2013
DOI: 10.1007/s00253-013-5447-z
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Recombinant expression of hydroxylated human collagen in Escherichia coli

Abstract: Collagen is the most abundant protein in the human body and thereby a structural protein of considerable biotechnological interest. The complex maturation process of collagen, including essential post-translational modifications such as prolyl and lysyl hydroxylation, has precluded large-scale production of recombinant collagen featuring the biophysical properties of endogenous collagen. The characterization of new prolyl and lysyl hydroxylase genes encoded by the giant virus mimivirus reveals a method for pro… Show more

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Cited by 76 publications
(69 citation statements)
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“…Saccharomyces cerevisiae and Pichia pastoris yeasts were the first to be investigated, given that as eukaryotes, they are capable of glycosylation. Considering that certain viruses harbor genes encoding prolyl 4‐hydroxylase and lysyl hydroxylase, the coexpression of a human collagen type III with mimivirus prolyl and lysyl hydroxylases in Escherichia coli has recently been reported . However, the yield of such systems is very low (e.g., 15 mg L −1 for yeast, 60 mg L −1 for baculovirus, 90 mg L −1 in E. coli ), thus limiting broad commercialization potential.…”
Section: Sources Of Collagenmentioning
confidence: 99%
“…Saccharomyces cerevisiae and Pichia pastoris yeasts were the first to be investigated, given that as eukaryotes, they are capable of glycosylation. Considering that certain viruses harbor genes encoding prolyl 4‐hydroxylase and lysyl hydroxylase, the coexpression of a human collagen type III with mimivirus prolyl and lysyl hydroxylases in Escherichia coli has recently been reported . However, the yield of such systems is very low (e.g., 15 mg L −1 for yeast, 60 mg L −1 for baculovirus, 90 mg L −1 in E. coli ), thus limiting broad commercialization potential.…”
Section: Sources Of Collagenmentioning
confidence: 99%
“…[110] As its purification can be complicated by heterogeneities between preparations and the possibility of disease transmission, [111] its large-scale production in a recombinant platform would be advantageous. This is hindered by the requirement for proline hydroxylation, which has proven difficult in E. coli, though expression can be achieved by exploiting folding catalyst over-expression [112] while collagen mimetics of various formats have also been efficiently expressed in E. coli. [113,114] Native collagen is frequently expressed, however, in non-procaryotic expression systems such as yeast, [115] insect [115c] or plant [116] species for purification and utilization.…”
Section: Expression Systems For Recombinant Productsmentioning
confidence: 99%
“…La producción de colágena tipo I de humano en la levadura Saccharomyces cerevisiae, reveló que los extremo N-o C-del propéptido de colágeno (procolágeno) así como la ausencia de hidroxilación en prolina, no son necesarios para la formación de la triple hélice [28] para fragmentos definidos [22,29] . [29][30][31][32][33][34] . Adicionalmente, se han empleado animales o plantas transgénicas en los cuales se introduce el DNA foráneo utilizando técnicas convencionales como microinyección del DNA deseado directamente en un óvulo [35] .…”
Section: Colágenaunclassified
“…Como hemos mencionado, la colágena se puede producir en una gran variedad de sistemas que difieren en facilidad, reproducibilidad, relación costo-eficiencia y rendimiento. Hemos descrito una gama de sistemas de expresión de colágenas de origen humano en bacterias, levaduras y células de mamífero, insecto y vegetales como el tabaco y el maíz (recombinantes) y colágenas de origen bacteriano (colágena no animal), como materiales de uso potencial en biomedicina [29][30][31][32]42] .…”
Section: Uso De La Colágena Recombinante En Ingeniería De Tejidosunclassified