L-Asparaginase from Erwinia carotovora: insights about its stability and activity.
Biophysical behavior
In solution characterization
L-asparaginase
Journal
Molecular biology reports
ISSN: 1573-4978
Titre abrégé: Mol Biol Rep
Pays: Netherlands
ID NLM: 0403234
Informations de publication
Date de publication:
Feb 2019
Feb 2019
Historique:
received:
09
08
2018
accepted:
30
10
2018
pubmed:
18
11
2018
medline:
11
7
2019
entrez:
18
11
2018
Statut:
ppublish
Résumé
Enzymatic prospection indicated that L-asparaginase from Erwinia carotovora (ECAR-LANS) posses low glutaminase activity and much effort has been made to produce therapeutic ECAR-LANS. However, its low stability precludes its use in therapy. Herein, biochemical and biophysical assays provided data highlighting the influence of solubilization and storage into ECAR-LANS structure, stability, and activity. Moreover, innovations in recombinant expression and purification guaranteed the purification of functional tetramers. According to solubilization condition, the L-asparaginase activity and temperature of melting ranged up to 25-32%, respectively. CD spectra indicate the tendency of ECAR-LANS to instability and the influence of β-structures in activity. These results provide relevant information to guide formulations with prolonged action in the bloodstream.
Identifiants
pubmed: 30446961
doi: 10.1007/s11033-018-4459-2
pii: 10.1007/s11033-018-4459-2
doi:
Substances chimiques
Asparaginase
EC 3.5.1.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1313-1316Références
Pieters R, Carroll WL (2008) Biology and treatment of acute lymphoblastic leukemia. Pediatr Clin North Am 55:1–20 ix
doi: 10.1016/j.pcl.2007.11.002
pubmed: 18242313
Silverman LB, Gelber RD, Dalton VK, Asselin BL, Barr RD, Clavell LA, Hurwitz CA, Moghrabi A, Samson Y, Schorin MA, Arkin S, Declerck L, Cohen HJ, Sallan SE (2001) Improved outcome for children with acute lymphoblastic leukemia: results of Dana-Farber Consortium Protocol 91-01. Blood 97:1211–1218
doi: 10.1182/blood.V97.5.1211
pubmed: 11222362
Amylon MD, Shuster J, Pullen J, Berard C, Link MP, Wharam M, Katz J, Yu A, Laver J, Ravindranath Y, Kurtzberg J, Desai S, Camitta B, Murphy SB (1999) Intensive high-dose asparaginase consolidation improves survival for pediatric patients with T cell acute lymphoblastic leukemia and advanced stage lymphoblastic lymphoma: a Pediatric Oncology Group study. Leukemia 13:335–342
doi: 10.1038/sj.leu.2401310
pubmed: 10086723
Abshire TC, Pollock BH, Billett AL, Bradley P, Buchanan GR (2000) Weekly polyethylene glycol conjugated L-asparaginase compared with biweekly dosing produces superior induction remission rates in childhood relapsed acute lymphoblastic leukemia: a Pediatric Oncology Group Study. Blood 96:1709–1715
pubmed: 10961868
Asselin BL (1999) The three asparaginases. Comparative pharmacology and optimal use in childhood leukemia. Adv Exp Med Biol 457:621–629
doi: 10.1007/978-1-4615-4811-9_69
pubmed: 10500842
Avramis VI, Tiwari PN (2006) Asparaginase (native ASNase or pegylated ASNase) in the treatment of acute lymphoblastic leukemia. Int J Nanomed 1:241–254
Pinkel D (1987) Curing children of leukemia. Cancer 59:1683–1691
doi: 10.1002/1097-0142(19870515)59:10<1683::AID-CNCR2820591002>3.0.CO;2-G
pubmed: 3470109
Cheung NK, Chau IY, Coccia PF (1986) Antibody response to Escherichia coli L-asparaginase. Prognostic significance and clinical utility of antibody measurement. Am J Pediatr Hematol Oncol 8:99–104
pubmed: 3526939
Moghrabi A, Levy DE, Asselin B, Barr R, Clavell L, Hurwitz C, Samson Y, Schorin M, Dalton VK, Lipshultz SE, Neuberg DS, Gelber RD, Cohen HJ, Sallan SE, Silverman LB (2007) Results of the Dana-Farber Cancer Institute ALL Consortium Protocol 95-01 for children with acute lymphoblastic leukemia. Blood 109:896–904
doi: 10.1182/blood-2006-06-027714
pubmed: 17003366
pmcid: 1785142
Krasotkina J, Borisova AA, Gervaziev YV, Sokolov NN (2004) One-step purification and kinetic properties of the recombinant L-asparaginase from Erwinia carotovora. Biotechnol Appl Biochem 39:215–221
doi: 10.1042/BA20030138
pubmed: 15032742
Eden OB, Shaw MP, Lilleyman JS, Richards S (1990) Non-randomised study comparing toxicity of Escherichia coli and Erwinia asparaginase in children with leukaemia. Med Pediatr Oncol 18:497–502
doi: 10.1002/mpo.2950180612
pubmed: 2233523
Yuen SH, Pollard AG (1952) The determination of nitrogen in agricultural materials by the nessler reagent. I.—preparation of the reagent. J Sci Food Agr 3:441–447
doi: 10.1002/jsfa.2740031002
Konarev PV, Volkov VV, Sokolova AV, Koch MHJ, Svergun DI (2003) PRIMUS: a Windows PC-based system for small-angle scattering data analysis. J Appl Crystallogr 36:1277–1282
doi: 10.1107/S0021889803012779
Jennings MP, Beacham IR (1990) Analysis of the Escherichia coli gene encoding L-asparaginase II, ansB, and its regulation by cyclic AMP receptor and FNR proteins. J Bacteriol 172:1491–1498
doi: 10.1128/jb.172.3.1491-1498.1990
pubmed: 2407723
pmcid: 208625
Kotzia GA, Labrou NE (2005) Cloning, expression and characterisation of Erwinia carotovora L-asparaginase. J Biotechnol 119:309–323
doi: 10.1016/j.jbiotec.2005.04.016
pubmed: 15951039
Pourhossein M, Korbekandi H (2014) Cloning, expression, purification and characterisation of Erwinia carotovora L-asparaginase in Escherichia coli. Adv Biomed Res 3:82
doi: 10.4103/2277-9175.127995
pubmed: 24761390
pmcid: 3988593
Cheng C-M, Tzou S-C, Zhuang Y-H, Huang C-C, Kao C-H, Liao K-W, Cheng T-C, Chuang C-H, Hsieh Y-C, Tai M-H, Cheng T-L (2014) Functional production of a soluble and secreted single-chain antibody by a bacterial secretion system. PLoS ONE 9:e97367
doi: 10.1371/journal.pone.0097367
pubmed: 24824752
pmcid: 4019604
Kaufmann M, Lindner P, Honegger A, Blank K, Tschopp M, Capitani G, Plückthun A, Grütter MG (2002) Crystal structure of the anti-His tag antibody 3D5 single-chain fragment complexed to its antigen. J Mol Biol 318:135–147
doi: 10.1016/S0022-2836(02)00038-4
pubmed: 12054774
Schlegel S, Rujas E, Ytterberg AJ, Zubarev RA, Luirink J, de Gier J-W (2013) Optimizing heterologous protein production in the periplasm of E. coli by regulating gene expression levels. Microb Cell Fact 12:24
doi: 10.1186/1475-2859-12-24
pubmed: 23497240
pmcid: 3605120
Zhou Y, Zhou Y, Li J, Chen J, Yao Y, Yu L, Peng D, Wang M, Su D, He Y, Gou L (2015) Efficient expression, purification and characterization of native human cystatin C in Escherichia coli periplasm. Protein Expr Purif 111:18–22
doi: 10.1016/j.pep.2015.03.006
pubmed: 25795130
Kozak M, Jurga S (2002) A comparison between the crystal and solution structures of Escherichia coli asparaginase II. Acta Biochim Pol 49:509–513
pubmed: 12362993
Wikman LEK, Krasotkina J, Kuchumova A, Sokolov NN, Papageorgiou AC (2005) Crystallization and preliminary crystallographic analysis of L-asparaginase from Erwinia carotovora. Acta Crystallogr Sect F Struct Biol Cryst Commun 61:407–409
doi: 10.1107/S1744309105008249
pubmed: 16511054
pmcid: 1952439