Disease relevance of Epitope Mapping

• Mutant conformation of p53. Precise epitope mapping using a filamentous phage epitope library [1].
• Overlapping 30-amino-acid-long peptides derived from the p24 protein sequence of HIV-1 were used in an epitope-mapping system [2].
• Human immunodeficiency virus type 1-neutralizing monoclonal antibodies which react with p17 core protein: characterization and epitope mapping [3].
• Although epitope mapping has identified residues on the human papillomavirus (HPV) major capsid protein (L1) that are important for binding mouse monoclonal antibodies, epitopes recognized by human antibodies are not known [4].
• Epitope-mapping studies define two major neutralization sites on the vaccinia virus extracellular enveloped virus glycoprotein B5R [5].

High impact information on Epitope Mapping

• High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis [6].
• Fine epitope mapping using nested peptides showed that clones using identical TCR beta chains, identical V alpha, but a different J alpha recognized distinct, nonoverlapping epitopes in the TPO 535-551 region [7].
• Here we report on the cDNA cloning and partial epitope mapping of the 100-kD autoantigen from human placenta and HeLa lambda gt11 libraries [8].
• In this report, we show that V1 bears structural similarities with V kappa regions through detailed epitope mapping of 26 CD4 mAbs [9].
• Our approach was to determine serial changes over a 12-18-mo period in response to an epitope-mapping series of 265 12-mer peptides of myelin proteolipid protein (PLP) by patients with isolated monosymptomatic demyelinating syndromes (IMDS), a group of distinct clinical disorders with variable rates of progression to MS [10].

Biological context of Epitope Mapping

• These epitope mapping data were compared with four putative TNF cell receptor binding sites presented in the literature [11].
• Evolutionarily conserved sequences of striated muscle myosin heavy chain isoforms. Epitope mapping by cDNA expression [12].
• Using the polymerase chain reaction to modify expression plasmids for epitope mapping [13].
• Synaptonemal complex proteins: occurrence, epitope mapping and chromosome disjunction [14].
• Resistance to hydrolysis by proteinase K and epitope mapping argue that the beta-sheet structures were formed by the interaction of residues lying between 109 and 141 [15].

Anatomical context of Epitope Mapping

• Antibody epitope mapping of untensioned microfibrils revealed the juxtaposition of epitopes at the COOH terminus and near the proline-rich region, and of two internal epitopes that would be 42-nm apart in unfolded molecules, which infers intramolecular folding [16].
• This study reaffirms the predictive value of A(k)-binding motifs in epitope mapping and doubles the number of known pathogenic T cell determinants in Tg that are now found scattered throughout the length of this large autoantigen [17].
• T and B cell epitope mapping revealed major and minor T and B cell epitopes in the N-terminal, first, and second loops of CCR5 [18].
• Epitope mapping of human thyroglobulin. Heterogeneous recognition by thyroid pathologic sera [19].
• Asparaginase display of polypeptides in the periplasm of Escherichia coli: potential rapid pepscan technique for antigen epitope mapping [20].

Associations of Epitope Mapping with chemical compounds

• Structure/function analysis of the integrin beta 1 subunit by epitope mapping [21].
• Antibody epitope mapping revealed that cleavage occurred at one or two target sites for caspases within the amino acid region YEWD31 (downward arrow) AGD34 (downward arrow) A, removing the N-terminal BH4 region known to be essential for the death-protective activity of Bcl-2 [22].
• Epitope mapping with recombinant fVIII fragments indicated that LE2E9 recognized the fVIII C1 domain, but not the Arg2150His-substituted C1 domain [23].
• Epitope mapping of inhibitory antibodies against platelet glycoprotein Ibalpha reveals interaction between the leucine-rich repeat N-terminal and C-terminal flanking domains of glycoprotein Ibalpha [24].
• Furthermore, the acetylcholine receptor-like epitope of the midsize neurofilament (NF-M) was identified by peptide epitope mapping [25].

Gene context of Epitope Mapping

• The soluble domain variants of BGP are ideal molecules for epitope mapping [26].
• Epitope mapping studies identified peptides from the sequence of the autoantigen that preferentially induced interleukin-10 production, rather than proliferation, and demonstrated that many contain naturally processed epitopes [27].
• Given that ADAMTS-13 may interact physiologically with various receptors or ligands, the occurrence, distribution, and the epitope mapping of nonneutralizing antibodies will be an important area for future research [28].
• Future epitope-mapping studies with other MRP-specific MAbs win provide additional insights into the topology of MRP, and may help to identify functionally important regions of this protein [29].
• These interactions are consistent with epitope mapping studies and with the observation that MRK-16 is specific for human class I P-glycoprotein [30].

Analytical, diagnostic and therapeutic context of Epitope Mapping

• LKM1-positive sera obtained from 16 patients with AIH and 16 with HCV infection were used as probes to perform a complete epitope mapping of CYP2D6 [31].
• The globular head domain of titin extends into the center of the sarcomeric M band. cDNA cloning, epitope mapping and immunoelectron microscopy of two titin-associated proteins [32].
• Synthetic peptides derived from the epitope mapping were reacted with sera in enzyme-linked immunosorbent assay [33].
• IgE and IgG4 epitope mapping by microarray immunoassay reveals the diversity of immune response to the peanut allergen, Ara h 2 [34].
• Utilizing a highly characterized monoclonal antibody library we employed ELISA, Western blot, immunocytochemical, and MHC epitope mapping techniques to determine which MHCs were present in the fibers of these muscles at different stages of development [35].

References