Ngoc Tuan Tran and Wei-Min Wang

DOI: 10.14456/sjst-psu.2018.124

pp. 1017 - 1025

Abstract

Cysteine cathepsins are described as lysosomal proteases with housekeeping and highly specialised functions in many
organisms. In this study, cysteine cathepsins were identified from the transcriptome profile of blunt snout bream (Megalobrama
amblycephala). A total of 41 cysteine cathepsin-like sequences were found and divided into groups of cathepsin (Cts): B, C, F, H,
K, L, S, and Z. Twenty-nine of these sequences contained coding sequences, encoding 92-473 amino acids, which exhibited the
highest (78%-95%) homology to the counterparts from zebrafish (Danio rerio). Multiple sequence alignment of the amino acids
showed highly conserved domains among the cysteine cathepsins of M. amblycephala to its homologs. The putative proteins,
including maCtsb1, maCtsc1, maCtsf2, maCtsh1, maCtsk5, maCtsl5, maCtss1, and maCtsz5 were characterised and structured
using in silico methods. Additionally, codon usage of full length open reading frame sequences of these cathepsins was analysed.
This study provided basic information for further studies on the specific functions of cysteine cathepsins of M. amblycephala in
the future.