metal ions in the dinuclear site and that the crystallographically identified mu-OH(H) bridge, which has been shown to mediate electronic interaction of the Co(II) ions, is likely broken upon binding LeuSH. EPR spectra of [CoCo(AAP)]-LeuSH, [ZnCo(AAP)]-LeuSH, and [Co_(AAP)]-LeuSH were also recorded at lower temperature (3.5-4.0 K) and high microwave power (50-553 mW). These signals were unusual and appeared to contain, in addition to the incompletely saturated contributions from the signals characterized at 19 K, a very sharp feature at g(eff) approximately 6.5 that is characteristic of thiolate-Co(II) interactions. Combination of the electronic absorption and EPR data indicates that LeuSH perturbs the electronic structure of both metal ions in the dinuclear active site of AAP. Since the spin-spin interaction seen in resting [CoCo(AAP)] is abolished upon the addition of LeuSH, it is unlikely that a mu-S(R) bridge is established.

Aeromonas↗
PubMed2001

Induction of inflammatory cytokines by extracellular products and LPS of the fish pathogen Aeromonas salmonicida ssp. achromogenes in mice and mouse cell cultures.

Balb/c mice, injected i.p. with extracellular products (ECP) of Aeromonas salmonicida subsp. achromogenes (Asa), displayed symptoms similar to toxic shock syndrome. The LD(50) observed was between 1.5 and 2.0 microg g(-1) and the mice died within 19 h. Four inflammatory cytokines were measured in mice receiving sublethal ECP doses. TNF-alpha and IL-6 showed a sharp peak in the serum while IL-1 beta and IL-2 were not detected. When peritoneal macrophages were cultivated in the presence of ECP, AsaP1 (a toxic caseinolytic metallo-protease purified from ECP) or LPS, all cultures produced TNF-alpha, IL-6 and IL-1 beta. The same antigens were mitogenic in spleen cell cultures. Furthermore, IL-2 production, which is a normal T-cell response to ConA stimulation, was downregulated in spleen cell cultures from mice injected with ECP.

Aeromonas↗
PubMed2001

Antibody response in salmonids against the 70 kDa serine protease of Aeromonas salmonicida studied by a monoclonal antibody-based ELISA.

An antigen-capture enzyme-linked immunosorbent assay (cELISA) based on monoclonal antibodies (mAb) was set up and evaluated for selective detection of salmonid antibody responses to the antigen P1, which is a weakly immunogenic exoprotease of typical Aeromonas salmonicida. This new assay permits a specific determination of anti-protease-antibodies, without antigen purification. Serum antibodies induced by the strongly immunogenic lipopolysaccharide could reliably be discriminated from anti-P1-antibodies. Antibody titres of 45 experimental antisera recorded by cELISA were moderately correlated with titres determined by routinely used indirect ELISA (iELISA) by detecting partially different antibody populations (r=0.753). Substitutions of immunoreactants and confirmatory immunoblotting strongly suggest that the mAb-based assay selectively recognises antibodies directed to epitopes of native protease. A conjugate of inhibited protease and cationized bovine serum albumin (cBSA) was found to engender a significant anti-protease-response in three salmonid species (P<0.05), whereas the unconjugated antigen and Apoject 1-Fural were proved to be ineffective. Recorded specific antibody titres were as high as 1:381,400, indicating a considerable enhanced immunogenicity of cBSA-conjugated P1 and high assay sensitivity. The established cELISA offers a promising approach to further improvement of monitoring fish humoral immune response to surface accessible epitopes of the immunosuppressive exoprotease, P1, and to scrutinize its protective significance.

Aeromonas↗
PubMed2002

In vitro stepwise autoprocessing of the proform of pro-aminopeptidase processing protease from Aeromonas caviae T-64.

PA protease (pro-aminopeptidase processing protease) is an extracellular zinc metalloprotease produced by the Gram-negative bacterium Aeromonas caviae T-64. The 590-amino-acid precursor of PA protease is composed of a putative 19-amino-acid signal sequence, a 165-amino-acid N-terminal propeptide, a 33 kDa mature protease domain and an 11 kDa C-terminal propeptide. The proform of PA protease, which was produced as inclusion bodies in Escherichia coli, was subjected to in vitro refolding. It was revealed that the processing of the proform involved a stepwise autoprocessing mechanism. Firstly, the N-terminal propeptide was autocatalytically removed on completion of refolding and secondly, the C-terminal propeptide was autoprocessed after the degradation of the N-terminal propeptide. Both the N- and C-terminal propeptides existed as intact peptides after their successive removal, and they were subsequently degraded gradually. The degradation of the N-terminal propeptide appears to be the rate-limiting step in the maturation of the proform of PA protease.

Aeromonas↗
PubMed1999

Molecular cloning and expression in Escherichia coli of the extracellular endoprotease of Aeromonas caviae T-64, a pro-aminopeptidase processing enzyme(1).

PA protease (pro-aminopeptidase processing protease) activates the pro-aminopeptidases from Aeromonas caviae T-64 and Vibrio proteolytica by removal of their pro-regions. Cloning and sequencing of the PA protease gene revealed that PA protease was translated as a preproprotein consisting of four domains: a signal peptide; an N-terminal propeptide; a mature region; and a C-terminal propeptide. The deduced amino acid sequence of the PA protease precursor showed significant homology with several bacterial metalloproteases. Expression of the PA protease gene in Escherichia coli indicated that the N-terminal propeptide of the PA protease precursor is essential to obtain the active form of the protease. The N- and C-terminal propeptides of the expressed pro-PA protease were processed autocatalytically.

Aeromonas↗
PubMed2001

Hatchery-level predictive values for infectious pancreatic necrosis virus and Aeromonas salmonicida in Ontario, Canada.

The probability and uncertainty of correctly classifying the IPNV and Aeromonas salmonicida status of fish-rearing and natural sites in Ontario were estimated through Monte Carlo simulations. Propagating several uncertain inputs showed the extent to which natural variability and our present lack of knowledge affect the probability of site misclassification. For the scenarios investigated, the site-level negative predictive values (SNPVs) were high and fairly constant. The site-level positive predictive values (SPPVs) - given a test specificity ranging between 0.999 and 1.0 - were much lower, more variable, and highly affected by cut-off point and sample size. Substantial uncertainty resides in classifying the pathogen status of test-positive sites, whereas much less uncertainty resides in classifying pathogen status of test-negative sites.

Aeromonas↗
PubMed2001

Host factors associated with the detection of Aeromonas salmonicida and Yersinia ruckeri in Ontario, Canada government fish hatcheries.

This paper presents an epidemiological investigation of Ontario Ministry of Natural Resources Fish Health Laboratory data from 1981 to 1997, to determine whether fish species and age were associated with lot-level detection of Aeromonas salmonicida and Yersinia ruckeri in hatchery fish. In stepwise logistic regression, the species brook trout and back-cross (lake trout crossed with the hybrid "splake") were more likely to test A. salmonicida-positive compared to all other species reared in the hatcheries. Similarly, the species brook trout was significantly more likely to test Y. ruckeri-positive compared to all other species. For both pathogens, the 1-5-month age group was associated significantly with detection. These findings suggest that purposive sampling of higher-risk fish lots could increase the likelihood of detecting both study pathogens.

Aeromonas↗
PubMed2002

Immuno-capture PCR for detection of Aeromonas hydrophila.

In this report, we describe the use of universal primer PCR (UPPCR) for the detection of 16S ribosomal RNA (rRNA) genes from Aeromonas hydrophila captured by anti-A. hydrophila antibody coupled to a microplate. The approach combining immuno-capture with UPPCR provides a quick, sensitive, and reproducible way for the detection of bacterial cells.

Aeromonas hydrophila↗