Bioinformatic analysis of the human recombinant iduronate 2-sulfate sulfatase

Edwin D. Morales-Álvarez, Claudia M. Rivera-Hoyos, Patricia Landázuri, Raúl A. Poutou-Piñales, Aura M. Pedroza-Rodríguez

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

Mucopolysaccharidosis type II is a human recessive disease linked to the X chromosome caused by deficiency of lysosomal enzyme Iduronate 2-Sulfate Sulfatase (IDS), which leads to accumulation of glycosaminoglycans in tissues and organs. The human enzyme has been expressed inEscherichia coli and Pichia pastoris in attempt to develop more successful expression systems that allow the production of recombinant IDS for Enzyme Replacement Therapy (ERT). However, the preservation of native signal peptide in the sequence has caused conflicts in processing and recognition in the past, which led to problems in expression and enzyme activity. With the main object being the improvement of the expression system, we eliminate the native signal peptide of human recombinant IDS. The resulting sequence showed two modified codons, thus, our study aimed to analyze computationally the nucleotide sequence of the IDSnh without signal peptide in order to determine the 3D structure and other biochemical properties to compare them with the native human IDS (IDSnh). Results showed that there are no significant differences between both molecules in spite of the two-codon modifications detected in the recombinant DNA sequence.

Original languageEnglish
Pages (from-to)124-132
Number of pages9
JournalOpen Microbiology Journal
Volume10
DOIs
StatePublished - 01 May 2016

Keywords

  • Bioinformatics
  • Hunter syndrome
  • Iduronate 2-sulfate sulfatase
  • Native signal peptide
  • Three dimensional protein structure

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