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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.
CD4-Ig works by mimicking the binding of CD4 to HIV, thereby preventing the virus from infecting T-helper cells. HIV infects T-helper cells by binding to the CD4 receptor and the co-receptor CCR5 or CXCR4. CD4-Ig binds to the viral envelope glycoprotein gp120, which is responsible for HIV binding to CD4. By binding to gp120, CD4-Ig prevents the ...
As well as being involved in forming a complex with MHC-II with TCR to control T-cell fate, the CD4 receptor is infamously the primary receptor that HIV envelope glycoprotein GP120 binds to. [6] In comparison, CD28 acts as a ‘co-coreceptor’ (costimulatory receptor) for the MHC-II binding with TCR and CD4. CD28 increases the IL-2 secretion ...
Since CD4 receptor binding is the most obvious step in HIV infection, gp120 was among the first targets of HIV vaccine research. Efforts to develop HIV vaccines targeting gp120, however, have been hampered by the chemical and structural properties of gp120, which make it difficult for antibodies to bind to it. gp120 can also easily be shed from the surface of the virus and captured by T cells ...
Antigen presentation: MHC molecules bind to both T cell receptor and CD4/CD8 co-receptors on T lymphocytes, and the antigen epitope held in the peptide-binding groove of the MHC molecule interacts with the variable Ig-Like domain of the TCR to trigger T-cell activation [26]
Low CD4 + predicted greater likelihood of intensive care unit admission, and CD4 + cell count was the only parameter that predicted length of time for viral RNA clearance. [42] Despite the reduced levels of CD4 + , COVID-19 patients with severe disease had higher levels of T h 1 CD4 + cells than patients with moderate disease. [ 43 ]
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The immunoglobulin domain, also known as the immunoglobulin fold, is a type of protein domain that consists of a 2-layer sandwich of 7-9 antiparallel β-strands arranged in two β-sheets with a Greek key topology, [1] [2] consisting of about 125 amino acids.