scholarly journals Outer-membrane protein- and rough lipopolysaccharide-specific monoclonal antibodies protect mice against Brucella ovis

1995 ◽  
Vol 43 (5) ◽  
pp. 344-347 ◽  
Author(s):  
R. A. Bowden ◽  
A. Cloeckaert ◽  
M. S. Zygmunt ◽  
G. Dubray
1998 ◽  
Vol 42 (11) ◽  
pp. 2870-2876 ◽  
Author(s):  
P. Christian Lück ◽  
Jürgen W. Schmitt ◽  
Arne Hengerer ◽  
Jürgen H. Helbig

ABSTRACT We determined the MICs of ampicillin, ciprofloxacin, erythromycin, imipenem, and rifampin for two clinical isolates of Legionella pneumophila serogroup 1 by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction assay and by quantitative culture. To test the influence of subinhibitory concentrations (sub-MICs) of antimicrobial agents on Legionella uptake into Acanthamoeba castellanii and U937 macrophage-like cells, both strains were pretreated with 0.25 MICs of the antibiotics for 24 h. In comparison to that for the untreated control, subinhibitory concentrations of antibiotics significantly reducedLegionella uptake into the host cells. Measurement of the binding of monoclonal antibodies against several Legionellaantigens by enzyme-linked immunoassays indicated that sub-MIC antibiotic treatment reduced the expression of the macrophage infectivity potentiator protein (Mip), the Hsp 60 protein, the outer membrane protein (OmpM), an as-yet-uncharacterized protein of 55 kDa, and a few lipopolysaccharide (LPS) epitopes. In contrast, the expression of some LPS epitopes recognized by monoclonal antibodies 8/5 and 30/4 as well as a 45-kDa protein, a 58-kDa protein, and the major outer membrane protein (OmpS) remained unaffected.


2019 ◽  
Vol 91 (3) ◽  
pp. 90-98
Author(s):  
O. Yu. Galkin ◽  
◽  
O. B. Besarab ◽  
Yu. V. Gorshunov ◽  
O. M. Ivanova ◽  
...  

2000 ◽  
Vol 68 (11) ◽  
pp. 6250-6256 ◽  
Author(s):  
Timothy F. Murphy ◽  
Aimee L. Brauer ◽  
Norine Yuskiw ◽  
Thomas J. Hiltke

ABSTRACT Outer membrane protein E (OMP E) is a 50-kDa protein ofMoraxella catarrhalis which possesses several characteristics indicating that the protein will be an effective vaccine antigen. To study the antigenic structure of OMP E, eight monoclonal antibodies were developed and characterized. Three of the antibodies recognized epitopes which are present on the bacterial surface. Fusion peptides corresponding to overlapping regions of OMP E were constructed, and immunoblot assays were performed to localize the areas of the molecule bound by the monoclonal antibodies. These studies identified a surface-exposed epitope in the region of amino acids 80 through 180. To further study the protein, two mutants which lack OMP E were constructed. In bactericidal assays, the mutants were more readily killed by normal human serum compared to the isogenic parent strains. These results indicate that OMP E is involved in the expression of serum resistance of M. catarrhalis.


Hybridoma ◽  
2007 ◽  
Vol 26 (1) ◽  
pp. 35-41 ◽  
Author(s):  
Cláudia P.H. Fernandes ◽  
Fabiana K. Seixas ◽  
Mariana L. Coutinho ◽  
Flávia A. Vasconcellos ◽  
Núbia Seyffert ◽  
...  

Microbiology ◽  
1987 ◽  
Vol 133 (9) ◽  
pp. 2639-2646 ◽  
Author(s):  
M. VIRJI ◽  
J. N. FLETCHER ◽  
K. ZAK ◽  
J. E. HECKELS

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