Cell
ArticleGenetic analysis of monoclonal antibody and HIV binding sites on the human lymphocyte antigen CD4
References (33)
- et al.
Rapid immunofluorescent screening procedure using primary cell cultures or tissue sections
J. Immunol. Meth.
(1984) Selective extraction of polyoma DNA from infected mouse cell cultures
J. Mol. Biol.
(1967)- et al.
Delineation of a region of the human immunodeficiency virus type I gp120 glycoprotein critical for interaction with the CD4 receptor
Cell
(1987) - et al.
A specific assay measuring binding of 1251-gp120 from HIV to T4+/CD4+ cells
J. Immunol. Meth.
(1987) - et al.
The isolation and nucleotide sequence of a cDNA encoding the T cell surface protein T4: a new member of the immunoglobulin gene family
Cell
(1985) - et al.
The T4 gene encodes the AIDS virus receptor and is expressed in the immune system and the brain
Cell
(1986) - et al.
The CD4 antigen: physiological ligand and HIV receptor
Cell
(1988) A year in the life of the immunoglobulin superfamily
Immunol. Today
(1987)- et al.
A soluble recombinant polypeptide comprising the amino-terminal half of the extracellular region of the CD4 molecule contains an active binding site for human immunodeficiency virus
- et al.
High mutation frequency in DNA transfected into mammalian cells
Expression of the HTLV-III envelope gene by a recombinant vaccinia virus
Nature
Monoclonal anti-idiotypic antibody mimics the CD4 receptor and binds human immunodeficiency virus
The CD4(T4) antigen is an essential component of the receptor for the AIDS retrovirus
Nature
Neutralisation of HIV isolates by anti-idiotypic antibodies which mimic the T4(CD4) epitope: a potential AIDS vaccine
Lancet
Structure of a novel Bence-Jones protein (RHE) fragment at 1.6 angstrom resolution
J. Mol. Biol.
Reactivity of the workshop CD4 and CD6 panel antibodies with the respective purified antigens
Cited by (283)
Electroinsertion: An Electrical Method for Protein Implantation into Cell Membranes
2012, Guide to Electroporation and ElectrofusionReduced monomeric CD4 is the preferred receptor for HIV
2010, Journal of Biological ChemistryCitation Excerpt :The nature of this conformational change is unknown, although residues located in domain 2 have been implicated in the change. Domain 2 residues Pro121, Pro122, Gly123 (32), and Asn164 (33) were found to be important for a high affinity CD4-gp120 interaction, and antibodies that bind to epitopes that encompass these residues block HIV syncitia formation and/or infection (29, 33–37). These residues are also within two stretches of domain 2 amino acids, 120–127 or 163–166, that from molecular modeling studies have been proposed to constitute a hinge that bends upon HIV binding to domain 1 (12).
Molecular and functional analysis of the antigen receptor of Art v 1-specific helper T lymphocytes
2008, Journal of Allergy and Clinical ImmunologyCitation Excerpt :Conventionally, altered peptide ligands are created by introducing single amino acid changes into peptide ligands of MHC, generating peptides able to influence autoimmune diseases but also allergies.39-42 The Ii-based allergen (peptide) expression system in combination with, for example, error-prone PCR approaches,43 might serve as a novel high-throughput screening approach for such purposes. Moreover, expressible allergen-specific TCRs might also lay the groundwork for the generation of valuable in vivo systems in the future, such as TCR tg “allergy mice” based on a human disease and based on human immune receptors.
Critical role of Arg<sup>59</sup> in the high-affinity gp120-binding region of CD4 for human immunodeficiency virus type 1 infection
2007, VirologyCitation Excerpt :Based on crystal structure analyses, phenylalanine at position 43 (Phe43) and arginine at position 59 (Arg59) within the high-affinity gp120-binding region of CD4 are predicted to make multiple contacts centered on Asp368, Glu370, and Trp427 of the C3 and C4 regions of gp120 (Kwong et al., 1998, 2000). Specifically, it has been shown that Asp368 of gp120 forms a salt bridge with Arg59 of the CD4 receptor (Brodsky et al., 1990; Peterson and Seed, 1988; Wyatt and Sodroski, 1998), and that the viral gp120 and cellular CD4 molecule form hydrogen bonds, which bridge the two proteins (Wyatt and Sodroski, 1998). These interactions are believed to trigger conformational changes in the viral gp120 (Sattentau and Moore, 1991) that facilitate binding of the gp120/CD4 complex to the cellular co-receptor (Deng et al., 1996; Salzwedel et al., 2000; Trkola et al., 1996; Wu et al., 1996).
LFA-1 and associated diseases: The dark side of a receptor
2006, Clinical and Applied Immunology ReviewsCitation Excerpt :Furthermore, it is of considerable interest that viruses have evolved to bind to the same regions of CD4 and ICAM-1 as do their cell adhesion counter-structures. Indeed, HIV binds to the first and part of the second immunoglobulin-like domains of CD4 [75,94–96], the region that binds to major histocompatibility complex class II molecules [95]. In the same way, LFA-1 and rhinoviruses bind to overlapping but distinct regions of the first immunoglobulin-like domain of ICAM-1 [97–100].