Cargando…
CH2 Domain of Mouse IgG3 Governs Antibody Oligomerization, Increases Functional Affinity to Multivalent Antigens and Enhances Hemagglutination
Mouse IgG3 is highly protective against several life-threatening bacteria. This isotype is the only one among mouse IgGs that forms non-covalent oligomers, has increased functional affinity to polyvalent antigens, and efficiently agglutinates erythrocytes. IgG3 also triggers the complement cascade....
Autores principales: | Klaus, Tomasz, Bereta, Joanna |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5974032/ https://www.ncbi.nlm.nih.gov/pubmed/29875771 http://dx.doi.org/10.3389/fimmu.2018.01096 |
Ejemplares similares
-
Mouse Antibody of IgM Class is Prone to Non-Enzymatic Cleavage between CH1 and CH2 Domains
por: Klaus, Tomasz, et al.
Publicado: (2018) -
Agglutinating mouse IgG3 compares favourably with IgMs in typing of the blood group B antigen: Functionality and stability studies
por: Klaus, Tomasz, et al.
Publicado: (2016) -
Interactions of IgG1 CH2 and CH3 Domains with FcRn
por: Ying, Tianlei, et al.
Publicado: (2014) -
Mouse IgG3 binding to macrophage-like cells is prevented by deglycosylation of the antibody or by Accutase treatment of the cells
por: Karabasz, Alicja, et al.
Publicado: (2021) -
The binding affinity of human IgG for its high affinity Fc receptor is determined by multiple amino acids in the CH2 domain and is modulated by the hinge region
Publicado: (1991)