Functional cysteine-less subunits of the transporter associated with antigen processing (TAP1 and TAP2) by de novo gene assembly

Within the adaptive immune system the transporter associated with antigen processing (TAP) plays a pivotal role in loading of peptides onto major histocompatibility (MHC) class I molecules. As a central tool to investigate the structure and function of the TAP complex, we created cysteine-less human...

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Veröffentlicht in:	FEBS letters 2003-01, Vol.533 (1), p.42-46
Hauptverfasser:	Heintke, Susanne, Chen, Min, Ritz, Ulrike, Lankat-Buttgereit, Brigitte, Koch, Joachim, Abele, Rupert, Seliger, Barbara, Tampé, Robert
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - metabolism Adenosine triphosphate-binding cassette transporter Amino Acid Substitution Antigen Presentation Antigen processing ATP Binding Cassette Transporter, Subfamily B, Member 2 ATP Binding Cassette Transporter, Subfamily B, Member 3 ATP-Binding Cassette Transporters - chemistry ATP-Binding Cassette Transporters - genetics ATP-Binding Cassette Transporters - metabolism Biological Transport, Active Cell Line Cysteine - chemistry Cysteine-scanning mutagenesis ECL, enhanced chemiluminescence FACS, fluorescence-activated cell sorting Histocompatibility Antigens Class I - metabolism Humans Membrane protein MHC, major histocompatibility complex Models, Molecular NBD, nucleotide-binding domain Protein Subunits Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism TAP, transporter associated with antigen processing TMD, transmembrane domain Transfection
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Zusammenfassung:	Within the adaptive immune system the transporter associated with antigen processing (TAP) plays a pivotal role in loading of peptides onto major histocompatibility (MHC) class I molecules. As a central tool to investigate the structure and function of the TAP complex, we created cysteine-less human TAP subunits by de novo gene synthesis, replacing all 19 cysteines in TAP1 and TAP2. After expression in TAP-deficient human fibroblasts, cysteine-less TAP1 and TAP2 are functional with respect to adenosine triphosphate (ATP)-dependent peptide transport and inhibition by ICP47 from herpes simplex virus. Cysteine-less TAP1 and TAP2 restore maturation and intracellular trafficking of MHC class I molecules to the cell surface.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/S0014-5793(02)03746-8