scholarly journals Immunity to Ricin: Fundamental Insights into Toxin–Antibody Interactions

Author(s):  
Joanne M. O’Hara ◽  
Anastasiya Yermakova ◽  
Nicholas J. Mantis
2021 ◽  
Vol 22 (1) ◽  
Author(s):  
Antonio Julià ◽  
María López-Lasanta ◽  
Francisco Blanco ◽  
Antonio Gómez ◽  
Isabel Haro ◽  
...  

Abstract Background Blocking of the Tumor Necrosis Factor (TNF) activity is a successful therapeutic approach for 50–60% of rheumatoid arthritis (RA) patients. However, there are yet no biomarkers to stratify patients for anti-TNF therapy. Rheumatoid factor (RF) and anti-cyclic-citrullinated antibodies (anti-CCP) have been evaluated as biomarkers of response but the results have shown limited consistency. Anti-carbamylated protein (anti-CarP) and anti-peptidylarginine deiminase type 4 (anti-PAD4) antibodies have been much less studied. Despite being linked to common immune processes, the interaction between these markers has not been evaluated yet. Our aim was to analyze the interaction between these four antibodies in relation to the response to anti-TNF therapy. Methods For this objective, a prospective cohort of n = 80 RA patients starting anti-TNF therapy was recruited. Serum determinations at baseline were performed for RF, anti-CCP, anti-CarP and anti-PAD4 antibodies using enzyme-linked immunosorbent assays (ELISA). The clinical response to anti-TNF therapy was determined at week 12 using the change in DAS28 score. Association was performed using multivariate linear regression adjusting for baseline DAS28, sex and age. Results The interaction between pairs of antibodies was tested by the addition of an interaction term. We found two highly significant antibody interactions associated with treatment response: anti-CarP with anti-PAD4 (p = 0.0062), and anti-CCP with RF (p = 0.00068). The latter antibody interaction was replicated in an independent retrospective cohort of RA patients (n = 199, p = 0.04). Conclusions The results of this study suggest that antibody interaction effects are important factors in the response to anti-TNF therapy in RA.


2002 ◽  
Vol 80 (8) ◽  
pp. 1131-1140 ◽  
Author(s):  
Henry N Yu ◽  
Chang-Chun Ling ◽  
David R Bundle

Disaccharides 1-3 corresponding to the antigenic determinants of Salmonella serotypes A, B, and D1 were synthesized in a form suited for use in biosensors. The disaccharide determinants each contain a unique 3,6-dideoxyhexose, namely abequose (3,6-dideoxy-D-xylo-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose), are α-linked to the 3-position of D-mannopyranose. The disaccharides were further derivatized with a linear aglycon that has a terminal amino group, and can be readily coupled to pertinent chains carrying a terminal thiol for the construction of self-assembled monolayers (SAMs). Efficient routes that employed a single 3,6-dideoxygenation step were developed for the synthesis of paratoside 15 and tyveloside 22.Key words: Salmonella O-antigens, lipopolysaccharide, abequose, paratose, tyvelose, 3,6-dideoxyhexose, deoxygenation, glycoside tethers, immobilization via pentenyl glycosides.


2021 ◽  
Vol 29 (3) ◽  
pp. 334-346
Author(s):  
Allison M. Weis ◽  
June L. Round

2012 ◽  
Vol 19 (5) ◽  
pp. 731-739 ◽  
Author(s):  
Miriam M. Ngundi ◽  
Bruce D. Meade ◽  
Stephen F. Little ◽  
Conrad P. Quinn ◽  
Cindi R. Corbett ◽  
...  

ABSTRACTAntibodies against the protective antigen (PA) component of anthrax toxin play an important role in protection against disease caused byBacillus anthracis. In this study, we examined defined combinations of PA-specific monoclonal antibodies for their ability to neutralize anthrax toxin in cell culture assays. We observed additive, synergistic, and antagonistic effects of the antibodies depending on the specific antibody combination examined and the specific assay used. Synergistic toxin-neutralizing antibody interactions were examined in more detail. We found that one mechanism that can lead to antibody synergy is the bridging of PA monomers by one antibody, with resultant bivalent binding of the second antibody. These results may aid in optimal design of new vaccines and antibody therapies against anthrax.


2010 ◽  
Vol 132 (30) ◽  
pp. 10239-10241 ◽  
Author(s):  
Matthias A. Oberli ◽  
Marco Tamborrini ◽  
Yu-Hsuan Tsai ◽  
Daniel B. Werz ◽  
Tim Horlacher ◽  
...  

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