Ferret T-Cell Surface Glycoprotein Cd4 Primacu™ ELI

T-cell surface glycoprotein CD4, is a single-pass type I membrane protein.

CD4 contains three Ig-like C2-type (immunoglobulin-like) domains and one Ig-like V-type (immunoglobulin-like) domain.

CD4 is a glycoprotein expressed on the surface of T helper cells, regulatory T cells, monocytes, macrophages, and dendritic cells.

The CD4 surface determinant, previously associated as a phenotypic marker for helper/inducer subsets of T lymphocytes, has now been critically identified as the binding/entry protein for human immunodeficiency viruses (HIV).

The human CD4 molecule is readily detectable on monocytes, T lymphocytes, and brain tissues.

All human tissue sources of CD4 bind radiolabeled gp120 to the same relative degree; however, the murine homologous protein, L3T4, does not bind the HIV envelope protein.

CD4 is a co-receptor that assists the T cell receptor (TCR) to activate its T cell following an interaction with an antigen-presenting cell.

Using its portion that resides inside the T cell, CD4 amplifies the signal generated by the TCR.

CD4 interacts directly with MHC class II molecules on the surface of the antigen-presenting cell via its extracellular domain.

The CD4 molecule is currently the object of intense interest and investigation both because of its role in normal T-cell function, and because of its role in HIV infection.

CD4 is a primary receptor used by HIV-1 to gain entry into host T cells.

HIV infection leads to a progressive reduction of the number of T cells possessing CD4 receptors.Viral protein U (VpU) of HIV-1 plays an important role in downregulation of the main HIV-1 receptor CD4 from the surface of infected cells.

Physical binding of VpU to newly synthesized CD4 in the endoplasmic reticulum is an early step in a pathway leading to proteasomal degradation of CD4.

Amino acids in both helices found in the cytoplasmic region of VpU in membrane-mimicking detergent micelles experience chemical shift perturbations upon binding to CD4, whereas amino acids between the two helices and at the C-terminus of VpU show no or only small changes, respectively.

Paramagnetic spin labels were attached at three sequence positions of a CD4 peptide comprising the transmembrane and cytosolic domains of the receptor.

VpU binds to a membrane-proximal region in the cytoplasmic domain of CD4