Journal
MOLECULAR IMMUNOLOGY
Volume 45, Issue 13, Pages 3567-3572Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.molimm.2008.05.014
Keywords
CD80; CD274; surface plasmon resonance; adhesion; antibody
Categories
Funding
- NIH/NIAID [R01 38310, R01 46414, P01 AI56299 BAA 05-11, P01 AI39671]
- Foundation for the National Institutes of Health
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Numerous studies have pointed to the role of programmed death-1 ligand 1 (PD-L1) in regulating tolerance, chronic infection, and tumor immunity. Recently, we have identified murine B7-1 as a new binding partner for murine PD-L1. Human and mouse B7-1 share only 46% identity, leading us to question whether human B7-1 and PD-L1 can participate in a similar interaction. Here we show that human B7-1 can interact with human PD-L1 with affinity greater than that of B7-1 with CD28, but less than that of B7-1 with CTLA-4 or of PD-L1 with PD-1. We characterize a series of anti-human PD-L1 monoclonal antibodies and identify antibodies that can block interactions of PD-L1 with B7-1, PD-1, or both. Since PD-L1 and CD28 on T cells may compete for B7-1 as a binding partner and CD8 T cells may express high or low levels of CD28, we examined when PD-L1 and CD28 are co-expressed on CD8 T cells. We compared the time-course and extent of PD-L1 induction on CD8 CD28(high) versus CD28(low) T cells following stimulation with anti-CD3. We show that PD-L1 is induced to a higher level on CD28high T cells than on CD28(low) T cells upon activation. These results suggest that PD-L1 may play an important and undervalued role on human T cells. (C) 2008 Elsevier Ltd. All rights reserved.
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