Influencia del a-Factor sobre la expresión de IDShr en Pichia pastoris: Revisión sistemática de literatura y análisis computacional

Carlos E. Barragán; Homero Sáenz; Raúl Alberto Poutou; Marcela María Mercado; Luis A. Barrera

doi:10.22490/24629448.339

Vol. 3 No. 4 (2005)

Published

2005-12-15

PDF (Spanish)

How to Cite

Barragán, C. E., Sáenz, H., Poutou, R. A., Mercado, M. M., & Barrera, L. A. (2005). Influence of a-Factor Over the Expression of Hrids in: Literature Review and Computational Analysis. NOVA Biomedical Sciences Journal, 3(4), 80-91. https://doi.org/10.22490/24629448.339

Download Citation

Metrics

Metrics Loading ...

Influence of a-Factor Over the Expression of Hrids in: Literature Review and Computational Analysis.

DOI: https://doi.org/10.22490/24629448.339

Section

Article of Systematic Review (before OJS)

Carlos E. Barragán Instituto de Errores Innatos del Metabolismo

Homero Sáenz Instituto de Errores Innatos del Metabolismo, Decanato de Medicina, Universidad Centroccidental Lisandro Alvarado,Barquisimeto, Venezuela

Raúl Alberto Poutou Instituto de Errores Innatos del Metabolismo, Grupo de Biotecnología Ambiental e Industrial, Departamento de Microbiología.

Marcela María Mercado Grupo de Enfermedades Infecciosas, Departamento de Microbiología, Pontificia Universidad Javeriana, Bogotá, Colombia

Luis A. Barrera Instituto de Errores Innatos del Metabolismo

Influence of a-Factor over the expression of hrIDS in Pichia pastoris: Literature review and computational analysis. In searching of alternatives to get the efficient secretions of the recombinant enzyme Iduronate Sulfatase (IDSh) in Pichia pastoris, we made a systematic review of the literature so that we could compile information to relate the expression level of human heterologous proteins, with secretion signal, and the characteristics of the molecules. 349 publications were found of which only 7 (2%) reported the expression of proteins that met find inclusion criteria. With the information obtained in these articles, we made a hypothesis test using the data compiled as samples and a qualitative analysis of the information. It was found that replacement of native secretion signal by a-Factor as leader peptide increases the level of expression of human heterologous proteins in P. pastoris (p=0.053). Moreover, the elimination of native signal peptide in the protein cDNA is 125 indispensable for the function of a-Factor in the secretion of recombinant proteins and for to increase the expression level. In the construct, GS115/pPIC9-IDS were simultaneously founded two sequences in the signal peptide, the native and the a-Factor. However, the activity found ~30 mmol/h mg of protein raises the question of a possible conflict between the two recognition sites. This may be the cause given the similarity in the hidrophobicity of those two sites.

systematic review, signal peptide, protein expression, Pichia pastoris

Neufeld EF, Muenzer J. The Mucopolysaccharidoses, in The Metabolic and Molecular Bases of Inherited Disease, CH Scriver, AL Beaudet, WS Sly, D Valle, Editors. 2001, MaGraw- Hill: New York. p. 3421-52.

Albano LMJ, Sugayama SSMM, Bertola DR, Andrade CEF, Utagawa CY, Puppi F, Nader HB, Toma L, Coelho J, Leistner S, Burin M, Giugliani R, Kim CA. Clinical and Laboratorial Study of 19 Cases of Mucopolysaccharidoses. Rev Hosp Clín Fac Med Sao Paulo 2000; 55 (6): 213-18.

Kettlesa DI, Sheppardb M, Liebmannc RD, Davidsona C. Left Ventricular Aneurysm, Aortic Valve Disease and Coronary Narrowing in a Patient with Hunter.s Syndrome. Card Pathol 2002; 11: 94-96.

Yoskovitch A, Tewfik TL, Brouillette RT, Schloss MD, Der Kaloustian VM. Acute Airway Obstruction in Hunter Syndrome. Internat J Ped Otorhinolaryngol 1998; 44: 273-78.

Menéndez C, Zaldívar C, González M. Errores Innatos del Metabolismo. Enfermedades Lisosomales. Rev Cub Pediat 2002; 74 (1): 68-76.

Desnick RJ. Enzyme Replacement and Enhancement Therapies for Lysosomal Diseases. J Inher Metab Dis 2004; 27: 385-410.

Sáenz H, Barrera LA. La Terapia de Reemplazo Enzimático en el Tratamiento de Enfermedades Genéticas. Univ Scient 2003; 8 (2): 31-42.

Landázuri P. Clonación Del cDNA de la Iduronato 2-Sulfato Sulfatasa Humana. Expresión de la Enzima en Escherichia coli y Pichia pastoris. Instituto de Errores Innatos del Metabolismo. Tesis Doctoral. 2002. Pontificia Universidad Javeriana. Bogotá, D.C. 115 p.

Chen Y, Jin M, Egborge T, Coppola G, Andre J, Calhoun DH. Expression and Characterization of Glycosylated and Catalytically Active Recombinant Human a-Galactosidase A Produced in Pichia pastoris. Prot Exp Purif 2000; 20: 472.84.

Files DA, Ogawa M, Scaman CH, Baldwin SA. Pichia pastoris Fermentation Process for Producing High-Levels of Recombinant Human Cystatin-C. Enz Microbiol Technol 2001; 26: 335 40.

Sinclair G, Choy F. Synonymous Codon Usage Bias and the Expression of Human Glucocerebrosidase in the Methylotrophic Yeast, Pichia pastoris. Prot Exp Purif 2002; 26: 96-105.

Xie J, Zhoub Q, Dub P, Ganb R, Ye Q. Use of Different Carbon Sources in Cultivation of Recombinant Pichia pastoris for Angiostatin Production. Enz Microb Technol 2005; 36: 210-16.

Poutou RA, Córdoba H, Quevedo BE, Landázuri P, Echeverri OY, Sáenz H, Vanegas A, Acero J, Gónzalez A, Herrera J, Algesira N, Caicedo L, Barrera LA. Expresión de Iduronato 2 sulfato Sulfatasa Humana Recombinante (IDShr) en Pichia pastoris. Univ Scient 2005; 10 (1): 73 94.

Cereghino GP, Cereghino J, Ilgen C, Cregg J. Production of Recombinant Proteins in Fermenter Cultures of the Yeast Pichia pastoris. Curr Opin Biotechnol 2002; 13: 329-32.

Cereghino JL, Cregg JM. Heterologous Protein Expression in the Methylotrophic Yeast Pichia pastoris. FEMS Microbiol Rev 2000; 24: 45-66.

Fischer R, Drossard J, Emans N, Commandeur U, Hellwig S. Towards Molecular Farming in the Future: Pichia pastoris- Based Production of Single-Chain Antibody Fragments. Biotechnol App Biochem 1999; 30: 117-20.

Romanos M. Advances in The Use of Pichia pasrtoris for High- Level Gene Expression. Curr Opin Biotechnol 1995; 6: 527-33.

Córdoba H, N. A, Poutou RA, Barrera LA. Pichia pastoris una Alternativa para la Producción de Glicoproteínas Humanas de Uso Terapéutico. Estrategias de Fermentación. Rev Col Biotecnol 2003; 5 (2): 73-84.

Hollenberg CP, Gellissen G. Production of Recombinant Proteins by Methylotrophic Yeast. Curr Opin Biotechnol 1997; 8: 554-60.

Caplan S, Green R, Rocco J, Kurjanlt J. Glycosylation and Structure of the Yeast MF Factor Precursor Is Important for Efficient Transport Through the Secretory Pathway. J Bacteriol 1991; 173 (2): 627-35.

Kurjan J, Herskowitz I. Structure of a Yeast Pheromone Gene (MF alpha): a Putative alpha factor Precursor Contains Four Tandem Copies of Mature alpha-factor. Cell 1982; 30: 933-43.

Egger M, Davey G, Altman D. Systematic Reviews in Health Care: Meta-analysis in Context. 2003; London: BMJ Books. 3-13, 23-29, 211-223.

Glasziou P, Irwig L, Bain C, Colditz G. Systematic Reviews in Health Care: A Practical Guide. 1 ed. 2001; Cambridge: Cambridge University Press. 4-14, 27- 31, 45-46.

. Rosenberg W, Donald A, Radcliffe J. Evidence Based Medici91 ne: An Approach to Clinical Problem-Solving, in Evidence Based Health Care Workbook: Understanding Research: for Individual Learning, A Donald, Editor. 1999, BMJ Publishing Group: London. p. 17-19, 37-38.

Daniel WW. Bioestadística. Base para el Análisis de las Ciencias de la Salud. 3a ed. 2000; Mexico: Ed. Limusa S.A. 245- 252,269-276.

Altschul SF, Madden TL, Schäffer AA, Zhang J, Zhang Z, Miller WJ, Lipman D. Gapped BLAST And PSI-BLAST: A New Generation of Protein Database Search Programs. Nuc Aci Res 1997; 25: 3389-3402.

Wilson PJ, Meaney CA, Hopwood JJ, Morris CP. Sequence of the Human Iduronate 2 Sulfatase (IDS) Gene. Genom 1993; 17: 773-75.

Koganesawa N, Aizawa T, Masaki K, Matsuura A, Nimori T, Bando H, Kawano K, Nitta K. Construction of an Expression System of Insect Lysozyme Lacking Thermal Stability: The Effect of Selection of Signal Sequence on Level of Expression in the Pichia pastoris Expression System. Prot Eng 2001; 14 (9): 705-10.

Oka C, Tanaka M, Muraki M, Harata K, Suzuki K, Jigami Y. Human Lysozyme Secretion Increased by Alpha-factor Prosequence in Pichia pastoris. Biosci Biotechnol Biochem 1999; 63 (11): 1977-83.

Reverter D, Ventura S, Villegas V, Vendrell JX, Avilés FX. Overexpression of Human Procarboxypeptidase A2 in Pichia pastoris and Detailed Characterization of Its Activation Pathway. The J Biol Chem 1998; 273 (6): 3535.41.

Roy N, Padmanabhan S, Smith M, Shi L, Navre M, Das G. Expression of Human Gelatinase B in Pichia pastoris. Prot Exp Purif 1999; 16: 324-30.

Sen Gupta C, Dighe R. Hyperexpression of Biologically Active Human Chorionic Gonadotropin Using the Methylotropic Yeast, Pichia pastoris. J Mol Endocrinol 1999; 22: 273-83.

Vuorela A, Myllyharju J, Nissi R, Pihlajaniemi T, Kivirikko KI. Assembly of Human prolyl 4 hydroxylase and Type III Collagen in the Yeast Pichia pastoris: Formation of a Stable Enzyme Tetramer Requires Coexpression with Collagen and Sssembly of a Stable Collagen Requires Coexpression with prolyl 4-hydroxylase. The EMBO J 1997; 16 (22): 6702.12.

Wendeler M, Hoernschemeyer J, John M, Werth N, Schoeniger M, Lemm T, Hartmann R, Kessler H, Sandhoff K. Expression of the GM2-Activator Protein in the Methylotrophic Yeast Pichia pastoris, Purification, Isotopic Labeling, and Biophysical Characterization. Prot Exp Puri f2004; 34: 147-57.

Kjeldsen T, Frost Pettersson A, Hach M. The Role of Leaders in Intracellular Transport and Secretion of the Insulin Precursor in the Yeast Saccharomyces cerevisiae. J Biotechnol 1999; 75: 195-208.

Murasugi A, Tohma-Aiba Y. Comparison of Three Signals for Secretory Expresión of Recombinant Human Midkine in Pichia pastoris. Biosci Biotechnol Biochem 2001; 65 (10): 2291 93.

Murasugi A, Tohma-Aiba Y. Production of Native Recombinant Human Midkine in the Yeast, Pichia pastoris. Prot Exp Purif 2003; 27: 244-52.

Kjeldsen T, Andersen A, Hach M, Diers I, Nikolajsen J, Markussen J. a-Factor Pro-Peptide N-linked Oligosaccharides Facilitate Secretion of the Insulin Precursor in Saccharomyces cerevisiae. Biotechnol App Biochem 1998; 27: 109-15.

Kjeldsen T, Pettersson AF, Hach M. Secretory Expression and Characterization of Insulin in Pichia pastoris. Biotechnol App Biochem 1999; 29: 79-86.

Liu SH, Chou W, Sheu C, Chang M. Improved Secretory Production of Glucoamylase in Pichia pastoris by Combination of Genetic Manipulations. Biochem Biophys Res Commun 2005; 326: 817-24.

Sreekrishna K, Brankamp R, Kropp K, Blankenship D, Tsay J-T, Smith P, Wierschke J, Subramaniam A, Birkenberger L. Strategies for optimal Synthesis and Secretion of Heterologous Proteins in the Methylotrophic Yeast Pichia pastoris. Gene 1997; 190: 55-62.

Cappai R, Mok SS, Galatis D, Tucker D, Henry A, Beyreuther K, Small D, Masters C. Recombinant Human Amyloid Precursor- Like Protein 2 (APLP2) Expressed in the Yeast Pichia pastoris Can Stimulate Neurite Outgrowth. FEBS Let 1999; 442: 95-98.

Pham C, Thomas D, Mercer J, Ley T. Production of Fully Active Recombinant Murine Granzyme B in Yeast. The J Biolo Chem 1998; 273 (16): 1629-33.

Goda S, Takano K, Yamagata Y, Katakura Y, Yutani K. Effect of NTerminal Residues on the Stability and Folding of Human Lysozyme Expressed in Pichia pastoris. Prot Eng 2000; 13 (4): 299 307.

Malmgren H, Calberg BM, Peterson U, Bondeson ML. Identificatión of an Alternative Transcript from the Human Iduronate 2- Sulfatase. Genomics 1995; 29: 291-93.

Invitrogen. Pichia Expression Kit. Protein Expression. A Manual of Methods for Expression of Recombinant Proteins in P. pastoris.Cat. No. K1710-01. 1996; California: Invitrogen.

Parodi A. Reglucosylation of Glycoproteins and Quality Control of Glycoprotein Folding in the Endoplasmic Reticulum of Yeast Cells. Biochim Biophys Acta 1999; 1426: 287-95.

Kowalski J, Parekh R, Mao J, Wittrup K. Protein Folding Stability Can Determine the Efficiency of Escape from Endoplasmic Reticulum Quality Control. The J Biol Chem 1998; 273 (31): 19453-58.

Dalbey RE, Lively MO, Bron S, Van Diijl JM. The Chemistry and Enzymology of the Type I Signal Peptidases. Prot Sci 1997; 6: 1129-38.

Peña O, Sosa A, Echeverri O, Sáenz H, Barrera LA. Producción de Anticuerpos Policlonales IgG Contra la Proteína Iduronato-2- sulfato Sulfatasa y Desarrollo de un Sistema de Detección para IDS Humana Recombinante. Bioméd 2005; 25: 181-88.

Download Citation

Published

How to Cite

Influence of a-Factor Over the Expression of Hrids in: Literature Review and Computational Analysis.

Declaración de privacidad.

Keywords