Molecular characterization of Capra hircus lysosomal alpha - mannosidase and potential mutant site for the therapy of locoweed poisoning

• Autorzy: Xiangya K. , Jiangye Z. , Ying W. , Jianfei L. , Qinfan L.
• Języki publikacji: EN

Abstrakty

EN

Lysosomal α-Mannosidase (LAM) belongs to the glycoside hydrolyzing enzymes family 38 and is involved in the biosynthesis and turnover of N-linked glycoproteins process. Locoweeds, which contain swainsonine (SW) that inhibits LAM, are the main poisoning plants in many regions of the world, and thereby resulting in animal poisoning or even death. Based on regions of protein sequence conservation between LAM from Bos taurus and Homo sapiens, we cloned cDNA encoding Capra hircus LAM (chLAM). Expression of cDNA in Pichia pastoris resulted in the secretion of aLAM activity into the culture medium. The recombinant chLAM was activated 1.6 and 1.2-fold with Zn2+ and Ca2+, respectively. By homology modeling, molecular docking and mutant analysis, we obtained the probable binding modes of SW at the allosteric sites of chLAM, and the potential mutant sites for the resistance to SW. Prediction of SW sensitivity to A28 W/G, D58 Y/G mutant chLAM is lower than wild type chLAM. The obtained results lead to a better understanding of not only interactions between substrate/SW and chLAM, but also of a potential strategy for a novel therapy for locoweed poisoning.

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2014
• Tom: 61
• Numer: 1
• Opis fizyczny: p.77-84,fig.,ref.

Twórcy

autor

Xiangya K.

• College of Veterinary Medicine, Northwest A&F University, Yangling 712100, Shaanxi, China

autor

Jiangye Z.

• College of Veterinary Medicine, Northwest A&F University, Yangling 712100, Shaanxi, China

autor

Ying W.

• College of Veterinary Medicine, Northwest A&F University, Yangling 712100, Shaanxi, China

autor

Jianfei L.

• College of Veterinary Medicine, Northwest A&F University, Yangling 712100, Shaanxi, China

autor

Qinfan L.

• College of Veterinary Medicine, Northwest A&F University, Yangling 712100, Shaanxi, China

Bibliografia

• Arnold K, Bordoli L, Kopp J, Schwede T (2006) The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22: 195-201. 
• Athanasopoulos VI, Niranjan K, Rastall RA (2005) The production, purification and characterisation of two novel mannosidases from Aspergillus phoenicis. Carbohyd Res 340: 609-617. 
• Auclair D, Hopwood JJ, Brooks DA, Lemontt JF, Crawley AC (2003) Replacement therapy in Mucopolysaccharidosis type VI: advantages of early onset of therapy, Mol Genet Metab 78: 163-174. 
• Bach G, Kohn G, Lasch EE, El Massri M, Ornoy A, Sekeles E, Legum C, Cohen MM (1978) A new variant of mannosidosis with increased residual enzymatic activity and mild clinical manifestation. Pediatr Res 12: 1010-1015. 
• Balogh KK, Dimande AP, van der Lugt JJ, Molyneux RJ, Naude TW, Welman WG (1999) A lysosomal storage disease induced by Ipomoea carnea in goats in Mozambique. J Vet Diagn Invest 11: 266-273. 
• Barbosa RC, Riet CF, Medeiros RM, Lima EF, Barros SS, Gimeno EJ, Molyneux RJ, Gardner DR (2006) Intoxication by Ipomoea sericophylla and Ipomoea riedelii in goats in the state of Paraiba, Northeastern Brazil. Toxicon 47: 371-379. 
• Bauer AM, Bryant SH (2004) CD-Search: protein domain annotations on the fly. Nucleic Acids Res 32: W327-W331. 
• Beccari T, Appolloni MG, Costanzi E, Stinchi S, Stirling JL, Fazia MA, Servillo G, Viola MP, Orlacchio A (1997) Lysosomal alpha-mannosidases of mouse tissues: characteristics of the isoenzymes, and cloning and expression of a full-length cDNA. Biochem J 327: 45-49. 
• Berg T, Tollersrud OK, Walkley SU, Siegel D, Nilssen O (1997) Purification of feline lysosomal alpha-mannosidase, determination of its cDNA sequence and identification of a mutation causing α-mannosidosis in Persian cats. Biochem J 328: 863-870. 
• Blom H, Reyes F, Carlsson J (2008) Purification and characterization of an α-mannosidase from the tropical fruit babaco. J Agri Food Chem 56: 10872-10887. 
• Bourne Y, Henrissat B (2001) Glycoside hydrolases and glycosyltransferases: families and functional modules. Curr Opin Struct Biol 11: 593-600. 
• Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B (2009) The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res 37: D233-D238. 
• Costanzi E, Balducci C, Cacan R, Duvet S, Orlacchio A, Beccari T (2006) Cloning and expression of mouse cytosolic α-mannosidase (Man2c1). BBA-Gen Subjects 1760: 1580-1586. 
• Crawley AC, King B, Berg T, Meikle PJ, Hopwood JJ (2006) Enzyme replacement therapy in α-mannosidosis guinea-pigs. Mol Genet Metab 89: 48-57. 
• Daniel PF, Winchester B, Warren CD (1994) Mammalian α-mannosidase multiple forms but a common purpose. Glycobiology 4: 551-566. 
• Dantas AF, Riet-Correa FR, Gardner DR, Medeiros RM, Barros SS, Anjos BL, Lucena RB (2007) Swainsonine-induced lysosomal storage disease in goats caused by the ingestion of Turbina cordata in Northeastern Brazil. Toxicon 49: 111-116. 
• De Preter K, Speleman F, Combaret V, Lunec J, Laureys G, Eussen BH, Francotte N, Board J, Pearson AD, De Paepe A, Van Roy N, Vandesompele J (2002) Quantification of MYCN, DDX1, and NAG gene copy number in neuroblastoma using a real-time quantitative PCR assay. Mod Pathol 15: 159-166. 
• Ellinwood NM, Vite CH, Haskins ME (2004) Gene therapy for lysosomal storage diseases: the lessons and promise of animal models. J Gene Med 6: 481-506. 
• Gabrielli O, Clarke LA, Bruni S, Coppa GV (2010) Enzyme-replacement therapy in a 5-month-old boy with attenuated presymptomatic MPS I: 5-year follow-up. Pediatrics 125: e183-e187. 
• Gasteiger E, Gattiker A, Hoogland C, Ivanyi I, Appel RD, Bairoch A (2003) ExPasy: the proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res 31: 3784-3788. 
• Ginalski K (2006) Comparative modeling for protein structure prediction. Curr Opin Struct Biol 16: 172-177. 
• Haraguchi M, Gorniak SL, Ikeda K, Minami H, Kato A, Watson AA, Nash R, Molyneux RJ, Asano N (2003) Alkaloidal components in the poisonous plant, Ipomoea carnea (Convolvulaceae). J Agric Food Chem 51: 4995-5000. 
• Henrissat B, Bairoch A (1993) New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 293: 781-788. 
• Heikinheimo P, Helland R, Leiros HK, Leiros I, Karlsen S, Evjen G, Ravelli R, Schoehn G, Ruigrok R, Tollersrud OK, McSweeney S, Hough E (2003) The structure of bovine lysosomal alpha-mannosidase suggests a novel mechanism for low-pH activation. J Mol Biol 327: 631-644. 
• Hossain MA, Nakano R, Nakamura K, Hossain MT, Kimura Y (2010) Molecular characterization of plant acidic α-mannosidase, a member of glycosylhydrolase family 38, involved in the turnover of N-glycans during tomato fruit ripening. J Biochem 148: 603-616. 
• Jiang X, Kumar K, Hu X, Wallqvist A, Reifman J (2008) DOVIS 2.0: an efficient and easy to use parallel virtual screeningtool based on AutoDock 4.0. Chem Cent J 2: 1-7. 
• Khan FA, Basu D (1982) Isolation and characterization of lysosomal alpha-mannosidase of placental tissue. J Biosci 4: 133-138.
• Kiefer F, Arnold K, Kunzli M, Bordoli L, Schwede T (2009) The SWISS-MODEL Repository and associated resources. Nucleic Acids Res 37: D387-D392. 
• Kishimoto T, Hori H, Takano D, Nakano Y, Watanabe M, Mitsui T (2001) Rice α-mannosidase digesting the high mannose glycopeptides of glutelin. Physiol Plant 112: 15-24. 
• Li JK (2003) The present situation and prospect of studies on locoweed in China. Scientia Agricultura Sinica 36: 1091-1099.
• Liao YF, Lal A, Moremen KW (1996) Cloning, Expression, purification, and characterization of the human broad specificity lysosomal acid α-mannosidase. The J Biol Chem 271: 28348-28358. 
• Marshall J, McEachern KA, Chuang WL, Hutto E, Siegel CS, Shayman JA, Grabowski GA, Scheule RK, Copeland DP, Cheng SH (2010) Improved management of lysosomal glucosylceramide levels in a mouse model of type I Gaucher disease using enzyme and substrate reduction therapy. J Inherit Metab Dis 33: 281-289. 
• Merkle RK, Zhang Y, Rues PJ, Liao YF, Moremen KW (1997) Cloning, expression, purification, and characterization of the murine lysosomal acid α-mannosidase. BBA-Gen Subjects 1336: 132-146. 
• Michalski JC, Klein A (1999) Glycoprotein lysosomal storage disorders: alpha- and beta-mannosidosis, fucosidosis and K-N-acetylgalactosaminidase deficiency. Biochim Biophys Acta 1455: 69-84. 
• Novikoff PM, Touster O, Novikoff AB, Tulsiani DP (1985) Effects of swainsonine on rat liver and kidney: Biochemical and morphological studies. J Cell Biol 101: 339-349. 
• Petersen TN, Brunak S, Von HG, Nielsen H (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 8: 785-786. 
• Rost B, Yachdav G, Liu J (2004) The PredictProtein server. Nucleic Acids Res 32: W321-W326. 
• Snaith SM, Levvy GA (1968) α-Mannosidase as a Zinc-dependent Enzyme. Nature 218: 91-92. 
• Snaith SM (1975) Characterization of jack-bean α-D-mannosidase as zinc metalloenzyme. Biochem J 147: 83-90. 
• Snaith SM (1977) Multdple α-mannosidase activities in mammalian tissues as shown by metal-ion activation. Biochem J 163: 557-564. 
• Thompson JD, Gibson TJ, Plewniak F (1997) The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25: 4876-4882. 
• Tollersrud OK, Berg T, Healy P, Evjen G, Ramachandran U, Nilssen Ø (1997) Purification of bovine lysosomal α-mannosidase, characterization of its gene and determination of two mutations that cause α-mannosidosis. Eur J Biochem 246: 410-419. 
• Uno Y, Hashidume S, Kurita O, Fujiwara T, Nomura K (2010) Dioscorea opposita Thunb. α-mannosidase belongs to the glycosyl hydrolase family 38. Acta Physiol Plant 32: 713-718.
• van Kampen KR, James LF (1969) Pathology of locoweed poisoning in sheep. Pathol Vet 6: 413-423.  
• Wagner JE, Yamamoto AI, McGrath JA, Hordinsky M, Keene DR, Woodley DT, Chen M, Riddle MJ, Osborn MJ, Lund T, Dolan M, Blazar BR, Tolar J (2010) Bone Marrow Transplantation for Recessive Dystrophic Epidermolysis Bullosa. New Engl J Med 363: 629-639.