Working Paper Article Version 1 This version is not peer-reviewed

The T Cell Receptor (TRB) Locus in Tursiops Truncatus: From Sequence to Structure of the Alpha/Beta Heterodimer in the Human/Dolphin Comparison

Version 1 : Received: 10 February 2021 / Approved: 11 February 2021 / Online: 11 February 2021 (13:26:26 CET)

How to cite: Linguiti, G.; Kossida, S.; Pierri, C.L.; Javado-Michaloud, J.; Folch, G.; Massari, S.; Lefranc, M.; Ciccarese, S.; Antonacci, R. The T Cell Receptor (TRB) Locus in Tursiops Truncatus: From Sequence to Structure of the Alpha/Beta Heterodimer in the Human/Dolphin Comparison. Preprints 2021, 2021020286 Linguiti, G.; Kossida, S.; Pierri, C.L.; Javado-Michaloud, J.; Folch, G.; Massari, S.; Lefranc, M.; Ciccarese, S.; Antonacci, R. The T Cell Receptor (TRB) Locus in Tursiops Truncatus: From Sequence to Structure of the Alpha/Beta Heterodimer in the Human/Dolphin Comparison. Preprints 2021, 2021020286

Abstract

Bottlenose dolphin (Tursiops truncatus) belongs to the Cetartiodactyla and similarly to the other cetaceans represent the most successful mammalian colonization of the aquatic environment. Here we report a genomic, evolutionary and expression study of Tursiops truncatus T cell receptor beta (TRB) genes. Although the organization of the dolphin TRB locus is similar to that of the other artiodactyl species, with three in tandem D-J-C clusters located at its 3’ end, its uniqueness is given by the reduction of the total length due essentially to the absence of duplications and to the deletions that have drastically reduced the number of the germline TRBV genes. We have analyzed the relevant mature transcripts from two subjects. The simultaneous availability of rearranged TRA and TRB cDNA from the peripheral blood of one of the two specimens, and the human/dolphin amino acids multi sequence alignments, allowed us to calculate the most likely interactions at the protein interface between the alpha/beta heterodimer in complex with major histocompatibility class I (MH1) protein. Interacting amino acids located in the CDR-IMGT of the dolphin variable V alpha and beta domains were identified. According to comparative modelisation, the atome pair contact sites analysis between the human MH1 grove (G) domains and the TR V domains confirms conservation of the structure of the dolphin TR/pMH.

Subject Areas

T cell receptor; dolphin genome ; TRB locus; TRBV; TRBJ; TRBD and TRBC genes; TRA and TRB gene expression analysis; multiple sequence alignments (MSA); 3D modelisation; IMGT

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