Establishing the yeast kluyveromyces lactis as an expression host for production of the saposin-like domain of the aspartic protease cirsin

Applied and Environmental Microbiology

Volumn 80, Issue 1, 2014, Pages 86-96

  Curto, Pedro ^a,b   Lufrano, Daniela ^c   Pinto, Cátia ^b   Custódio, Valéria ^b   Gomes, Ana Catarina ^b   Trejo, Sebastián A ^c   Bakás, Laura ^d   Vairo Cavalli, Sandra ^d   Faro, Carlos ^a,b   Simõesa, Isaura ^a,b  

^a UNIVERSITY OF COIMBRA   (Portugal)

^b Biocant Biotechnology Innovation Center   (Portugal)

^c UNIVERSITAT AUTÒNOMA DE BARCELONA   (Spain)

^d FACULTAD DE CIENCIAS EXACTAS   (Argentina)

Author keywords

[No Author keywords available]

Indexed keywords

ANTI-FUNGAL ACTIVITY; ASPARTIC PROTEASE; BIOTECHNOLOGICAL POTENTIALS; DEFENSIVE WEAPONS; KLUYVEROMYCES LACTIS; PHYTOPATHOGENIC FUNGI; PLANT-SPECIFIC INSERTS; PURIFICATION PROTOCOL;

PRODUCTION PLATFORMS; PROTEINS;

YEAST;

BIOTRANSFORMATION; ENZYME ACTIVITY; FUNGUS; GENE EXPRESSION; HOST-PATHOGEN INTERACTION; MEMBRANE; PROTEIN; YEAST;

ANTIFUNGAL AGENT; ASPARTIC PROTEINASE; RECOMBINANT PROTEIN; SPHINGOLIPID ACTIVATOR PROTEIN;

ARTICLE; GENE EXPRESSION; GENETIC TRANSFORMATION; GENETICS; ISOLATION AND PURIFICATION; KLUYVEROMYCES; METABOLISM; MICROBIAL SENSITIVITY TEST;

ANTIFUNGAL AGENTS; ASPARTIC ACID PROTEASES; GENE EXPRESSION; KLUYVEROMYCES; MICROBIAL SENSITIVITY TESTS; RECOMBINANT PROTEINS; SAPOSINS; TRANSFORMATION, GENETIC;

EID: 84891059538     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.03151-13     Document Type: Article

References (33)

1. Guruprasad K, Tormakangas K, Kervinen J, Blundell TL. 1994. Comparative modelling of barley-grain aspartic proteinase: a structural rationale for observed hydrolytic specificity. FEBS Lett. 352:131-136. http://dx.doi.org/10.1016/0014-5793(94)00935-X.
2. Kervinen J, Tobin GJ, Costa J, Waugh DS, Wlodawer A, Zdanov A. 1999. Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting. EMBO J. 18:3947-3955. http://dx.doi.org/10.1093/emboj/18.14.3947.
3. Simoes I, Faro C. 2004. Structure and function of plant aspartic proteinases. Eur. J. Biochem. 271:2067-2075. http://dx.doi.org/10.1111/j.1432-1033.2004.04136.x.
4. Bruhn H. 2005. A short guided tour through functional and structural features of saposin-like proteins. Biochem. J. 389:249-257. http://dx.doi.org/10.1042/BJ20050051.
5. Munford RS, Sheppard PO, O'Hara PJ. 1995. Saposin-like proteins (SAPLIP) carry out diverse functions on a common backbone structure. J. Lipid Res. 36:1653-1663.
6. Ryan MA, Akinbi HT, Serrano AG, Perez-Gil J, Wu H, McCormack FX, Weaver TE. 2006. Antimicrobial activity of native and synthetic surfactant protein B peptides. J. Immunol. 176:416-425.
7. Duarte P, Pissarra J, Moore I. 2008. Processing and trafficking of a single isoform of the aspartic proteinase cardosin A on the vacuolar pathway. Planta 227:1255-1268. http://dx.doi.org/10.1007/s00425-008-0697-1.
8. Egas C, Lavoura N, Resende R, Brito RM, Pires E, de Lima MC, Faro C. 2000. The saposin-like domain of the plant aspartic proteinase precursor is a potent inducer of vesicle leakage. J. Biol. Chem. 275:38190-38196. http://dx.doi.org/10.1074/jbc.M006093200.
9. Munoz FF, Mendieta JR, Pagano MR, Paggi RA, Daleo GR, Guevara MG. 2010. The swaposin-like domain of potato aspartic protease (StAsp-PSI) exerts antimicrobial activity on plant and human pathogens. Peptides 31:777-785. http://dx.doi.org/10.1016/j.peptides.2010.02.001.
10. Bryksa BC, Bhaumik P, Magracheva E, De Moura DC, Kurylowicz M, Zdanov A, Dutcher JR, Wlodawer A, Yada RY. 2011. Structure and mechanism of the saposin-like domain of a plant aspartic protease. J. Biol. Chem. 286:28265-28275. http://dx.doi.org/10.1074/jbc.M111.252619.
11. Parisien A, Allain B, Zhang J, Mandeville R, Lan CQ. 2008. Novel alternatives to antibiotics: bacteriophages, bacterial cell wall hydrolases, and antimicrobial peptides. J. Appl. Microbiol. 104:1-13. http://dx.doi.org/10.1111/j.1365-2672.2007.03498.x.
12. Giuliani A, Pirri G, Nicoletto S. 2007. Antimicrobial peptides: an overview of a promising class of therapeutics. Cent. Eur. J. Biol. 2:1-33. http://dx.doi.org/10.2478/s11535-007-0010-5.
13. Yeaman MR, Yount NY. 2003. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 55:27-55. http://dx.doi.org/10.1124/pr.55.1.2.
14. Lufrano D, Faro R, Castanheira P, Parisi G, Verissimo P, Vairo-Cavalli S, Simoes I, Faro C. 2012. Molecular cloning and characterization of procirsin, an active aspartic protease precursor from Cirsium vulgare (Asteraceae). Phytochemistry 81:7-18. http://dx.doi.org/10.1016/j.phytochem.2012.05.028.
15. Haught C, Davis GD, Subramanian R, Jackson KW, Harrison RG. 1998. Recombinant production and purification of novel antisense antimicrobial peptide in Escherichia coli. Biotechnol. Bioeng. 57:55-61. http://dx.doi.org/10.1002/(SICI)1097-0290(19980105)57:1<55::AID-BIT7>3.0.CO;2-U.
16. Parachin NS, Mulder KC, Viana AA, Dias SC, Franco OL. 2012. Expression systems for heterologous production of antimicrobial peptides. Peptides 38:446-456. http://dx.doi.org/10.1016/j.peptides.2012.09.020.
17. Caplan S, Green R, Rocco J, Kurjan J. 1991. Glycosylation and structure of the yeast MF alpha 1 alpha-factor precursor is important for efficient transport through the secretory pathway. J. Bacteriol. 173:627-635.
18. Murphy KP, Jr, Gagne P, Pazmany C, Moody MD. 1998. Expression of human interleukin-17 in Pichia pastoris: purification and characterization. Protein Expr. Purif. 12:208-214. http://dx.doi.org/10.1006/prep.1997.0832.
19. Saito A, Usui M, Song Y, Azakami H, Kato A. 2002. Secretion of glycosylated alpha-lactalbumin in yeast Pichia pastoris. J. Biochem. 132: 77-82. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a003202.
20. Yamada M, Inui K, Hamada D, Nakahira K, Yanagihara K, Sakai N, Nishigaki T, Ozono K, Yanagihara I. 2004. Analysis of recombinant human saposin A expressed by Pichia pastoris. Biochem. Biophys. Res. Commun. 318:588-593. http://dx.doi.org/10.1016/j.bbrc.2004.04.069.
21. Ciani M, Fatichenti F. 2001. Killer toxin of Kluyveromyces phaffii DBVPG 6076 as a biopreservative agent to control apiculate wine Yeasts. Appl. Environ. Microbiol. 67:3058-3063. http://dx.doi.org/10.1128/AEM.67.7.3058-3063.2001.
22. Comitini F, De IJ, Pepe L, Mannazzu I, Ciani M. 2004. Pichia anomala and Kluyveromyces wickerhamii killer toxins as new tools against Dekkera/Brettanomyces spoilage yeasts. FEMS Microbiol. Lett. 238:235-240. http://dx.doi.org/10.1111/j.1574-6968.2004.tb09761.x.
23. Rosini G. 1983. The occurrence of killer characters in yeasts. Can. J. Microbiol. 29:1462-1464. http://dx.doi.org/10.1139/m83-224.
24. Munoz F, Palomares-Jerez MF, Daleo G, Villalain J, Guevara MG. 2011. Cholesterol and membrane phospholipid compositions modulate the leakage capacity of the swaposin domain from a potato aspartic protease (StAsp-PSI). Biochim. Biophys. Acta 1811:1038-1044. http://dx.doi.org/10.1016/j.bbalip.2011.08.013.
25. Kjeldsen T. 2000. Yeast secretory expression of insulin precursors. Appl. Microbiol. Biotechnol. 54:277-286. http://dx.doi.org/10.1007/s002530000402.
26. Antebi A, Fink GR. 1992. The yeast Ca(2+)-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution. Mol. Biol. Cell 3:633-654. http://dx.doi.org/10.1091/mbc.3.6.633.
27. Kjeldsen T, Brandt J, Andersen AS, Egel-Mitani M, Hach M, Pettersson AF, Vad K. 1996. A removable spacer peptide in an alpha-factor-leader/ insulin precursor fusion protein improves processing and concomitant yield of the insulin precursor in Saccharomyces cerevisiae. Gene 170:107-112. http://dx.doi.org/10.1016/0378-1119(95)00822-5.
28. Rayon C, Lerouge P, Lc Faye. 1998. The protein N-glycosylation in plants. J. Exp. Botany 49:1463-1472.
29. Bonekamp F, Oosterom J. 1994. On the safety of Kluyveromyces lactis: a review. Appl. Microbiol. Biotechnol. 41:1-3. http://dx.doi.org/10.1007/BF00166072.
30. van Ooyen AJ, Dekker P, Huang M, Olsthoorn MM, Jacobs DI, Colussi PA, Taron CH. 2006. Heterologous protein production in the yeast Kluyveromyces lactis. FEMS Yeast Res. 6:381-392. http://dx.doi.org/10.1111/j.1567-1364.2006.00049.x.
31. Montesinos E, Bardaji E. 2008. Synthetic antimicrobial peptides as agricultural pesticides for plant-disease control. Chem. Biodivers. 5:1225-1237. http://dx.doi.org/10.1002/cbdv.200890111.
32. Montesinos E. 2007. Antimicrobial peptides and plant disease control. FEMS Microbiol. Lett. 270:1-11. http://dx.doi.org/10.1111/j.1574-6968.2007.00683.x.
33. Vidaver AK. 2002. Uses of antimicrobials in plant agriculture. Clin. Infect. Dis. 34(Suppl 3):S107-S110. http://dx.doi.org/10.1086/340247.