| pubmed-article:20587542 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20587542 | lifeskim:mentions | umls-concept:C1705358 | lld:lifeskim |
| pubmed-article:20587542 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:20587542 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:20587542 | lifeskim:mentions | umls-concept:C1540292 | lld:lifeskim |
| pubmed-article:20587542 | lifeskim:mentions | umls-concept:C1425745 | lld:lifeskim |
| pubmed-article:20587542 | lifeskim:mentions | umls-concept:C1705357 | lld:lifeskim |
| pubmed-article:20587542 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:20587542 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:20587542 | pubmed:dateCreated | 2010-7-23 | lld:pubmed |
| pubmed-article:20587542 | pubmed:abstractText | The programmed death-1 (PD-1) molecule is involved in peripheral tolerance and in the immune escape mechanisms during chronic viral infections and cancer. PD-1 interacts with two ligands, PD-L1 and PD-L2. We have investigated the molecular mechanisms of PD-1 interactions with its ligands by surface plasmon resonance and cell surface binding as well as the ability of the two ligands to compete for PD-1 binding. PD-L1 and PD-L2 bound PD-1 with comparable affinities, but striking differences were observed at the level of the association and dissociation characteristics. PD-L1, but not PD-L2, had a delayed interaction reminiscent of a phenomenon of conformational transition. These mechanisms were confirmed by using PD-L1 mAbs that delayed the dissociation of PD-L1 from PD-1. This mechanism was not restricted to PD-1 binding since PD-L1 behaved in a similar manner with its second ligand, CD80. Finally, we could demonstrate that PD-L1 and PD-L2 competed for PD-1 binding and conversely, an antagonist PD-1 mAb blocked both PD-L1 and PD-L2 binding to PD-1 and strongly enhanced T-cell proliferation. These data further emphasize the differential molecular mechanisms of interaction of PD-L1 and PD-L2 with PD-1, and suggest possible new approach for the therapy of chronic infection, cancer and transplantation. | lld:pubmed |
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| pubmed-article:20587542 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:20587542 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:20587542 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20587542 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:20587542 | pubmed:issn | 1460-2377 | lld:pubmed |
| pubmed-article:20587542 | pubmed:author | pubmed-author:OliveDanielD | lld:pubmed |
| pubmed-article:20587542 | pubmed:author | pubmed-author:TrunehAlemseg... | lld:pubmed |
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| pubmed-article:20587542 | pubmed:author | pubmed-author:PastorSoniaS | lld:pubmed |
| pubmed-article:20587542 | pubmed:author | pubmed-author:NunèsJacques... | lld:pubmed |
| pubmed-article:20587542 | pubmed:author | pubmed-author:GhiottoMargue... | lld:pubmed |
| pubmed-article:20587542 | pubmed:author | pubmed-author:SerriariNacer... | lld:pubmed |
| pubmed-article:20587542 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20587542 | pubmed:volume | 22 | lld:pubmed |
| pubmed-article:20587542 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20587542 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20587542 | pubmed:pagination | 651-60 | lld:pubmed |
| pubmed-article:20587542 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:20587542 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20587542 | pubmed:articleTitle | PD-L1 and PD-L2 differ in their molecular mechanisms of interaction with PD-1. | lld:pubmed |
| pubmed-article:20587542 | pubmed:affiliation | Institut National de la Santé et de la Recherche Médicale, Unité 891, Centre de Recherche en Cancérologie de Marseille, Marseille, France. | lld:pubmed |
| pubmed-article:20587542 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20587542 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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