Anaerobic sulfatase maturase AslB from Escherichia coli activates human recombinant iduronate-2-sulfate sulfatase (IDS) and N -acetylgalactosamine-6-sulfate sulfatase (GALNS)

Alméciga-Díaz, Carlos J.; Tolosa-Díaz, Andrés Dario; Pimentel, Luisa; Bonilla, Yahir Andres; Rodríguez-López, Alexander; Espejo-Mojica, Angela Johana; Patiño, Juan David; Sánchez, Oscar F.; Santos, Janneth González

doi:10.1016/j.gene.2017.08.043

Cited by 5 publications

(4 citation statements)

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“…However, prIDS activity was significantly lower than that reported for the enzyme produced in mammalian cells, for which enzyme activity levels between 1.6 and 2.5 × 10 6 U mg −1 have been reported . This marked difference in enzyme activity could be associated with the lack of formylglycine‐generating enzymes (FGE) similar to those described in mammals or bacteria . FGE catalyzes the formation of a formylglycine (FGly) residue from a cysteine at the active site of the enzyme .…”

Section: Resultsmentioning

confidence: 75%

Production and characterization of a human lysosomal recombinant iduronate‐2‐sulfatase produced inPichia pastoris

Pimentel

Rodríguez-López

Diaz

et al. 2018

Biotech and App Biochem

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Hunter syndrome (Mucopolysaccharidosis II, MPS II) is an X-linked lysosomal storage disease produced by the deficiency of the lysosomal enzyme iduronate-2-sulfatase (IDS). Currently, MPS II patients are mainly treated with enzyme replacement therapy (ERT) using recombinant enzymes produced in mammalian cells. As an alternative, several studies have shown the production of active and therapeutic forms of lysosomal proteins in microorganisms. In this paper, we report the production and characterization of a recombinant IDS produced in the yeast Pichia pastoris (prIDS). We evaluated the effect of culture conditions and gene sequence optimization on prIDS production. The results showed that the highest production of prIDS was obtained at oxygen-limited conditions using a codon-optimized IDS cDNA. The purified enzyme showed a final activity of 12.45 nmol mg H and an apparent molecular mass of about 90 kDa. The highest stability was achieved at pH 6.0, and prIDS also showed high stability in human serum. Noteworthy, the enzyme was taken up by culture cells in a dose-dependent manner through mannose receptors, which allowed the delivery of the enzyme to the lysosome. In summary, these results show the potential of Pichia pastoris as a host to produce an IDS intended for a MPS II ERT.

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Section: Resultsmentioning

confidence: 75%

Production and characterization of a human lysosomal recombinant iduronate‐2‐sulfatase produced inPichia pastoris

Pimentel

Rodríguez-López

Diaz

et al. 2018

Biotech and App Biochem

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“…In mammals, FGE overexpression significantly increases the activity of sulfatases, favoring the production of enzymes with higher enzyme activity [ 14 , [46] , [47] , [48] , [49] ]. Our group shown that overexpression of E. coli AslB (an anSME-type enzyme) increased the activity of recombinant human sulfatase (i.e., GALNS and IDS) produced in E. coli by up to 4.6-fold [ 50 ]. The co-expression of AslB, together with the implementation of synthetic biology approaches [ 35 ] could be used in the future to improve the production and activity of the rGALNS produced in E. coli .…”

Section: Resultsmentioning

confidence: 99%

“…This may limit the translation of this enzyme to the clinics. Future studies should focus on increasing the rGALNS opt Gly activity through strategies such as co-expression of E. coli sulfatase maturing enzyme AslB, implementing synthetic biology approaches, and regulating the cellular stress response [ 35 , 50 ]. Additionally, other N-glycans should also be taken into consideration, including those with mannose-6-phosphate ends.…”

Section: Resultsmentioning

confidence: 99%

Novel human recombinant N-acetylgalactosamine-6-sulfate sulfatase produced in a glyco-engineered Escherichia coli strain

Pimentel-Vera,

Rodríguez-López,

Espejo-Mojica

et al. 2024

Heliyon

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“…Contributions from Colombia in basic and applied research for MPS IVA have included production and characterization of recombinant GALNS in bacteria [110,111,112,113,114] and yeast [115,116], the design of viral vectors for gene therapy [117,118,119,120,121,122,123,124], the identification of pharmacological chaperones [125], and the generation of induced pluripotent stem cell lines [126]. Results from recombinant GALNS showed that N-glycosylations are not necessary for production of active enzyme but for cell uptake [112], and that recombinant GALNS produced in the yeast P. pastoris is taken up by cultured cells and reach the lysosomes, in which it can mediate the reduction of KS level [116].…”

Section: Mucopolysaccharidosis Type Iva (Morquio a Syndrome)mentioning

confidence: 99%

A perspective on research, diagnosis, and management of lysosomal storage disorders in Colombia

Puentes-Tellez

Lerma-Barbosa

Garzón-Jaramillo

et al. 2020

Heliyon

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Lysosomal storage diseases (LSDs) are a group of about 50 inborn errors of metabolism characterized by the lysosomal accumulation of partially or non-degraded molecules due to mutations in proteins involved in the degradation of macromolecules, transport, lysosomal biogenesis or modulators of lysosomal environment. Significant advances have been achieved in the diagnosis, management, and treatment of LSDs patients. In terms of approved therapies, these include enzyme replacement therapy (ERT), substrate reduction therapy, hematopoietic stem cell transplantation, and pharmacological chaperone therapy. In this review, we summarize the Colombian experience in LSDs thorough the evidence published. We identified 113 articles published between 1995 and 2019 that included Colombian researchers or physicians, and which were mainly focused in Mucopolysaccharidoses, Pompe disease, Gaucher disease, Fabry disease, and Tay-Sachs and Sandhoff diseases. Most of these articles focused on basic research, clinical cases, and mutation reports. Noteworthy, implementation of the enzyme assay in dried blood samples, led to a 5-fold increase in the identification of LSD patients, suggesting that these disorders still remain undiagnosed in the country. We consider that the information presented in this review will contribute to the knowledge of a broad spectrum of LSDs in Colombia and will also contribute to the development of public policies and the identification of research opportunities.

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Anaerobic sulfatase maturase AslB from Escherichia coli activates human recombinant iduronate-2-sulfate sulfatase (IDS) and N -acetylgalactosamine-6-sulfate sulfatase (GALNS)

Cited by 5 publications

References 45 publications

Production and characterization of a human lysosomal recombinant iduronate‐2‐sulfatase produced inPichia pastoris

Production and characterization of a human lysosomal recombinant iduronate‐2‐sulfatase produced inPichia pastoris

Novel human recombinant N-acetylgalactosamine-6-sulfate sulfatase produced in a glyco-engineered Escherichia coli strain

A perspective on research, diagnosis, and management of lysosomal storage disorders in Colombia

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