caa a22 4500 467907390 CHVBK 20180406152838.0 cr unu---uuuuu 170328e20060601xx s 000 0 eng 10.1007/s00251-006-0103-8 doi (NATIONALLICENCE)springer-10.1007/s00251-006-0103-8 Characterization of porcine TAP genes: alternative splicing of TAP1 [Elektronische Daten] [Carmen García-Borges, Bounleut Phanavanh, Mark Crew] The transporter associated with antigen processing (TAP) is a heterodimer composed of TAP1 and TAP2 subunits that belong to the ATP-binding cassette family of transporters. TAP translocates small peptides (usually 8- to 12-amino-acid-long) from the cytosol to the endoplasmic reticulum for subsequent loading onto the major histocompatibility complex (MHC) class I molecules. The translocated peptides are required for the stable cell surface expression of MHC class I molecules. Virus-encoded proteins, which inhibit TAP activity, include ICP47 from herpes simplex virus and US6 from human cytomegalovirus. We have previously shown that ICP47 downregulated porcine MHC class I [swine leukocyte Ag class I (SLA I)] cell-surface expression in the pig epithelial cell line PK(15). Here we show that SLA I cell-surface expression in the pig epithelial cell line LLC-PK1 is relatively unaffected by expression of ICP47. Anticipating that this might be due to differences in the primary structure of TAP1 or TAP2 expressed by these two cell lines, cDNAs from PK(15) and LLC-PK1 encoding the complete open reading frames of porcine TAP1 and TAP2 were cloned and sequenced. Porcine TAP1 and TAP2 exhibited 80% amino acid identity with their human orthologs. Two splice variants of TAP1 were found. In LLC-PK1 cells, an alternatively spliced TAP1 transcript was detected, which was predicted to encode a protein with nine fewer amino acids. While the deleted amino acids may be in close proximity to the putative peptide/ICP47-binding site, we were unable to demonstrate that this imparted an apparent resistance to the effects of ICP47 on SLA I surface expression. Springer-Verlag, 2006 TAP nationallicence SLA class I nationallicence HSV ICP47 nationallicence García-Borges Carmen Department of Biochemistry & Molecular Biology, University of Arkansas for Medical Sciences, 151 Research, 4300 West 7th Street, 72205, Little Rock, Arkansas, USA aut Phanavanh Bounleut Department of Microbiology & Immunology, University of Arkansas for Medical Sciences, 151 Research, 4300 West 7th Street, 72205, Little Rock, Arkansas, USA aut Crew Mark Central Arkansas Veterans Healthcare System, University of Arkansas for Medical Sciences, 151 Research, 4300 West 7th Street, 72205, Little Rock, Arkansas, USA aut Immunogenetics Springer-Verlag 58/5-6(2006-06-01), 374-382 0093-7711 58:5-6<374 2006 58 251 https://doi.org/10.1007/s00251-006-0103-8 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00251-006-0103-8 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- García-Borges Carmen Department of Biochemistry & Molecular Biology, University of Arkansas for Medical Sciences, 151 Research, 4300 West 7th Street, 72205, Little Rock, Arkansas, USA aut NATIONALLICENCE 700 1- Phanavanh Bounleut Department of Microbiology & Immunology, University of Arkansas for Medical Sciences, 151 Research, 4300 West 7th Street, 72205, Little Rock, Arkansas, USA aut NATIONALLICENCE 700 1- Crew Mark Central Arkansas Veterans Healthcare System, University of Arkansas for Medical Sciences, 151 Research, 4300 West 7th Street, 72205, Little Rock, Arkansas, USA aut NATIONALLICENCE 773 0- Immunogenetics Springer-Verlag 58/5-6(2006-06-01), 374-382 0093-7711 58:5-6<374 2006 58 251 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer