We are analyzing https://link.springer.com/article/10.1007/s00251-004-0749-z.

Title:
Characterization of the peptide-binding specificity of Mamu-A*11 results in the identification of SIV-derived epitopes and interspecies cross-reactivity | Immunogenetics
Description:
The SIV-infected Indian rhesus macaque is the most established model of HIV infection, providing insight into pathogenesis and a system for testing novel vaccines. However, only a limited amount of information is available regarding the peptide-binding motifs and epitopes bound by their class I and class II MHC molecules. In this study, we utilized a library of over 1,000 different peptides and a high throughput MHC-peptide binding assay to detail the binding specificity of the rhesus macaque class I molecule Mamu-A*11. These studies defined the fine specificity of primary anchor positions, and dissected the role of secondary anchors, for peptides of 8–11 residues in length. This detailed information was utilized to develop size-specific polynomial algorithms to predict Mamu-A*11 binding capacity. Testing SIVmac239-derived Mamu-A*11 binding peptides for recognition by peripheral blood mononuclear cells (PBMC) from Mamu-A*11-positive, SIV-infected macaques, identified five novel SIV-derived Mamu-A*11 epitopes. Finally, we detected extensive cross-reactivity at the binding level between Mamu-A*11 and the mouse H-2 class I molecule Kk. Further experiments revealed that three out of four Mamu-A*11 binding peptides which bound Kk and were immunogenic in Kk mice were also recognized in Mamu-A*11-infected macaques. This is the first detailed description of mouse-macaque interspecies cross-reactivity, potentially useful in testing novel vaccines in mice and macaques.
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Keywords {🔍}

google, scholar, article, sette, sidney, class, immunol, immunodeficiency, virus, watkins, simian, binding, peptide, virol, epitopes, cytotoxic, rhesus, allen, mamua, mhc, molecules, major, complex, histocompatibility, mothe, ctl, southwood, macaques, altman, lymphocytes, del, guercio, peptides, molecule, oconnor, letvin, kubo, grey, infection, wilson, kuroda, cas, pubmed, immunogenetics, specificity, identification, jing, epitope, dzuris, schmitz,

Topics {✒️}

nih-niaid contracts no1-ai-95362 marie-france del guercio mouse-macaque interspecies cross-reactivity cytotoxic-t-lymphocyte responses elicited overlapping peptide-binding repertoires immunodominant h-2dk-restricted epitope peptide/major histocompatibility class month download article/chapter cytotoxic t-lymphocyte responses siv-infected rhesus monkeys dna-vaccinated rhesus monkeys high-dose challenge dominant epitope-specific cytotoxic detected extensive cross-reactivity hla-a24 human class cytokine-augmented dna vaccination t-cell hybridoma class detect cytokine-secreting murine simian immunodeficiency virus rhesus macaque class counting antigen-specific cd8 rhesus macaque detected human immunodeficiency virus b7-restricted ctl response jeff alexander related subjects common hla molecules rhesus mhc class interspecies cross-reactivity full article pdf testing sivmac239-derived mamu allele-specific motifs revealed major hla class huynh-hoa bui 17-restricted epitopes derived conserved mhc class mhc/peptide interactions siv-infected macaques immunodominant ctl epitope rhesus macaques vaccinated multiepitope dna vaccination privacy choices/manage cookies mouse h-2 class peptide binding motif cd8 responses specific gag-specific cytotoxic acute phase cytotoxic del guercio mf disease progression [ siv-derived epitopes

Questions {❓}

In one of two cytotoxic T-lymphocyte epitopes bound by a high-frequency major histocompatibility complex class I molecule, Mamu-A*02: a paradigm for virus evolution and persistence?

Schema {🗺️}

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         headline:Characterization of the peptide-binding specificity of Mamu-A*11 results in the identification of SIV-derived epitopes and interspecies cross-reactivity
         description:The SIV-infected Indian rhesus macaque is the most established model of HIV infection, providing insight into pathogenesis and a system for testing novel vaccines. However, only a limited amount of information is available regarding the peptide-binding motifs and epitopes bound by their class I and class II MHC molecules. In this study, we utilized a library of over 1,000 different peptides and a high throughput MHC-peptide binding assay to detail the binding specificity of the rhesus macaque class I molecule Mamu-A*11. These studies defined the fine specificity of primary anchor positions, and dissected the role of secondary anchors, for peptides of 8–11 residues in length. This detailed information was utilized to develop size-specific polynomial algorithms to predict Mamu-A*11 binding capacity. Testing SIVmac239-derived Mamu-A*11 binding peptides for recognition by peripheral blood mononuclear cells (PBMC) from Mamu-A*11-positive, SIV-infected macaques, identified five novel SIV-derived Mamu-A*11 epitopes. Finally, we detected extensive cross-reactivity at the binding level between Mamu-A*11 and the mouse H-2 class I molecule Kk. Further experiments revealed that three out of four Mamu-A*11 binding peptides which bound Kk and were immunogenic in Kk mice were also recognized in Mamu-A*11-infected macaques. This is the first detailed description of mouse-macaque interspecies cross-reactivity, potentially useful in testing novel vaccines in mice and macaques.
         datePublished:2005-03-04T00:00:00Z
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      headline:Characterization of the peptide-binding specificity of Mamu-A*11 results in the identification of SIV-derived epitopes and interspecies cross-reactivity
      description:The SIV-infected Indian rhesus macaque is the most established model of HIV infection, providing insight into pathogenesis and a system for testing novel vaccines. However, only a limited amount of information is available regarding the peptide-binding motifs and epitopes bound by their class I and class II MHC molecules. In this study, we utilized a library of over 1,000 different peptides and a high throughput MHC-peptide binding assay to detail the binding specificity of the rhesus macaque class I molecule Mamu-A*11. These studies defined the fine specificity of primary anchor positions, and dissected the role of secondary anchors, for peptides of 8–11 residues in length. This detailed information was utilized to develop size-specific polynomial algorithms to predict Mamu-A*11 binding capacity. Testing SIVmac239-derived Mamu-A*11 binding peptides for recognition by peripheral blood mononuclear cells (PBMC) from Mamu-A*11-positive, SIV-infected macaques, identified five novel SIV-derived Mamu-A*11 epitopes. Finally, we detected extensive cross-reactivity at the binding level between Mamu-A*11 and the mouse H-2 class I molecule Kk. Further experiments revealed that three out of four Mamu-A*11 binding peptides which bound Kk and were immunogenic in Kk mice were also recognized in Mamu-A*11-infected macaques. This is the first detailed description of mouse-macaque interspecies cross-reactivity, potentially useful in testing novel vaccines in mice and macaques.
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      dateModified:2005-03-04T00:00:00Z
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         SIV
         MHC
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