References of "FEMS Immunology & Medical Microbiology"
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See detailSecreted dipeptidyl peptidases as potential virulence factors for Microsporum canis.
Vermout, Sandy; Baldo, Aline ULg; Tabart, Jeremy et al

in FEMS Immunology & Medical Microbiology (2008), 54(3), 299-308

Dermatophytoses caused by Microsporum canis are frequently encountered in cats and dogs; they are highly contagious and readily transmissible to humans. In this study, two single genes, respectively ... [more ▼]

Dermatophytoses caused by Microsporum canis are frequently encountered in cats and dogs; they are highly contagious and readily transmissible to humans. In this study, two single genes, respectively coding for dipeptidyl peptidases IV and V (DppIV and DppV), were isolated and characterized. Both proteins share homology with serine proteases of the S9 family, some of which display properties compatible with implication in pathogenic processes. Both genes are expressed in vivo in experimentally infected guinea-pigs and in naturally infected cats, and when the fungus is grown on extracellular matrix proteins as the sole nitrogen and carbon source. DppIV and V were produced as active recombinant proteases in the yeast Pichia pastoris; the apparent molecular weight of rDppV is 83 kDa, whereas rDppIV appears as a doublet of 95 and 98 kDa. Like other members of its enzymatic subfamily, rDppIV has an unusual ability to cleave Pro-X bonds. This activity does not enhance the solubilization of keratin by fungal secreted endoproteases, and the protease probably acts solely on small soluble peptides. RDppV showed no ability to induce delayed-type hypersensitivity (DTH) skin reactions in guinea-pigs, despite the known immunogenic properties of homologous proteins. [less ▲]

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See detailCharacterization of the cattle serum antibody responses against TEM beta-lactamase and the nonimmunogenic Escherichia coli heat-stable enterotoxin (STaI)
Zervosen, Astrid ULg; Saegerman, Claude ULg; Antoniotti, Ingrid et al

in FEMS Immunology & Medical Microbiology (2008), 54(3), 319-329

In order to test the use of a subunit recombinant vaccine for its capacity to induce antibodies against the nonimmunogenic heat-stable enterotoxin STa from Escherichia coli and the TEM-1 beta-lactamase ... [more ▼]

In order to test the use of a subunit recombinant vaccine for its capacity to induce antibodies against the nonimmunogenic heat-stable enterotoxin STa from Escherichia coli and the TEM-1 beta-lactamase, cattle were immunized with a hybrid protein created by insertion of the STa sequence at position 197 of the TEM-1 beta-lactamase. Specific anti-STa IgG and IgG1 antibodies were detected at low levels, while no IgG2 antibodies were detected. In contrast, high levels of the different anti-TEM IgG subtypes were detected in cattle sera. In addition, beta-lactamase activity was inhibited by the sera. The presence of antibodies against STa and TEM-1 beta-lactamase was assessed in sera from 366 cattle taken from the field. No significant level of IgGs against the toxin or the TEM-1 was detected. A comparison of the antibody level between the immunized and the nonimmunized animals clearly demonstrated that STa was not able to induce a significant level of antibodies in the vaccinated animals. In contrast, a strong antibody response against TEM-1 beta-lactamase was demonstrated. [less ▲]

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See detailEvaluation of immunogenicity and protective efficacy of a Microsporum canis metalloprotease subunit vaccine in guinea pigs.
Vermout, Sandy M; Brouta, Frederic D; Descamps, Frederic F et al

in FEMS Immunology & Medical Microbiology (2004), 40(1), 75-80

In order to identify protective immunogens against Microsporum canis infection, a purified recombinant keratinolytic metalloprotease (r-MEP3) was tested as a subunit vaccine in experimentally infected ... [more ▼]

In order to identify protective immunogens against Microsporum canis infection, a purified recombinant keratinolytic metalloprotease (r-MEP3) was tested as a subunit vaccine in experimentally infected guinea pigs. Both humoral and cellular specific immune responses developing towards r-MEP3 were evaluated, by enzyme-linked immunosorbent assay and by in vitro lymphocyte transformation tests respectively. Vaccination induced a strong antibody response, and a significant but transient lymphoproliferative response against the protein. However, the protocol failed to prevent fungal invasion or development of dermatophytic lesions. These results show that under the present experimental conditions, r-MEP3 specific antibodies are not protective against a challenge exposure. They also suggest that in the same model, the induction of cell-mediated immunity towards r-MEP3 is not sufficient, indicating the need for further research in the field of specific immune mechanisms involved in M. canis dermatophytosis. [less ▲]

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See detailPerformance of the VERSANT (R) HIV-1 Resistance Assays (LiPA) for detecting drug resistance in therapy-naive patients infected with different HIV-1 subtypes
Derdelinckx, Inge; Van Laethem, Kristel; Maes, Baert et al

in FEMS Immunology & Medical Microbiology (2003), 39(2), 119-124

In this study we evaluated the performance of the VERSANT((R)) HIV-1 Resistance Assays (LiPA) in detecting drug resistance in therapy-naive HIV-infected patients diagnosed in Belgium in 2000. We compared ... [more ▼]

In this study we evaluated the performance of the VERSANT((R)) HIV-1 Resistance Assays (LiPA) in detecting drug resistance in therapy-naive HIV-infected patients diagnosed in Belgium in 2000. We compared the results with population sequencing and found concordance to be in line with previous studies in treatment-experienced patients (86.87% for reverse transcriptase (RT); 92.77% for protease (PRO)). Discordance was mainly due to indeterminate reactions on LiPA (8.45% for RT; 6.85% for PRO) and minor discordances (4.13% for RT; 0.25% for PRO). Major discordances were rare (0.46% for RT; 0.12% for PRO). Indeterminate reactions were significantly associated with strains belonging to non-B subtypes. (C) 2003 Federation of European Microbiological Societies. Published by Elsevier B.V.. All rights reserved. [less ▲]

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See detailRecombinant expression and antigenic properties of a 31.5-kDa keratinolytic subtilisin-like serine protease from Microsporum canis
Descamps, Frédéric; Brouta, Frédéric; Vermout, Sandy et al

in FEMS Immunology & Medical Microbiology (2003), 38(1), 29-34

A secreted 31.5-kDa keratinolytic subtilase (SUB3; AJ431180) is thought to be a Microsporum canis virulence factor and represents a candidate for vaccination trials. In this study, the recombinant ... [more ▼]

A secreted 31.5-kDa keratinolytic subtilase (SUB3; AJ431180) is thought to be a Microsporum canis virulence factor and represents a candidate for vaccination trials. In this study, the recombinant keratinase (r-SUB3) was produced by the Pichia pastoris expression system and purified to homogeneity. Recombinant SUB3 displayed identical biochemical properties with the native protease. Experimentally cutaneously infected guinea pigs showed specific lymphoproliferative response towards r-SUB3, while no specific humoral immune response was induced except for one animal. The heterologous expression of SUB3 provides a valuable tool for addressing further investigations on the role of this keratinase in the specific cellular immune response and on its use in vaccination trials in the cat. (C) 2003 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved. [less ▲]

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