O-Antigenic Cross-Reactivity In Fusobacterium Nucleatum

Fusobacterium nucleatum is becoming increasingly recognised as an emerging pathogen, gaining attention as a potential factor for exacerbating colorectal cancer and is strongly linked with pregnancy complications including pre-term and still births. Little is known about the virulence factors of this organism; thus, we have initiated studies to examine the bacterium’s surface glycochemistry. In an effort to characterise the surface carbohydrates of F. nucleatum, the aims of this study were to investigate the structure of the lipopolysaccharide (LPS) O-antigen of the cancer-associated isolate F. nucleatum strain CC 7/3 JVN3 C1 (hereafter C1) and to develop monoclonal antibodies (mAbs) to the LPS O-antigen that may be beneficial to the growing field of F. nucleatum research. In this study, we combined several technologies, including nuclear magnetic resonance (NMR) spectroscopy, to elucidate the structure of the LPS O-antigen repeat unit as -[-4-β-Gal-3-α-FucNAc4N-4-α-NeuNAc-]-. We have previously identified this structure as the LPS O-antigen repeat unit from strain 10953. In this present study, we developed a mAb to the C1 LPS O-antigen and confirmed the mAbs cross-reactivity to the 10953 strain, thus confirming the structural identity.

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O-ANTIGENIC CROSS-REACTIVITY IN FUSOBACTERIUM NUCLEATUM: CHEMOTYPE V LIPOPOLYSACCHARIDES

Acta Pathologica Microbiologica Scandinavica Series B Microbiology ◽

10.1111/j.1699-0463.1983.tb00015.x ◽

2009 ◽

Vol 91B (1-6) ◽

pp. 93-95 ◽

Cited By ~ 1

Author(s):

BRITT ÅDNEGARD ◽

TOR HOFSTAD

Keyword(s):

Fusobacterium Nucleatum ◽

Cross Reactivity

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Cross-Reactive Monoclonal Antibodies Induced by Lps from Periodontopathic Bacteria

Advances in Dental Research ◽

10.1177/08959374880020022001 ◽

1988 ◽

Vol 2 (2) ◽

pp. 319-322 ◽

Cited By ~ 2

Author(s):

T. Kato ◽

K. Okuda ◽

I. Takazoe

Keyword(s):

Monoclonal Antibodies ◽

Fusobacterium Nucleatum ◽

Fusobacterium Necrophorum ◽

Cross Reactivity ◽

Clinical Isolates ◽

Antibody Isotype ◽

Western Immunoblotting ◽

Immunoblotting Analysis ◽

Periodontopathic Bacteria ◽

M 12

Monoclonal antibodies against lipopolysaccharides (LPS) of Fusobacterium nucleatum ATCC 25586 and Eikenella corrodens FDC 1073 were used for the study of antigenic characteristics of periodontopathic bacteria. LPS was extracted by the hot-phenol/water method. Three monoclonal antibodies (isotype IgM) against F. nucleatum ATCC 25586 were cross-reactive with LPS from E. corrodens FDC 1073. Four hybridomas producing antibody to E. corrodens FDC 1073 LPS were also obtained. Three out of four monoclonal antibodies (isotype IgM) were found to exhibit cross-reactivity with LPS from F. nucleatum ATCC 25586. These six monoclonal antibodies reacted with four out of seven E. corrodes and nine out of 27 F. nucleatum clinical isolates. Western immunoblotting analysis demonstrated that the six antibodies reacted with a similar fast-migrating band of LPS from F. nucleatum ATCC 25586 and E. corrodens FDC 1073. Another monoclonal antibody (isotype IgG3) against E. corrodens FDC 1073 LPS exhibited cross-reactivity with LPS from Fusobacterium necrophorum ATCC 25286 and Capnocytophaga ochracea M-12. This antibody was found to react with slow-migrating bands of E. corrodens FDC 1073 LPS and a fast-migrating band of LPS from F. necrophorum ATCC 25286 and C. ochracea M-12 by Western immunoblotting analysis. Four out of seven clinical isolates of E. corrodens reacted strongly with this antibody. The present findings indicate that there is a common LPS core epitope between F. nucleatum ATCC 25586 and E. corrodens FDC 1073. They also indicated that the O-side-chain epitope of E. corrodens FDC 1073 might be common to the LPS core epitopes of F. necrophorum ATCC 25286 and C. ochracea M-12.

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CME-Antworten: «Fusobacterium nucleatum/naviforme – eine seltene, aber nicht zu unterschätzende Ursache für pyogene Leberabszesse» aus Praxis Nr. 19

Praxis ◽

10.1024/1661-8157/a002996 ◽

2018 ◽

Vol 107 (20) ◽

pp. 1109-1109

Author(s):

Mario Rifaat ◽

Carsten Depmeier ◽

Victor Jeger ◽

Markus Schneemann ◽

Alexia Anagnostopoulos

Keyword(s):

Fusobacterium Nucleatum

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Concomitant Clinical Sensitivity (CCS) and Cross-Reactivity

Allergy & Clinical Immunology International - Journal of the World Allergy Organization ◽

10.1027/0838-1925.15.1.18 ◽

2003 ◽

Vol 15 (01) ◽

pp. 018-029 ◽

Cited By ~ 1

Author(s):

Harris Steinman ◽

Steve Lee

Keyword(s):

Cross Reactivity ◽

Clinical Sensitivity

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Human Prothrombin Activation: Determination of Plasma and Serum Levels of Prothrombin Fragment 3 by Radioimmunoassay

10.1055/s-0038-1665668 ◽

1979 ◽

Author(s):

Daniel Walz ◽

Thomas Brown

Keyword(s):

Blood Clotting ◽

Factor Xa ◽

Heart Association ◽

Serum Levels ◽

Cross Reactivity ◽

Assay Procedure ◽

A Chain ◽

Prothrombin Activation ◽

Theoretical Amount

Human prothrombin activation is unique in that, in addition to the release of fragment 1.2 (FI.2) from the NH-terminus of prothrombin by factor Xa during the generation of thrombin, an additional 13 residue polypeptide, fragment 3 (F3), is autocatalytically removed from the amino-terminus of the thrombin A chain. We have developed a rapid radioimmunoassay for human F3 which incorporates short incubation times and the use of a preprecipitated second antibody; the assay can be performed in three hours. Specificity studies in buffer systems show prothrombin and prethrombin 1 cross-reacting at a level of 0.001; purified thrombin does not cross-react. In the presence of 5% BSA, prothrombin displays considerably less cross-reactivity. No immunoreactive material to F3 antibodies could be detected in 400 μL of plasma. Serum, obtained from whole blood clotting, contained measurable quantities of F3 (40-100 ng/mL). This amount in serum represents only 5-10% of the theoretical amount available should all of the fragment be hydrolytically cleaved during the conversion of prothrombin to thrombin. This assay procedure is currently being utilized to monitor the activation of purified human prothrombin in the absence and presence of selected plasma inhibitors. (Supported in part by NIH 05384-17 and the Michigan Heart Association).

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