NDLI: Identification of a CD4 Domain Required for Interleukin-16 Binding and Lymphocyte Activation

Content Provider	Journal of Biological Chemistry (JBC)
Author	Liu, Yu Cruikshank, William W. O’Loughlin, Terence O’Reilly, Phillip Center, David M. Kornfeld, Hardy
Abstract	Interleukin-16 (IL-16) activates CD4+ cells, possibly by direct interaction with CD4. IL-16 structure and function are highly conserved across species, suggesting similar conservation of a putative IL-16 binding site on CD4. Comparison of the human CD4 amino acid sequence with that of several different species revealed that immunoglobulin-like domain 4 is the most conserved extracellular region. Potential interaction of this domain with IL-16 was studied by testing murine D4 sequence-based oligopeptides for inhibition of IL-16 chemoattractant activity and inhibition of IL-16 binding to CD4 in vitro. Three contiguous 12-residue D4 region peptides (designated A, B, and C) blocked IL-16 chemoattractant activity, with peptide B the most potent. Peptides A and B were synergistic for inhibition, but peptide C was not. Peptides A and B also blocked IL-16 binding to CD4 in vitro, whereas peptide C did not. CD4, in addition to its known function as a receptor for major histocompatibility complex class II, contains a binding site for IL-16 in the D4 domain. The D4 residues required for IL-16 binding overlap those previously shown to participate in CD4-CD4 dimerization following class II major histocompatibility complex binding, providing a mechanistic explanation for the known function of IL-16 to inhibit the mixed lymphocyte reaction.
Related Links	http://www.jbc.org/content/274/33/23387.abstract
Ending Page	23395
Starting Page	23387
Page Count	9
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	33
Volume Number	274
DOI	10.1074/jbc.274.33.23387
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	1999-08-13
Access Restriction	Open
Subject Keyword	Interleukin-16 (IL-16) Recombinant IL-16 (rIL-16) Major histocompatibility complex (MHC) Amino acid (aa) GlutathioneS-transferase (GST) Human immunodeficiency virus-1 (HIV-1) Human immunodeficiency virus-2 (HIV-2) Fluorescein isothiocyanate (FITC) Interleukin-2 receptor (IL-2R) Polyacrylamide gel electrophoresis (PAGE) PROTEIN CHEMISTRY AND STRUCTURE
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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