TCR binding differs for a bacterial superantigen (SEE) and a viral superantigen (Mtv-9)
| Autor: | A Popowicz, A Molano, A Marinescu, R P Sekaly, J D Fraser, C Ciurli, David N. Posnett, L Liao |
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| Rok vydání: | 1996 |
| Předmět: |
Models
Molecular medicine.drug_class Receptors Antigen T-Cell alpha-beta Molecular Sequence Data Immunology chemical and pharmacologic phenomena Enterotoxin Plasma protein binding Biology Lymphocyte Activation Monoclonal antibody medicine.disease_cause Polymerase Chain Reaction Enterotoxins parasitic diseases medicine Superantigen Humans Immunology and Allergy Amino Acid Sequence Binding site Fluorescent Antibody Technique Indirect Gene Alleles Mutation Binding Sites Superantigens T-cell receptor Articles Flow Cytometry Virology Molecular biology Calcium Protein Binding Signal Transduction |
| Zdroj: | The Journal of Experimental Medicine |
| ISSN: | 1540-9538 0022-1007 |
| Popis: | Both superantigens (SAG) and many anti-TCR monoclonal antibodies (mAb) have specificity for the V beta region of the TCR encoded by TCRBV genes. For instance the bacterial SAG staphylococcal enterotoxin E (SEE), the retroviral SAG MTV-9 and the mAb OT145 each react with human T cells expressing BV6S7. This BV gene encodes two common alleles. We found that SEE and the mAb preferentially activate T cells expressing BV6S7*1 as opposed to BV6S7*2, but Mtv-9 activates T cells expressing either allele. Thus binding to the TCR differs between the two SAGs. A mutation in the TCR HVR-4 region of BV6S7*1 (G72E), where the two BV6S7 alleles differ, indicated that HVR-4 is a component of the binding site for SEE and for the mAb OT145. BV6S7*2 has a charged E72 which may result in electrostatic repulsion of SEE, as SEE contains a similarly acidic aspartic acid residue at a TCR interaction site (204D). |
| Databáze: | OpenAIRE |
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