scholarly journals Broadly Distributed Chemical Reactivity of Natural Antibodies Expressed in Coordination with Specific Antigen Binding Activity

2003 ◽  
Vol 278 (22) ◽  
pp. 20436-20443 ◽  
Author(s):  
Stephanie Planque ◽  
Hiroaki Taguchi ◽  
Gary Burr ◽  
Gita Bhatia ◽  
Sangeeta Karle ◽  
...  
Keyword(s):  
Chemical Reactivity ◽  
Specific Antigen ◽  
Binding Activity ◽  
Natural Antibodies ◽  
Antigen Binding

scholarly journals Human rheumatoid factor crossidiotypes. I. WA and BLA are heat-labile conformational antigens requiring both heavy and light chains.

1986 ◽  
Vol 164 (5) ◽  
pp. 1809-1814 ◽  
Author(s):  
V Agnello ◽  
J L Barnes
Keyword(s):  
Rheumatoid Factor ◽  
Primary Structure ◽  
Binding Activity ◽  
Light Chains ◽  
Heat Denaturation ◽  
Antigen Binding ◽  
Rheumatoid Factors ◽  
Simple Method ◽  
Heat Labile

Evidence was obtained that both the WA and BLA crossidiotype (XId) groups are conformational antigens requiring both L and H chains and that with heat denaturation the antigens that define the XIds and antigen-binding activity are lost in parallel. In contrast, the primary structure-dependent crossreactive idiotype (CRI), PSL2, which is only weakly detected on native Wa and Bla monoclonal rheumatoid factors (mRFs), became prominently detected on the heated Wa and Bla mRFs. Heat denaturation may provide a simple method for distinguishing Ids determined by conformational antigen from primary structure-dependent Ids. In addition to heat denaturation, some acid conditions commonly used for preparation of RFs were also found to cause marked loss of Id antigen. The finding of PSL2-CRI on Bla mRF indicates that this Id is not unique to the WA XId.

Antibodies to Rotaviruses in Chickens' Eggs: A Potential Source of Antiviral Immunoglobulins Suitable for Human Consumption

PEDIATRICS ◽  
1988 ◽  
Vol 81 (2) ◽  
pp. 291-295
Author(s):  
Robert H. Yolken ◽  
Flora Leister ◽  
Siok-Bi Wee ◽  
Robin Miskuff ◽  
Steven Vonderfecht
Keyword(s):  
Binding Activity ◽  
Human Consumption ◽  
Antigen Binding ◽  
Rotavirus Gastroenteritis ◽  
Potential Source ◽  
Egg Products ◽  
Egg Yolks ◽  
The Individual ◽  
Antibody Levels ◽  
Infants And Young Children

The prevalence of antibodies to human rotaviruses in commercially available eggs and egg products that are suitable for human consumption was investigated. The yolks of virtually all of the individual eggs and pasteurized pooled egg preparations contain antirotavirus antibodies detectable by means of enzyme immunoassay systems. Also, the eggs and egg preparations are capable of inhibiting the growth of two strains of rotaviruses in tissue culture. Chromatographic studies indicated that the antigen-binding activity is limited largely to the immunoglobulin fractions of the egg yolks. The antibody levels in eggs can be increased by the immunization of hens with purified rotavirus preparations, and the immunoglobulins isolated from the eggs of immunized hens can prevent the development of rotavirus gastroenteritis in experimentally infected animals. Egg preparations might serve as a practical source of antiviral antibodies suitable for consumption by infants and young children.

scholarly journals The generation of the human mab RabD4 specific to the rabies virus glycoprotein and characterization thereof

2019 ◽  
Vol 485 (3) ◽  
pp. 370-373
Author(s):  
Е. N. Ilina ◽  
E. V. Solopova ◽  
Т. К. Aliev ◽  
М. V. Larina ◽  
D. S. Balabashin ◽  
...  
Keyword(s):  
B Cells ◽  
Rabies Virus ◽  
Binding Activity ◽  
Antigen Binding ◽  
Rabies Virus Glycoprotein ◽  
Neutralizing Activity ◽  
Virus Glycoprotein ◽  
Peripheral B Cells

We generated a novel human neutralizing human mAb RabD4 against rabies virus glycoprotein using in vitro stimulation human peripheral B cells produced from immunized donor. It was revealed that the human mAb RabD4 demonstrated high antigen-binding activity and virus-neutralizing activity in the FAVN test with the CVS-11 rabies virus.

Time- and dose-dependent digoxin redistribution by digoxin-specific antigen binding fragments in a rat model

Toxicology ◽  
1999 ◽  
Vol 137 (2) ◽  
pp. 117-127 ◽  
Author(s):  
C Renard ◽  
E Weinling ◽  
B Pau ◽  
J.-M Scherrmann
Keyword(s):  
Rat Model ◽  
Specific Antigen ◽  
Antigen Binding ◽  
Dose Dependent

scholarly journals Induction of idiotype-bearing, nuclease-specific helper T cells by in vivo treatment with anti-idiotype.

1981 ◽  
Vol 154 (1) ◽  
pp. 24-34 ◽  
Author(s):  
G G Miller ◽  
P I Nadler ◽  
Y Asano ◽  
R J Hodes ◽  
D H Sachs
Keyword(s):  
T Cells ◽  
Network Theory ◽  
Individual Cell ◽  
Binding Activity ◽  
Helper T Cells ◽  
Antigen Binding ◽  
Receptor Interactions ◽  
Detectable Antigen

Treatment of BALB/c mice with purified pig anti-(BALB/c anti-nuclease) anti-idiotypic antibodies has been found to induce the appearance of idiotype-bearing immunoglobulins (Id') in the serum of these mice in the absence of detectable antigen binding activity. This phenomenon appeared to require T cells in the hosts because no Id' was detected in the serum of nude mice similarly treated. Furthermore, the spleens of BALB/c mice treated with anti-idiotype were found to contain helper T cells capable of providing help in an in vitro plaque-forming cell response to trinitrophenyl-nuclease equivalent to that provided by helper T cells from the spleens of nuclease-primed animals. Helper T cells from both anti-idiotype-treated and nuclease-treated animals were found to be antigen-specific and to be similarly susceptible to elimination by treatment with anti-idiotype plus complement. Therefore, treatment with both antigen and anti-idiotype appeared to prime similar populations of antigen-specific helper T cells, while having different effects on the induction of antibody. These findings are consistent with the network theory of receptor interactions in the immune response, and may provide a means for studying individual cell populations involved in such interactions.

Androgen-dependent and DNA binding-independent association of androgen receptor with chromatic regions coding androgen-induced non-coding RNAs

2021 ◽  
Author(s):  
Takahiro Sawada ◽  
Koichi Nishimura ◽  
Jinichi Mori ◽  
Yoshiaki Kanemoto ◽  
Alexander Kouzmenko ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Sites ◽  
Specific Antigen ◽  
Binding Activity ◽  
Lncap Cells ◽  
Coding Regions ◽  
Dna Binding Activity ◽  
Genome Wide ◽  
Non Coding Rnas ◽  
Independent Association

Abstract Androgen induces the binding of its receptor (AR) to androgen-responsive elements (AREs), while genome-wide studies showed that most androgen-induced AR binding sites on chromatin were unrelated to AREs. Enhancer RNAs (eRNAs), a class of non-coding RNAs(ncRNAs), are transcribed from super-enhancers (SEs), and trigger the formation of large ribonucleoprotein (RNP) condensates of transcription factors. By in silico search, an SE is found to be located on the locus of KLK3 that encodes prostate specific antigen (PSA). On the KLK3 SE, androgen-induced expression of ncRNAs was detected and designated as KLK3eRNAs in LNCaP cells, and androgen-induced association of AR and FOXA1 on the KLK3eRNA coding regions was detected. Such androgen-induced association of an AR mutant lacking DNA binding activity on the KLK3eRNA coding regions was undetectable on an exogenous ARE. Thus, the present findings suggest a molecular basis of androgen-induced association of AR with chromatin on ARE-unrelated sequences.

Expression of functional eGFP-fused antigen-binding fragment of ranibizumab in Pichia pastoris

Bioimpacts ◽  
2021 ◽  
Author(s):  
Shirin Movaghar Asareh ◽  
Tahereh Savei ◽  
Sareh Arjmand ◽  
Seyed Omid Ranaei Siadat ◽  
Fataneh Fatemi ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Fluorescent Protein ◽  
Antibody Fragment ◽  
Binding Activity ◽  
Age Related Macular Degeneration ◽  
Light Chains ◽  
Antigen Binding ◽  
Active Structure ◽  
Age Related ◽  
Fragment Antigen Binding

Introduction: Ranibizumab is a mouse monoclonal antibody fragment antigen-binding (Fab) against human vascular endothelial growth factor-A (VEGF-A), inhibiting angiogenesis. This antibody is commercially produced in Escherichia coli host and used to treat wet age-related macular degeneration (AMD).Methods: In this study, the heavy and light chains of ranibizumab were expressed in Pichia pastoris. The expressed chains were incubated overnight at 4°C for interaction. The formation of an active structure was evaluated based on the interaction with substrate VEGF-A using an indirect ELISA, and an electrochemical setup. Furthermore, reconstruction of split enhanced green fluorescent protein (eGFP) reporter, chimerized at the C-terminus of the heavy and light chains, was used to characterize chains’ interaction. Results: P. pastoris efficiently expressed designed constructs and secreted them into the culture medium. The anti-Fab antibody detected the constructed Fab structure in western blot analysis. Reconstruction of the split reporter confirmed the interaction between heavy and light chains. The designed ELISA and electrochemical setup results verified the binding activity of the recombinant Fab structure against VEGF-A. Conclusion: In this work, we indicated that the heavy and light chains of ranibizumab Fab fragments (with or without linkage to split parts of eGFP protein) were produced in P. pastoris. The fluorescence of reconstructed eGFP was detected after incubating the equal ratio of chimeric-heavy and light chains. Immunoassay and electrochemical tests verified the bioactivity of constructed Fab. The data suggested that P. pastoris could be considered a potential efficient eukaryotic host for ranibizumab production.

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