Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0038362 (stomatitis)
 8,852 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Previously, we reported that expression of the murine beta 2-microglobulinb (beta 2mb) antigenic epitopes defined by the mAb S19.8 and 23 (SJL [beta 2ma] anti-B10.S beta 2mb]) was dependent upon association of beta 2m with MHC class I heavy chains. We have further explored the antigenic properties of beta 2m under circumstances requiring the induction of MHC class I surface expression with heavy chain-specific peptide-ligand. For the RMA-S cell line, which is class I surface null due to a defect in the TAP-2 peptide transporter, treatment with the H-2Kb-specific vesicular stomatitis virus-derived N p52-59 peptide resulted in the cell surface expression of the epitopes defined by the anti-H-2Kb mAb Y-3, as well as equally strong expression of the epitopes defined by the anti-beta 2mb mAb S19.8 and 23. Similarly, the FLU-NP p366-374 peptide induced H-2Db on the surface of RMA-S cells as determined by cytofluorometry with the mAb MKQ8; however, expression of the epitope defined by S19.8 was only partially recovered and no reactivity was observed for mAb 23. That the H-2Db heavy chain was assembled with beta 2mb on the cell surface was established from immunoprecipitation experiments with 125I-surface-radiolabeled RMA-S cells treated with FLU-NP p366-374; MKQ8 immunoprecipitated prominent heavy chain and beta 2m bands, whereas S19.8 and 23 isolated a weak beta 2m band (12-15% of that co-immunoprecipitated with MKQ8). These results are consistent with the observation that human beta 2m-deficient cells (designated FO-1) transfected with the B2mb allele were induced, in combination with the endogenous HLA class I heavy chains, to express the epitope defined by S19.8, but not mAb 23, whereas both were expressed when contransfection was performed with the H-2Kb gene. That the determinants recognized by S19.8 and 23 were formed by a discontinuous cluster of amino acids within beta 2m was established from experiments demonstrating that H-2Kb heavy chain assembled with a chimeric beta 2m molecule (comprising human beta 2m from 1-69 and mouse beta 2m from amino acid 70-99, including the polymorphic residue Ala 85) did not lead to expression of the S19.8 and 23 epitopes. The results of this study provide evidence that heavy chain polymorphism can affect the antigenic properties of beta 2m and offer insight into the basis by which CTL may react against beta 2mb when assembled with the H-2Kb molecule.
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PMID:MHC class I heavy chain-dependent expression of discontinuous antigenic epitopes on beta 2-microglobulinb is inducible with peptide-ligand. 753 Aug 67

With the use of monospecific rabbit anti-G protein and mouse monoclonal anti-H-2Kk, we have analyzed the spatial relationship of the serologically defined H-2Kk antigens and the major surface glycoprotein (G protein) of vesicular stomatitis virus (VSV) to those antigens recognized by B10.A (k, d) anti-VSV cytotoxic T lymphocytes (CTLs). The ability of monoclonal anti-H-2Kk or rabbit anti-G protein to inhibit specifically the cytolytic activity of B10.A anti-VSV CTLs indicates that the G protein and the H-2Kk molecules are in close proximity to the viral and H-2Kk antigens recognized by the anti-VSV (CTLs. By the method of sequential immunoprecipitation, we also demonstrated that only 10-30 percent of the serologically defined G and H-2Kk molecules are in the G-H-2Kk complexes.
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PMID:The spatial relationship of the viral and H-2 antigens recognized by anti-viral CTLs. 2245 20

Entry inhibitors are promising novel antivirals against hepatitis B virus (HBV) infection. The existing potential entry inhibitors have targeted the cellular receptor(s). In this study, we aim to develop the first entry inhibitor that inhibits HBV infection via targeting viral particles. The preS1 segment of the large envelope glycoprotein of HBV is essential for virion attachment and infection. Previously, we obtained a preS1-binding short peptide B10 by screening a phage display peptide library using the N-terminal half of preS1 (residues 1 to 60, genotype C). We report here that by means of concatenation of B10, we identified a quadruple concatemer 4B10 that displayed a markedly increased preS1-binding activity. The main binding site of 4B10 in preS1 was mapped to the receptor binding enhancing region. 4B10 blocked HBV attachment to hepatic cells and inhibited HBV infection of primary human and tupaia hepatocytes at low nanomolar concentrations. The 4B10-mediated inhibition of HBV infection is specific as it did not inhibit the infection of vesicular stomatitis virus glycoprotein pseudotyped lentivirus or human immunodeficiency virus type 1. Moreover, 4B10 showed no binding activity to hepatic cells. In conclusion, we have identified 4B10 as a promising candidate for a novel class of HBV entry inhibitors.
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PMID:Efficient Inhibition of Hepatitis B Virus Infection by a preS1-binding Peptide. 2738 14