| Literature DB >> 19197722 |
Ghofran Al Qudaihi1, Cynthia Lehe, Muna Negash, Monther Al-Alwan, Hazem Ghebeh, Said Yousuf Mohamed, Abu-Jafar Mohammed Saleh, Hind Al-Humaidan, Abdelghani Tbakhi, Anne Dickinson, Mahmoud Aljurf, Said Dermime.
Abstract
The Wilms tumor antigen 1 (WT1) antigen is over-expressed in human leukemias, making it an attractive target for immunotherapy. Most WT1-specific Cytotoxic T Lymphocytes (CTLs) described so far displayed low avidity, limiting its function. To improve the immunogenicity of CTL epitopes, we replaced the first-amino-acid of two known immunogenic WT1-peptides (126 and 187) with a tyrosine. This modification enhances 126Y analogue-binding ability, triggers significant number of IFN-gamma-producing T cells (P = 0.0003), induces CTL that cross-react with the wild-type peptide, exerts a significant lytic activity against peptide-loaded-targets (P = 0.0006) and HLA-A0201-matched-leukemic cells (P = 0.0014). These data support peptide modification as a feasible approach for the development of a leukemia-vaccine.Entities:
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Year: 2009 PMID： 19197722 DOI： 10.1080/10428190802578478
Source DB: PubMed Journal: Leuk Lymphoma ISSN： 1026-8022