Use of Monoclonal Antibodies to Lipopolysaccharide for Antigenic Analysis of
            <i>Coxiella burnetii</i>

Hotta, Akitoyo; Kawamura, Midori; To, Ho; Andoh, Masako; Yamaguchi, Tsuyoshi; Fukushi, Hideto; Amano, Ken‐ichi; Hirai, Katsuya

doi:10.1128/jcm.41.4.1747-1749.2003

Cited by 7 publications

(5 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Several PI-LPS specific mAbs have been developed for analysis of antigenicity of immunogenic components of C. burnetii LPS and detection of the virulent form of C. burnetii (33–36). Hotta et al (34) reported generation of 19 PI-LPS specific mAbs and demonstrated that these mAbs were able to be separated into three groups based on their reactivity with O-polysaccharide chains (27 kDa of PI-LPS), O-polysaccharide chains (15 to 27 kDa of PI-LPS) and outer-core oligosaccharides (14 kDa of PI-LPS).…”

Section: Discussionmentioning

confidence: 99%

Development of a Lipopolysaccharide-Targeted Peptide Mimic Vaccine against Q Fever

Peng

Zhang

Mitchell

et al. 2012

The Journal of Immunology

View full text Add to dashboard Cite

C burnetii is a gram-negative bacterium that causes acute and chronic Q fever in humans. Creation of a safe and effective new generation vaccine to prevent Q fever remains an important public health goal. Previous studies suggested that antibody (Ab)-mediated immunity to C. burnetii phase I lipopolysaccharide (PI-LPS) is protective. To identify the potential peptides that can mimic the protective epitopes on PI-LPS, a PI-LPS specific monoclonal antibody (mAb) 1E4 was generated, characterized and used to screen a phage display library. Interestingly, our results indicate that 1E4 was able to inhibit C. burnetii infection in vivo, suggesting that 1E4 is a protective mAb. After three rounds of biopanning by 1E4 from the phage display library, a mimetic peptide, m1E41920 was identified, chemically synthesized and conjugated to KLH for examining its immunogenicity. The results indicate that the synthetic peptide m1E41920 was able to inhibit the binding of 1E4 to PI antigen, suggesting m1E41920 shares the same binding site of 1E4 with the epitopes of PI antigen. In addition, m1E41920-KLH elicited a specific IgG response to PI antigen and immune sera from m1E41920-KLH-immunized mice was able to inhibit C. burnetii infection in vivo, suggesting that m1E41920 may specifically mimic the protective epitope of PI-LPS. Furthermore, m1E41920-KLH was able to confer significant protection against C. burnetii challenge. Thus, m1E41920-KLH is a protective antigen and may be useful for developing a safe and effective vaccine against Q fever. This study demonstrates the feasibility of developing a peptide mimic vaccine against Q fever.

show abstract

Section: Discussionmentioning

confidence: 99%

Development of a Lipopolysaccharide-Targeted Peptide Mimic Vaccine against Q Fever

Peng

Zhang

Mitchell

et al. 2012

The Journal of Immunology

View full text Add to dashboard Cite

show abstract

“…The others were stocked and/or maintained at NIID. The inactivated Coxiella burnetii cultures (23) and Wolbachia pestis (24) genomic DNA were kindly provided by Drs. Hideto Fukushi (Department of Veterinary Medicine, Faculty of Applied Biological Science, Gifu University, Gifu, Japan) and Tetsuhiko Sasaki (Department of Biological Science, Graduate School of Science, University of Tokyo, Tokyo, Japan), respectively.…”

Section: Methodsmentioning

confidence: 99%

Development of a Real-Time PCR Assay for Detection and Quantification of <i>Francisella tularensis</i>

Fujita,

Tatsumi,

Tanabayashi

et al. 2006

Jpn J Infect Dis

View full text Add to dashboard Cite

The facultative intracellular bacterium, Francisella tularensis, is an etiological agent of tularemia and is also considered to be a potential biological threat agent due to its extreme infectivity. We established a real-time PCR assay using the LightCycler (LC) system to detect a Francisella-specific sequence of the outer membrane protein (fopA) gene. Twenty-five F. tularensis strains including 16 Japanese isolates were subjected to this LC-PCR assay, and were tested positive, whereas Francisella philomiragia and other bacteria species did not show any specific fluorescent signal. A linear response was observed using F. tularensis genomic DNAs of between 20 fg and 2 ng, corresponding to 1.2 to 1.2×10 5 bacteria. The newly established real-time PCR allows the detection of the F. tularensis genome specifically, sensitively, and rapidly. This assay may contribute to the standardization of the laboratory diagnosis of tularemia.

show abstract

“…Complete elimination from an immunocompetent host leads to the phase II developmental stage. 5 As others have done previously, 3,4,8,11,12,14,15 we employed the specificity of monoclonal antibodies (Mabs) as probes to detect antigenic differences. We prepared several Mabs and used them to differentiate numerous isolates.…”

Section: Introductionmentioning

confidence: 99%

Identification and Characterization of Coxiella burnetii Strains and Isolates Using Monoclonal Antibodies

Sekeyová

Kovacóvá

2006

Annals of the New York Academy of Sciences

View full text Add to dashboard Cite

We evaluated 6 monoclonal antibodies (MAbs) for their usefulness in identifying and characterizing recognized laboratory strains as well as field isolates of Coxiella burnetii. Five had been generated in response to strain Nine Mile (3 IgM class, 1 IgG class, 1 light chain producers only) and were polypeptide-specific, and 1 was anti-Priscilla (IgG class) and was lipopolysaccharide (LPS)-specific. Initially, the MAbs were used in conjunction with a dot blot assay with which we could differentiate C. burnetii from rickettsiae or chlamydiae. Confirmation of the specificity of these MAbs was provided by demonstrating that only C. burnetii antigens were recognized by certain combinations of antibodies used for immunoblotting proteins of various C. burnetii strains. Subsequently, we characterized antigens of 11 C. burnetii field isolates and 3 reference strains by Western blotting with individual MAbs. MAb 921 and 922 (IgG class), MAb 241, 242, 384, 386, 614 (IgM class), and 7A5, 7A1 (light chain) consistently recognized a protein. Staining intensity differed, depending on the strain tested, and there was variability in the size of the antigen immunoreactive with MAb 14H (IgG class, LPS-specific). The most reactive region was at about 249 kD. Variability of reactivities with field isolates was seen in both the distribution of individual bands and their intensities. We conclude that an extensive immunoblotting technique may be useful for C. burnetii strain differentiation and routine identification of C. burnetii can be accomplished using this MAb-based dot blot assay.

show abstract

Use of Monoclonal Antibodies to Lipopolysaccharide for Antigenic Analysis of Coxiella burnetii

Cited by 7 publications

References 21 publications

Development of a Lipopolysaccharide-Targeted Peptide Mimic Vaccine against Q Fever

Development of a Lipopolysaccharide-Targeted Peptide Mimic Vaccine against Q Fever

Development of a Real-Time PCR Assay for Detection and Quantification of <i>Francisella tularensis</i>

Identification and Characterization of Coxiella burnetii Strains and Isolates Using Monoclonal Antibodies

Contact Info

Product

Resources

About