Role of antigen-binding cells in the formation of producers of antibodies and antigen-dependent nonspecific immunoglobulins

1985 ◽  
Vol 100 (3) ◽  
pp. 1234-1237
Author(s):  
M. G. Agadzhanyan ◽  
T. B. Megrabyan ◽  
E. V. Sidorova
Keyword(s):  
Antigen Binding ◽  
Nonspecific Immunoglobulins

scholarly journals The mycoplasma surface proteins MIB and MIP promote the dissociation of the antibody-antigen interaction

2021 ◽  
Vol 7 (10) ◽  
pp. eabf2403
Author(s):  
Pierre Nottelet ◽  
Laure Bataille ◽  
Geraldine Gourgues ◽  
Robin Anger ◽  
Carole Lartigue ◽  
...  
Keyword(s):  
Surface Proteins ◽  
Mycoplasma Species ◽  
Antigen Binding ◽  
Antigen Binding Site ◽  
Fab Fragment ◽  
Cryo Electron Microscopy ◽  
Antigen Complex ◽  
Antigen Interaction ◽  
Immunoglobulin Binding

Mycoplasma immunoglobulin binding (MIB) and mycoplasma immunoglobulin protease (MIP) are surface proteins found in the majority of mycoplasma species, acting sequentially to capture antibodies and cleave off their VH domains. Cryo–electron microscopy structures show how MIB and MIP bind to a Fab fragment in a “hug of death” mechanism. As a result, the orientation of the VL and VH domains is twisted out of alignment, disrupting the antigen binding site. We also show that MIB-MIP has the ability to promote the dissociation of the antibody-antigen complex. This system is functional in cells and protects mycoplasmas from antibody-mediated agglutination. These results highlight the key role of the MIB-MIP system in immunity evasion by mycoplasmas through an unprecedented mechanism, and open exciting perspectives to use these proteins as potential tools in the antibody field.

Role of the mobility of antigen binding site in high affinity antibody elucidated by surface plasmon resonance

2016 ◽  
Vol 161 (1) ◽  
pp. 37-43 ◽  
Author(s):  
Natsuki Fukuda ◽  
Yoshiaki Suwa ◽  
Makiyo Uchida ◽  
Yoshihiro Kobashigawa ◽  
Hideshi Yokoyama ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Binding Site ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Antigen Binding ◽  
Antigen Binding Site ◽  
High Affinity

Role of various subpopulations of B lymphocytes in production of antigen-induced nonspecific immunoglobulins

1999 ◽  
Vol 128 (6) ◽  
pp. 1251-1253
Author(s):  
I. N. Chernyshova ◽  
T. K. Borisova ◽  
Yu. A. Emel'yantseva ◽  
E. V. Sidorova
Keyword(s):  
B Lymphocytes ◽  
Nonspecific Immunoglobulins

scholarly journals Role of Tyr Residues in the Contact Region of Anti-lysozyme Monoclonal Antibody HyHEL10 for Antigen Binding

1995 ◽  
Vol 270 (31) ◽  
pp. 18551-18557 ◽  
Author(s):  
Kouhei Tsumoto ◽  
Kyoko Ogasahara ◽  
Yoshitaka Ueda ◽  
Kimitsuna Watanabe ◽  
Katsuhide Yutani ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Contact Region ◽  
Antigen Binding

scholarly journals Hapten-specific T cell responses to 4-hydroxy-3-nitrophenyl acetyl. V. Role of idiotypes in the suppressor pathway.

1980 ◽  
Vol 152 (1) ◽  
pp. 161-169 ◽  
Author(s):  
J Z Weinberger ◽  
R N Germain ◽  
B Benacerraf ◽  
M E Dorf
Keyword(s):  
Cell Population ◽  
Direct Evidence ◽  
Suppressor Cells ◽  
Suppressor Cell ◽  
Cell Types ◽  
Induction Phase ◽  
Antigen Binding ◽  
Binding Properties ◽  
Cell Responses

4-Hydroxy-3-nitrophenyl (NP) derivatized syngeneic spleen cells injected intravenously stimulate maturation of an antigen-binding, idiotype-bearing induction-phase suppressor cell population, as well as an idiotype-binding anti-idiotype-bearing effector-phase suppressor cell population. Both cell types are present simultaneously in the spleen cell population 7-d after their induction. Furthermore, the cell population with antigen-binding properties can, in the presence of NP-derivatized syngeneic cells, induce a population of effector suppressor cells. The precursors of the effector suppressor population are not sensitive to concentrations of cyclophosphamide which prevented the generation of induction phase suppressor cells. These data provide direct evidence in support of the theory of network regulation of immune suppression. X

scholarly journals B cells discriminate HIV-1 Envelope protein affinities by sensing antigen binding association rates

2022 ◽  
Author(s):  
Md. Alamgir Hossain ◽  
Kara Anasti ◽  
Brian Watts ◽  
Kenneth Cronin ◽  
Advaiti Pai Kane ◽  
...  
Keyword(s):  
B Cells ◽  
B Cell ◽  
Cell Activation ◽  
Neutralizing Antibody ◽  
Antigen Binding ◽  
B Cell Activation ◽  
Kinetic Rates ◽  
Env Protein ◽  
Hiv 1

HIV-1 Envelope (Env) proteins designed to induce neutralizing antibody responses allow study of the role of affinities (equilibrium dissociation constant, KD) and kinetic rates (association/dissociation rates) on B cell antigen recognition. It is unclear whether affinity discrimination during B cell activation is based solely on Env protein binding KD, and whether B cells discriminate between proteins of similar affinities but that bind with different kinetic rates. Here we used a panel of Env proteins and Ramos B cell lines expressing IgM BCRs with specificity for CD4 binding-site broadly neutralizing (bnAb) or a precursor antibody to study the role of antigen binding kinetic rates on both early (proximal/distal signaling) and late events (BCR/antigen internalization) in B cell activation. Our results support a kinetic model for B cell activation in which Env protein affinity discrimination is based not on overall KD, but on sensing of association rate and a threshold antigen-BCR half-life.

scholarly journals Mutational landscape of antibody variable domains reveals a switch modulating the interdomain conformational dynamics and antigen binding

2017 ◽  
Vol 114 (4) ◽  
pp. E486-E495 ◽  
Author(s):  
Patrick Koenig ◽  
Chingwei V. Lee ◽  
Benjamin T. Walters ◽  
Vasantharajan Janakiraman ◽  
Jeremy Stinson ◽  
...  
Keyword(s):  
Somatic Mutations ◽  
Conformational Dynamics ◽  
Human Antibody ◽  
Antigen Binding ◽  
Mutational Landscape ◽  
Antibody Maturation ◽  
Binding Function ◽  
Variable Domains

Somatic mutations within the antibody variable domains are critical to the immense capacity of the immune repertoire. Here, via a deep mutational scan, we dissect how mutations at all positions of the variable domains of a high-affinity anti-VEGF antibody G6.31 impact its antigen-binding function. The resulting mutational landscape demonstrates that large portions of antibody variable domain positions are open to mutation, and that beneficial mutations can be found throughout the variable domains. We determine the role of one antigen-distal light chain position 83, demonstrating that mutation at this site optimizes both antigen affinity and thermostability by modulating the interdomain conformational dynamics of the antigen-binding fragment. Furthermore, by analyzing a large number of human antibody sequences and structures, we demonstrate that somatic mutations occur frequently at position 83, with corresponding domain conformations observed for G6.31. Therefore, the modulation of interdomain dynamics represents an important mechanism during antibody maturation in vivo.

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