Skip to main content


Springer Nature is making Coronavirus research free. View research | View latest news | Sign up for updates

Fig. 1 | BMC Molecular Biology

Fig. 1

From: Immunoglobulin T from sea bass (Dicentrarchus labrax L.): molecular characterization, tissue localization and expression after nodavirus infection

Fig. 1

Alignment of the predicted sea bass IgT heavy chain amino acid sequence with other known IgT molecules. The amino acids of the signal peptide in the sea bass sequence are in italics. The position of the framework (FR) and CDR regions for the sea bass IgT V-DOMAIN (following the IMGT numbering) is indicated above the sequences, together with the J region, the four CH domains and the secretory tail; in this region the typical conserved amino acids in the sea bass sequence are in bold and italics. The N-linked glycosylation site in the sea bass IgT sequence is evidenced (see the CH3 domain). The conserved amino acids are indicated with an asterisk below the sequences, while dot and semicolon showed amino acids with conserved physical and chemical properties. The conserved cysteine (in bold and underlined) and tryptophan (in bold) residues that are required for the correct folding of the immunoglobulin superfamily (IgSF) CH domains are highlighted along the sequences. The conserved cysteine residues possibly involved in the disulphide bond with the IgT light chain and the ones related to the possible polymerization with other IgT heavy chains are evidenced in bold during the sequences. Accession numbers: Oncorhynchus mykiss (rainbow trout) AAW66978; Larimichthys crocea (large yellow croaker) XP_010754058; Thunnus orientalis (Pacific blue tuna) AHC31432; Dicentrarchus labrax (sea bass) KM410929; Siniperca chuatsi (mandarin fish) AAY42141; Epinephelus coioides (orange-spotted grouper) GU182366

Back to article page