|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
1
|
|
pubmed:dateCreated |
2001-6-21
|
|
pubmed:abstractText |
Complete activation of T cells requires two signals: an Ag-specific signal delivered via the TCR by the peptide-MHC complex and a second costimulatory signal largely provided by B7:CD28/CTLA-4 interactions. Previous studies have shown that B7 blockade can either ameliorate experimental autoimmune encephalomyelitis by interfering with CD28 signaling or exacerbate the disease by concomitant blockade of CTLA-4 interaction. Therefore, we developed a functional CD28 mimic to selectively block B7:CD28 interactions. The design, synthesis, and structural and functional properties of the CD28 free peptide, the end group-blocked CD28 peptide, and its retro-inverso isomer are shown. The synthetic T cell-costimulatory receptor peptides fold into a polyproline type II helical structure commonly seen in regions of globular proteins involved in transient protein-protein interactions. The binding determinants of CD28 can be transferred onto a short peptide mimic of its ligand-binding region. The CD28 peptide mimics effectively block the expansion of encephalitogenic T cells in vitro suggesting the potential usefulness of the peptides for the treatment of autoimmune disease conditions requiring down-regulation of T cell responses.
|
|
pubmed:grant |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
AIM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD28,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes, T-Lymphocyte,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Fc Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Immunosuppressive Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Myelin Basic Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell...,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Solutions,
http://linkedlifedata.com/resource/pubmed/chemical/myelin basic protein 1-11,
http://linkedlifedata.com/resource/pubmed/chemical/polyproline
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jul
|
|
pubmed:issn |
0022-1767
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
1
|
|
pubmed:volume |
167
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
578-85
|
|
pubmed:dateRevised |
2007-11-14
|
|
pubmed:meshHeading |
pubmed-meshheading:11418697-Amino Acid Motifs,
pubmed-meshheading:11418697-Amino Acid Sequence,
pubmed-meshheading:11418697-Animals,
pubmed-meshheading:11418697-Antigens, CD28,
pubmed-meshheading:11418697-Cells, Cultured,
pubmed-meshheading:11418697-Encephalomyelitis, Autoimmune, Experimental,
pubmed-meshheading:11418697-Epitopes, T-Lymphocyte,
pubmed-meshheading:11418697-Female,
pubmed-meshheading:11418697-Guinea Pigs,
pubmed-meshheading:11418697-Immunoglobulin Fc Fragments,
pubmed-meshheading:11418697-Immunosuppressive Agents,
pubmed-meshheading:11418697-Lymphocyte Activation,
pubmed-meshheading:11418697-Mice,
pubmed-meshheading:11418697-Mice, Inbred C57BL,
pubmed-meshheading:11418697-Mice, Transgenic,
pubmed-meshheading:11418697-Molecular Mimicry,
pubmed-meshheading:11418697-Molecular Sequence Data,
pubmed-meshheading:11418697-Myelin Basic Proteins,
pubmed-meshheading:11418697-Peptide Fragments,
pubmed-meshheading:11418697-Peptides,
pubmed-meshheading:11418697-Protein Binding,
pubmed-meshheading:11418697-Protein Conformation,
pubmed-meshheading:11418697-Protein Structure, Secondary,
pubmed-meshheading:11418697-Receptors, Antigen, T-Cell, alpha-beta,
pubmed-meshheading:11418697-Recombinant Fusion Proteins,
pubmed-meshheading:11418697-Solutions,
pubmed-meshheading:11418697-T-Lymphocytes
|
|
pubmed:year |
2001
|
|
pubmed:articleTitle |
A retro-inverso peptide mimic of CD28 encompassing the MYPPPY motif adopts a polyproline type II helix and inhibits encephalitogenic T cells in vitro.
|
|
pubmed:affiliation |
Department of Microbiology, College of Biological Sciences, Ohio State University, Columbus, OH 43210, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|
