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M Jacques

Publications and source records attributed to M Jacques.

At least 55 records · Page 3Linked to original sources
PubMed1995

Streptococcus pneumoniae types 19A and 19F and Streptococcus suis capsular type 8 share common capsular epitopes.

Two monoclonal antibodies (MAbs) to Streptococcus pneumoniae types 19A and 19F were tested with the 35 reference strains and 334 field strains of Streptococcus suis by dot blotting. Both MAbs reacted with the capsular type 8 reference strain, and one reacted with 69% and one reacted with 100% of 81 S. suis capsular type 8 field strains tested. Epitopes recognized by both MAbs are capsular in origin.

Antigens, Bacterial↗
PubMed1995

Interaction with pig ileal explants of Escherichia coli O45 isolates from swine with postweaning diarrhea.

We have previously observed that Escherichia coli O45 isolates from swine postweaning diarrhea (PWD) induced attaching-effacing (A/E) lesions in experimentally inoculated gnotobiotic piglets. In the present work, ileal explant culture has been used as an in vitro model for the study of the development of A/E lesions due to these isolates. The characteristic intimate bacterial attachment and microvilli effacement with cupping and pedestal formation, identical to that observed in gnotobiotic piglets, was demonstrated in pig ileal explants inoculated with O45 E. coli isolates. The initial attachment of bacteria to the enterocytes was observed from 2 to 4 h postinoculation (PI) and full development of A/E lesions was observed within 8 h PI. In this model, we observed that 22 of 25 eaeA-positive O45 isolates induced A/E lesions. However, A/E lesions were not observed for any of 7 eaeA-negative O45 isolates. Thus, we describe a useful in vitro model for the study of A/E capacity of porcine E. coli. Use of this model has enabled us to demonstrate the relatedness of the eaeA gene to A/E capability among porcine O45 E. coli from PWD.

Animals↗
PubMed1995

Growth of Serpulina (Treponema) hyodysenteriae under iron-restricted conditions.

Reference strains of Serpulina hyodysenteriae expressed at least three iron-regulated proteins with apparent molecular masses of > 200, 134, and 109 kDa when grown under iron-restricted conditions. Cells of S. hyodysenteriae grown under these conditions also showed increased outer membrane bleb formation when examined by electron microscopy after negative staining. S. hyodysenteriae did not use the 2 most common types of siderophore, namely catechol and hydroxamate. Western blotting with serum from a pig experimentally infected with S. hyodysenteriae B204 indicated that the 109-kDa major iron-regulated protein was expressed in vivo and was conserved among all strains tested.

Animals↗
PubMed1994

Increase of capsular material thickness following in vivo growth of virulent Streptococcus suis serotype 2 strains.

Protein profile and capsular material thickness of Streptococcus suis serotype 2 strains were compared after in vitro and in vivo growth. Three virulent and one avirulent strains were used. These strains were grown in Brain Heart Infusion (BHI) broth, cells were collected by centrifugation, resuspended in a sterile saline solution and injected in diffusion chambers. The devices were then inserted in rat abdomens for 17 h. In vitro grown strains were also inoculated into fresh BHI broth and cultivated for 17 h at 37 degrees C. In vivo as well as in vitro grown bacteria were harvested by centrifugation, processed in a French pressure cell, treated with lysozyme and centrifuged to collect cell proteins for SDS-PAGE analysis. Transmission electron microscopy using polycationic ferritin labeling to stabilize capsular material was also carried out. No significant modification was noted in the protein profile for any strain after in vivo growth except for a 39 kDa protein of one virulent strain. On the other hand, an increase in thickness of capsular material was noted for the three in vivo grown virulent strains while no change was noted for the avirulent strain. This increase in capsular material thickness of virulent strains was accompanied by an increased resistance to killing by pig polymorphonuclear leukocytes. The capacity to produce more capsular material in vivo seems to be an attribute of some virulent S. suis serotype 2 strains.

Animals↗
PubMed1994

Modulation of Pasteurella multocida capsular polysaccharide during growth under iron-restricted conditions and in vivo.

Addition of the iron chelators 2,2'-dipyridyl, deferoxamine mesylate or apo-transferrin to culture media affected the composition and the morphology of Pasteurella multocida cells. Cells grown under iron-restricted conditions expressed iron-regulated proteins and, in addition, iron deprivation markedly reduced the amount of capsular material covering the cells of P. multocida. The addition of iron neutralized the effect of these chelators on capsule production. Cells of P. multocida grown under iron-restricted conditions were more labelled by gold particles coated with polymyxin which is known to interact with the lipid A-core region of lipopolysaccharides, and showed increased affinity for porcine respiratory tract mucus than cells grown under iron-sufficient conditions. Bacterial cells grown in vivo in peritoneal chambers in rats were also only covered by a thin layer (15-20 nm) of capsular material. Although the capsule is believed to be an important virulence factor, our data indicate that under iron-restricted conditions, such as those encountered in vivo, P. multocida may not be heavily encapsulated.

Animals↗
PubMed1994

Virulence properties and attaching-effacing activity of Escherichia coli O45 from swine postweaning diarrhea.

Escherichia coli O45 isolates associated with swine postweaning diarrhea in Québec were characterized with respect to virulence determinants genetically and investigated for their attaching and effacing (A/E) activities by experimental inoculation of gnotobiotic piglets and by the HEp-2 cell adherence assay. All of 32 isolates tested were negative for enterotoxigenic and verotoxigenic E. coli virulence determinants, heat-labile enterotoxin (LT), heat-stable enterotoxins (STap, STb), verotoxins (VT1, VT2), and F4 (K88), F5 (K99), F6 (987P), and F41, except one STb-positive and two F4-positive isolates. A total of 25 isolates hybridized with an EaeA probe, and 11 hybridized with an enteropathogenic E. coli adherence factor (EAF) probe. None of 32 isolates hybridized with a bundle-forming pilus (BFP) probe. The EAF, EaeA, and BFP factors have been associated with human enteropathogenic E. coli strains. A total of 10 of 12 eaeA-positive porcine O45 isolates induced A/E lesions characterized by intimate adherence of bacteria to the intestinal epithelial cell membrane with effacement of the microvilli, similar to those of human attaching-effacing E. coli. However, A/E lesions were not observed in the piglets inoculated with any one of three eaeA-negative O45 isolates. All E. coli O45 isolates were non-adherent to HEp-2 cells. Thus, we have demonstrated the production of typical A/E lesions by nonenterotoxigenic E. coli O45 isolates from swine postweaning diarrhea. The results indicate the significance of the eaeA gene in A/E activities of these isolates and suggest that EAF and BFP are not involved in O45 E. coli infection of weaning piglets.

Adhesins, Bacterial↗
PubMed1994

Proteins found within porcine respiratory tract secretions bind lipopolysaccharides of Actinobacillus pleuropneumoniae.

Affinity for porcine respiratory tract secretions was found in some isolates of Actinobacillus pleuropneumoniae and involved lipopolysaccharides (LPS) (M. Bélanger, S. Rioux, B. Foiry, and M. Jacques, FEMS Microbiol. Lett. 97:119-126, 1992). In the present study, the affinity for a crude preparation of porcine respiratory tract mucus of isolates of the Pasteurellaceae family, i.e., Actinobacillus, Haemophilus, and Pasteurella spp., and of some unrelated gram-negative bacteria was examined. Affinity for crude porcine respiratory tract mucus was not a property shared by all Pasteurellaceae isolates tested. Furthermore, affinity for the porcine crude mucus preparation was not unique to the Pasteurellaceae group and did not seem to be restricted to bacteria originating from pigs. Different surface properties of A. pleuropneumoniae isolates in relation to their adherence to crude mucus were examined. The capsular layer seemed to mask the adhesin and interfered with adherence to crude mucus. Two poorly capsulated isolates, which had a more hydrophobic surface and bound Congo red, were also heavily labeled by gold particles coated with polymyxin, which is known to interact with the lipid A-core region of LPS, and adhered strongly to respiratory tract secretions. Tetramethylurea, charged polymers, divalent cations, chelators, monosaccharides and amino sugars, or lectins were unable to inhibit adherence of A. pleuropneumoniae to the crude mucus preparation. To identify the receptor(s) recognized by the lipopolysaccharidic adhesin of A. pleuropneumoniae, affinity chromatography was used. Two bands, which were proteinaceous in nature, of 10 and 11 kDa were recovered. Our results suggest that two low-molecular-mass proteins present in porcine respiratory tract secretions bind A. pleuropneumoniae LPS.

Actinobacillus pleuropneumoniae↗
PubMed1994

High-molecular-mass lipopolysaccharides are involved in Actinobacillus pleuropneumoniae adherence to porcine respiratory tract cells.

Actinobacillus pleuropneumoniae is the causative agent of porcine pleuropneumonia. The major adhesin of A. pleuropneumoniae has been identified as the lipopolysaccharides (LPSs) (M. Bélanger, D. Dubreuil, J. Harel, C. Girard, and M. Jacques, Infect. Immun. 58:3523-3530, 1990). Using immunoelectron microscopy and flow cytometry, we showed in the present study that LPSs were well exposed at the surface of this encapsulated microorganism. Immunolocalization with porcine lung and tracheal frozen sections showed that extracted LPS bound to the lung mesenchyme and vascular endothelium and to the tracheal epithelium, respectively. Inhibition of adherence of A. pleuropneumoniae with extracted LPS was also performed with lung and tracheal frozen sections. Acid hydrolysis of LPS revealed that the active component of LPS was not lipid A but the polysaccharides. LPSs from A. pleuropneumoniae serotypes 1 and 2 were separated by chromatography on Sephacryl S-300 SF, in the presence of sodium deoxycholate, according to their molecular masses. The adherence-inhibitory activity was found in the high-molecular-mass fractions. These high-molecular-mass fractions contained 2-keto-3-deoxyoctulosonic acid and neutral sugars, and they were recognized by a monoclonal antibody directed against A. pleuropneumoniae O antigen but not recognized by a monoclonal antibody against capsular antigen.

Actinobacillus pleuropneumoniae↗
PubMed1994

Characterization of Serpulina hyodysenteriae isolates of serotypes 8 and 9 from Quebec by restriction endonuclease fingerprinting and ribotyping.

This study was undertaken to assess the discriminatory value of restriction endonuclease fingerprinting (REF) analysis and ribotyping of 21 Serpulina hyodysenteriae isolates of serotypes 8 and 9. For REF analysis, DNAs were digested with the BglII restriction enzyme and the resultant fragments were separated by polyacrylamide gel electrophoresis. For ribotyping, hybridization of BglII genomic fragments with a probe of rrnB operon using an Escherichia coli rDNA probe was performed on all isolates. Although many isolates shared a common pattern by BglII REF and BglII ribotyping analysis, differences among some S. hyodysenteriae isolates were observed. REF and ribotyping using BglII restriction enzyme, were not specific for serotypes. The predominance of an REF and a ribotype pattern among S. hyodysenteriae isolates from Quebec suggested that epidemiologically important S. hyodysenteriae types occur in different swine herds.

Bacterial Typing Techniques↗
PubMed1994

Reduced in vitro displacement of valproic acid from protein binding by salicylate in uremic sera compared with normal sera. Role of uremic compounds.

Limited studies indicate increased free fraction of valproic acid in uremia. One study also described displacement of valproic acid from protein binding by salicylate in children with epilepsy. The authors studied in vitro interaction of valproic acid and salicylate in uremic sera and compared their results with same interactions in normal sera. As expected, the concentrations of free valproic acid were always significantly higher in uremic sera compared with normal sera. When uremic sera were supplemented with both valproic acid and salicylate, a much lower displacement of valproic acid by salicylate was observed, compared with the effects observed in normal sera. Treatment of uremic sera with charcoal removed those uremic compounds, and the concentration of free valproic acid in charcoal-treated uremic sera were comparable to the concentrations observed in normal sera. When uremic compounds were extracted from charcoal with methanol, lyophilized, and added to normal serum, an increase in free valproic acid concentration in normal serum was observed, indicating that uremic compounds, rather than altering albumin structure, are responsible for elevated free valproic acid concentration in uremia. However, uremic extract failed to produce any further displacement of valproic acid in normal serum in the presence of salicylate. The authors concluded that uremic compounds are responsible for elevated free valproic acid concentrations, but the displacement of valproic acid by salicylate in uremic sera are less remarkable compared with such effect in normal sera.

Charcoal↗
PubMed1993

Distribution and conservation of sequences homologous to the 1731 retrotransposon in Drosophila.

The distribution of 1731 retrotransposon-hybridizing sequences in the family Drosophilidae has been studied using a 1731 probe from Drosophila melanogaster. Squash blot and Southern blot analyses of 42 species reveal that the 1731 sequences are widespread within both the Sophophora and Drosophila subgenera and are also present in the genera Scaptomyza and Zaprionus. Hence the 1731 retrotransposon family appears to have a long evolutionary history in the Drosophilidae genome. Differences of hybridization signal intensity suggested that the 1731 sequence is well conserved only in the three species most closely related to D. melanogaster (D. simulans, D. mauritiana, and D. sechellia). A survey of insertion sites in numerous different populations of the previous four species by in situ hybridization to polytene chromosomes has shown in all cases both chromocentric hybridizations and a low number of sites (0-5) on the chromosomal arms. This number of sites is among the lowest observed in D. melanogaster and D. simulans when 1731 is compared with other retrotransposon families. In addition, we have observed species-specific patterns of the chromocentric hybridization signal, suggesting rapid modifications of the beta-heterochromatin components since the radiation of the melanogaster subgroup.

Animals↗
PubMed1993

Detection of immunoglobulin-G-binding proteins in Streptococcus suis.

This study was undertaken to search for the presence of immunoglobulin G (IgG)-binding proteins in Streptococcus suis, an important swine pathogen. Whole bacterial cells were incubated with human or pig IgG conjugated to gold particles and examined by transmission electron microscopy. Cells of some S. suis strains were labelled as were cells of the positive control strain, Staphylococcus aureus Cowan I. Binding of pig and human IgG to five different bacterial species of group D streptococci, to reference strains representing the 29 capsular types of S. suis, and to 12 S. suis capsular type 2 strains was then examined using Western blotting. All strains interacted with pig and human IgG, although the binding profiles were slightly different. A 52 kDa protein was observed in all capsular types of S. suis. This protein, absent in other group D streptococcal species, was observed in all capsular type 2 isolates originating from diseased or clinically healthy pigs, and was shown to bind human IgG-Fc fragments. The IgG-binding activity was also observed in the culture supernatant and was sensitive to proteolysis.

Animals↗
PubMed1993

Alterations in the cellular envelope of spontaneous IIIManL-defective mutants of Streptococcus salivarius.

In Streptococcus salivarius, the phosphoenolpyruvate: mannose phosphotransferase system (PTSMan) transports and concomitantly phosphorylates mannose, glucose, fructose and 2-deoxyglucose. PTSMan consists of a membrane Enzyme II and two forms of Enzyme III (IIIMan) having molecular masses of 38.9 kDa (IIIManH) and 35.2 kDa (IIIManL) respectively. We have previously reported the isolation of spontaneous mutants lacking IIIManL, and showed that they exhibited abnormal growth when cultured in mixtures of sugars containing glucose. The mutants also synthesize several cytoplasmic glucose-repressible proteins during growth on glucose and some of them constitutively express a fructose PTS which is induced by fructose in the parental strain. We have now investigated the properties and composition of the cellular envelope of three S. salivarius IIIManL-defective mutants (strains A37, B31 and G29) after growth on glucose. The mutants have altered sensitivity to various toxic compounds that interfere with cell-envelope functions. The mutants also exhibited altered membrane-protein profiles when analysed by two-dimensional PAGE and modified total lipid and phosphorus contents and lipid/protein ratio. In one mutant (strain G29), the proportion of the phospholipids separated by TLC was different from the parental strain. Electron microscopy indicated that one mutant (strain A37) possessed more fimbriae than the parental strain. The results suggested that these IIIManL-defective mutants were affected in a global regulatory gene controlling several cellular or physiological functions, many of these being related to the cellular envelope.

Bacterial Proteins↗
PubMed1993

Virulence of capsulated and noncapsulated isolates of Pasteurella multocida and their adherence to porcine respiratory tract cells and mucus.

The virulence and the adherence to porcine respiratory tract cells and mucus of three toxigenic, capsular type D Pasteurella multocida isolates and their noncapsulated variants were evaluated in the present study. Loss of capsule by P. multocida, verified by transmission electron microscopy after polycationic ferritin labeling, was associated with a massive reduction in virulence of the organisms in mice. Specific-pathogen-free piglets inoculated intranasally with one of the capsulated isolates or its noncapsulated variant developed turbinate lesions characterized by bone resorption and by an inflammation of the mucosa associated with hyperplasia and squamous metaplasia of the epithelium. Infection with the capsulated isolate led to more severe lesions and atrophy of turbinates. The interactions of these P. multocida isolates with porcine respiratory tract cells and mucus were studied in vitro. The presence of capsule resulted in a decrease in binding of respiratory tract mucus were studied in vitro. The presence of capsule resulted in a decrease in binding of respiratory tract mucus to P. multocida isolates as determined by a dot blot assay. The presence of capsule also resulted in a significant decrease in adherence to porcine tracheal rings maintained in culture. The capsule seemed to mask outer membrane components which are involved in adherence. One of these components might be lipopolysaccharide since purified lipopolysaccharide bound respiratory tract mucus and blocked adherence of this microorganism to porcine tracheal rings. Our data indicate that capsular material does not seem to be involved in adherence of P. multocida to respiratory tract cells and mucus, but capsulated isolates are more virulent in mice and also in piglets.

Animals↗
PubMed1993

Pathogenicity of an Escherichia coli O115:K"V165" mutant negative for F165(1) fimbriae in septicemia of gnotobiotic pigs.

To evaluate the role of the F165(1) fimbrial system in the pathogenesis of septicemia, 2-day-old germfree pigs were inoculated intragastrically with Escherichia coli O115:K"V165":F165 wild-type strain 5131, its F165(1)-negative TnphoA mutant M48, or E. coli O115:K(-):F165(-) wild-type strain 862B. Pigs were sacrificed at different times (3, 6, 12, 24, 48, and 96 h) postinfection (p.i.). Pigs inoculated with strain 5131 developed clinical signs (anorexia, lameness, reluctance to move, or lack of motor coordination) and were moribund within 48 h p.i., and, at necropsy, infecting bacteria were isolated in various extraintestinal organs. Strain 5131 was isolated as early as 6 h p.i. from the blood of inoculated pigs. Pigs inoculated with mutant M48 developed only mild clinical signs at 96 h p.i. Mutant M48 colonized extraintestinal organs of pigs but to a lesser extent than the parent strain did. In contrast to the parent strain, this mutant was not isolated in the blood of inoculated pigs. Pigs inoculated with strain 862B remained normal during the experiment. All of the strains colonized the mucus layer of the intestine, but no histological changes of intestinal mucosa were observed by either light or electron microscopy. The parent strain, but not the mutant M48, expressed F165(1) in vivo. In a competitive study in which the parent strain and its afimbrial mutant were inoculated simultaneously, clinical signs of septicemia developed 24 h after inoculation, and only the parent strain 5131 was isolated from the blood of inoculated pigs. Our results suggest that the F165(1) fimbrial system of E. coli O115:K"V165" strains may play an important role in the ability of the bacteria to survive in the blood and spread systemically through the porcine host.

Animals↗
PubMed1993

A species-specific periplasmic flagellar protein of Serpulina (Treponema) hyodysenteriae.

We have previously reported that a 46-kDa protein present in an outer membrane protein preparation seemed to be a species-specific antigen of Serpulina hyodysenteriae (Z. S. Li, N. S. Jensen, M. Bélanger, M.-C. L'Espérance, and M. Jacques, J. Clin. Microbiol. 30:2941-2947, 1992). The objective of this study was to further characterize this antigen. A Western blot (immunoblot) analysis and immunogold labeling with a monospecific antiserum against this protein confirmed that the protein was present in all S. hyodysenteriae reference strains but not in the nonpathogenic organism Serpulina innocens. The immunogold labeling results also indicated that the protein was associated with the periplasmic flagella of S. hyodysenteriae. N-terminal amino acid sequencing confirmed that the protein was in fact a periplasmic flagellar sheath protein. The molecular mass of this protein, first estimated to be 46 kDa by Western blotting, was determined to be 44 kDa when the protein was evaluated more precisely by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the protein was glycosylated, as determined by glycoprotein staining and also by N-glycosidase F treatment. Five other periplasmic flagellar proteins of S. hyodysenteriae, which may have been the core proteins and had molecular masses of 39, 35, 32, 30, and 29 kDa, were antigenically related and cross-reacted with the periplasmic flagellar proteins of S. innocens. Finally, serum from a pig experimentally infected with S. hyodysenteriae recognized the 44-kDa periplasmic flagellar sheath protein. Our results suggest that the 44-kDa periplasmic flagellar sheath protein of S. hyodysenteriae is a species-specific glycoprotein antigen.

Amino Acid Sequence↗