Characterization of an 18-kilodalton Brucella cytoplasmic protein which appears to be a serological marker of active infection of both human and bovine brucellosis

Goldbaum, F.A.; Leoni, Juliana; Wallach, Jorge C.; Fossati, Carlos A.

doi:10.1128/jcm.31.8.2141-2145.1993

Cited by 75 publications

(41 citation statements)

References 20 publications

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“…In this acute human infection, high levels of IgM antibodies against LPS were detected in initial samples, by both agglutination and ELISA tests, in agreement with previous reports [25]. Antibodies against cytoplasmic proteins of Brucella, which constitute appropriate markers of active brucellosis [18,20], were also detected in all but 5 patients.…”

Section: Discussionsupporting

confidence: 90%

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Human infection by Brucella melitensis: an outbreak attributed to contact with infected goats

Wallach¹

1997

FEMS Immunology and Medical Microbiology

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Although several outbreaks of Brucella melitensis infection have been reported among laboratory workers or goat cheese consumers, outbreaks related to rural labour have been rarely studied. An outbreak of human brucellosis among farm workers of Argentina was studied and revealed a close relationship with an epidemic of caprine abortions which occurred shortly before on the same farm. High rates of B. melitensis infection were found among goats. Active brucellosis was diagnosed in 33 subjects (14 with positive blood culture for B. melitensis), while other 27 did not show evidence of illness. While 25 of the brucellosis active patients were rural workers, only 5 of the healthy subjects were engaged in rural labour. Active brucellosis was diagnosed in 91.3% of the subjects in continuous contact with goats and in 32% of those having an occasional contact with the animals. All the 60 subjects denied consumption of goat cheese or milk. As shown here, epidemic human infections by B. melitensis may develop among people frequently in contact with infected goat herds or goat manure.

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Section: Discussionsupporting

confidence: 90%

“…cytoplasmic protein of Brucella Serum reactivity against an 18 kDa cytoplasmic protein of Brucella was titrated by capture ELISA with the monoclonal antibody BI24, as described previously [20]. Puri¢ed BI24 was adsorbed at 1 Wg/well in PBS onto polystyrene plates.…”

Section: Elisa For Detecting Antibodies To the 18 Kdamentioning

confidence: 99%

Human infection by Brucella melitensis: an outbreak attributed to contact with infected goats

Wallach¹

1997

FEMS Immunology and Medical Microbiology

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“…SDS-PAGE analysis along expression and purification process of the chimeric protein BLS-FliC131 indicated that the monomeric protein has the expected molecular weight of 52 kDa. The BLS-FliC131 chimeric protein is recognized by previously described anti-flagellin and anti-BLS monoclonal antibodies, 14,28 as shown by Western blot (Fig. 1).…”

Section: Bls-flic131 Chimeric Protein Keeps Folding Properties Of Flimentioning

confidence: 68%

Characterization of structural and immunological properties of a fusion protein between flagellin from Salmonella and lumazine synthase from Brucella

et al. 2017

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Aiming to combine the flexibility of Brucella lumazine synthase (BLS) to adapt different protein domains in a decameric structure and the capacity of BLS and flagellin to enhance the immunogenicity of peptides that are linked to their structure, we generated a chimeric protein (BLS-FliC131) by fusing flagellin from Salmonella in the N-termini of BLS. The obtained protein was recognized by anti-flagellin and anti-BLS antibodies, keeping the oligomerization capacity of BLS, without affecting the folding of the monomeric protein components determined by circular dichroism. Furthermore, the thermal stability of each fusion partner is conserved, indicating that the interactions that participate in its folding are not affected by the genetic fusion. Besides, either in vitro or in vivo using TLR5-deficient animals we could determine that BLS-FliC131 retains the capacity of triggering TLR5. The humoral response against BLS elicited by BLS-FliC131 was stronger than the one elicited by equimolar amounts of BLS + FliC. Since BLS scaffold allows the generation of hetero-decameric structures, we expect that flagellin oligomerization on this protein scaffold will generate a new vaccine platform with enhanced capacity to activate immune responses.

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“…Members of our group have previously shown that the immunoglobulin G (IgG) response to cytoplasmic proteins depleted of LPS (CPs, formerly called LPS-free CYT) of Brucella, measured by enzyme-linked immunosorbent assay (ELISA), allows differentiation of active from inactive human brucellosis and shows good correlation with the clinical progression of the disease (3,8). Similar results were obtained by measuring antibodies to an 18-kDa cytoplasmic protein of Brucella (9). Recent studies performed by members of our group have shown that IgM and IgG antibodies to CP and to the 18-kDa protein can be detected in patients having less than 40 days of symptoms of Brucella melitensis infection (3a).…”

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confidence: 68%

Effect of Early Antibiotic Treatment on the Antibody Response to Cytoplasmic Proteins of Brucella melitensis in Mice

Bowden

Racaro

Baldi

1999

Clin Diagn Lab Immunol

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To test whether antibiotic therapy hampers the antibody response toBrucella antigens, 30 BALB/c mice were infected withBrucella melitensis H38 and randomized for treatment with doxycycline administered intraperitoneally for 42 days starting at 7 or 28 days postinfection (p.i.) (groups DOX7 and DOX28, respectively) or for no treatment (control group). Antibodies to smooth lipopolysaccharide (LPS) reached peak levels (mean optical density [OD] = 2.618) between days 56 and 70 p.i. in the control group, and similar peak levels (mean OD = 2.486) were observed in the DOX28 group, but significantly lower peak levels (mean OD = 0.821) were observed at 28 days p.i. in the DOX7 group. The antibody response against cytoplasmic proteins depleted of LPS (CPs) reached maximal levels (mean OD = 2.402) between days 56 and 70 p.i. in the control group, but no response was detected in the DOX7 group. Anti-CP antibodies were detected in only three animals from the DOX28 group, at levels significantly lower than those in the control group (mean maximal OD = 0.791). The pattern of antibody response to an 18-kDa cytoplasmic protein of Brucella spp. was similar to that against the CP antigen. This study shows that early antibiotic treatment affects the antibody response of mice to cytoplasmic proteins of Brucella and, to a lesser extent, to LPS.

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Characterization of an 18-kilodalton Brucella cytoplasmic protein which appears to be a serological marker of active infection of both human and bovine brucellosis

Cited by 75 publications

References 20 publications

Human infection by Brucella melitensis: an outbreak attributed to contact with infected goats

Human infection by Brucella melitensis: an outbreak attributed to contact with infected goats

Characterization of structural and immunological properties of a fusion protein between flagellin from Salmonella and lumazine synthase from Brucella

Effect of Early Antibiotic Treatment on the Antibody Response to Cytoplasmic Proteins of Brucella melitensis in Mice

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