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Image of CD4 co-receptor binding to MHC (Major Histocompatibility Complex) non-polymorphic region. In molecular biology, CD4 (cluster of differentiation 4) is a glycoprotein that serves as a co-receptor for the T-cell receptor (TCR). CD4 is found on the surface of immune cells such as helper T cells, monocytes, macrophages, and dendritic cells.
Boehme et al. demonstrated this interesting dual outcome by blocking the binding of CD4 to MHC-II which prevented the programmed cell death reaction that active T-cells typically display. [6] The CD4 receptor is composed of four concatamerized Ig-like domains and is anchored to the cell membrane by a single transmembrane domain.
CD4 immunoadhesin was first developed in the mid-1990s as a potential therapeutic agent and treatment for HIV/AIDS. The protein is a fusion of the extracellular domain of the CD4 receptor and the Fc domain of human immunoglobulin G (IgG), the most abundant antibody isotype in the human body. [1]
CR3 is a human cell surface receptor, found on polymorphonuclear leukocytes (mostly neutrophils), NK cells, and mononuclear phagocytes like macrophages, which is capable of recognizing and binding to many molecules found on the surfaces of invading bacteria. Binding to the receptor causes phagocytosis and destruction of the foreign cell. CD11c
The CD nomenclature was proposed and established in the 1st International Workshop and Conference on Human Leukocyte Differentiation Antigens (HLDA), held in Paris in 1982. [4] [5] This system was intended for the classification of the many monoclonal antibodies (mAbs) generated by different laboratories around the world against epitopes on the surface molecules of leukocytes (white blood cells).
The extracellular and transmembrane part of the coreceptor is from wild-type CD8 coreceptor, whereas the intracellular domain from CD4 coreceptor. [1] This model was created to examine role of coreceptor coupling to Lck (lymphocyte-specific protein tyrosine kinase) [1] as the CD4 and CD8 coreceptors have an Lck-binding site in their ...
Exposed on the surface of the viral envelope, the glycoprotein gp120 binds to the CD4 receptor on any target cell that has such a receptor, particularly the helper T-cell. Strains of HIV-1 have been isolated that are able to enter host cells that are CD4 negative. This CD4-independence is associated with spontaneous mutation in the env gene.
The binding of the antigen-MHC to the TCR complex and CD4 may also help the APC and the T h cell adhere during T h cell activation, but the integrin protein LFA-1 on the T cell and ICAM on the APC are the primary molecules of adhesion in this cell interaction. [citation needed]