Expression and characterization of recombinant human secretory leukocyte protease inhibitor (SLPI) protein from Pichia pastoris

Protein Expression and Purification

Volumn 67, Issue 2, 2009, Pages 175-181

  Li, Zhiguo ^a   Moy, Allison ^a   Sohal, Kirti ^a   Dam, Carolyn ^a   Kuo, Peter ^a   Whittaker, James ^b   Whittaker, Mei ^b   Düzgünes, Nejat ^c   Konopka, Krystyna ^c   Franz, Andreas H ^a   Lin Cereghino, Joan ^a   Lin Cereghino, Geoff P ^a  

^a UNIVERSITY OF THE PACIFIC   (United States)

^b OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^c UNIVERSITY OF THE PACIFIC   (United States)

Author keywords

HIV; Human secretory leukocyte protease inhibitor; Pichia pastoris; Recombinant protein; SLPI

Indexed keywords

RECOMBINANT PROTEIN; SECRETORY LEUKOCYTE PROTEINASE INHIBITOR; SLPI PROTEIN, HUMAN; TRYPSIN;

ARTICLE; BIOSYNTHESIS; CHEMISTRY; CULTURE TECHNIQUE; FERMENTATION; GENETIC TRANSFECTION; GENETICS; GLYCOSYLATION; HUMAN; ISOLATION AND PURIFICATION; METABOLISM; PICHIA; PROTEIN FOLDING;

CELL CULTURE TECHNIQUES; FERMENTATION; GLYCOSYLATION; HUMANS; PICHIA; PROTEIN FOLDING; RECOMBINANT PROTEINS; SECRETORY LEUKOCYTE PEPTIDASE INHIBITOR; TRANSFECTION; TRYPSIN;

BACTERIA (MICROORGANISMS); HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1; PICHIA PASTORIS;

EID: 67650117727     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2009.06.001     Document Type: Article

References (48)

1. Doumas S., Kolokotronis A., and Stefanopoulos P. Anti-inflammatory and antimicrobial roles of secretory leukocyte protease inhibitor. Infect. Immun. 73 (2005) 1271-1274
2. Moreau T., Baranger K., Dade S., Dallet-Choisy S., Guyot N., and Zani M.L. Multifaceted roles of human elafin and secretory leukocyte proteinase inhibitor (SLPI), two serine protease inhibitors of the chelonianin family. Biochimie 90 (2008) 284-295
3. Lee J.K., Chae S.W., Cho J.G., Lee H.M., Hwang S.J., and Jung H.H. Expression of secretory leukocyte protease inhibitor in middle ear cholesteatoma. Eur. Arch. Otorhinolaryngol. 263 (2006) 1077-1081
4. Weldon S., McGarry N., Taggart C.C., and McElvaney N.G. The role of secretory leucoprotease inhibitor in the resolution of inflammatory responses. Biochem. Soc. Trans. 35 (2007) 273-276
5. Ashcroft G.S., Lei K., Jin W., Longenecker G., Kulkarni A.B., Greenwell-Wild T., Hale-Donze H., McGrady G., Song X.Y., and Wahl S.M. Secretory leukocyte protease inhibitor mediates non-redundant functions necessary for normal wound healing. Nat. Med. 6 (2000) 1147-1153
6. Williams S.E., Brown T.I., Roghanian A., and Sallenave J.M. SLPI and elafin: one glove, many fingers. Clin. Sci. (Lond.) 110 (2006) 21-35
7. Hiemstra P.S., Maassen R.J., Stolk J., Heinzel-Wieland R., Steffens G.J., and Dijkman J.H. Antibacterial activity of antileukoprotease. Infect. Immun. 64 (1996) 4520-4524
8. Tomee J.F., Koeter G.H., Hiemstra P.S., and Kauffman H.F. Secretory leukoprotease inhibitor: a native antimicrobial protein presenting a new therapeutic option?. Thorax 53 (1998) 114-116
9. Chattopadhyay A., Gray L.R., Patton L.L., Caplan D.J., Slade G.D., Tien H.C., and Shugars D.C. Salivary secretory leukocyte protease inhibitor and oral candidiasis in human immunodeficiency virus type 1-infected persons. Infect. Immun. 72 (2004) 1956-1963
10. Cole A.M., and Cole A.L. Antimicrobial polypeptides are key anti-HIV-1 effector molecules of cervicovaginal host defense. Am. J. Reprod. Immunol. 59 (2008) 27-34
11. Fakioglu E., Wilson S.S., Mesquita P.M., Hazrati E., Cheshenko N., Blaho J.A., and Herold B.C. Herpes simplex virus downregulates secretory leukocyte protease inhibitor: a novel immune evasion mechanism. J. Virol. 82 (2008) 9337-9344
12. Gomez S.A., Arguelles C.L., Guerrieri D., Tateosian N.L., Amiano N.O., Slimovich R., Maffia P.C., Abbate E., Musella R.M., Garcia V.E., and Chuluyan H.E. Secretory leukocyte protease inhibitor: a secreted pattern recognition receptor for mycobacteria. Am. J. Respir. Crit. Care Med. 179 (2009) 247-253
13. Kazmi S.H., Naglik J.R., Sweet S.P., Evans R.W., O'Shea S., Banatvala J.E., and Challacombe S.J. Comparison of human immunodeficiency virus type 1-specific inhibitory activities in saliva and other human mucosal fluids. Clin. Vaccine Immunol. 13 (2006) 1111-1118
14. McNeely T.B., Dealy M., Dripps D.J., Orenstein J.M., Eisenberg S.P., and Wahl S.M. Secretory leukocyte protease inhibitor: a human saliva protein exhibiting anti-human immunodeficiency virus 1 activity in vitro. J. Clin. Invest. 96 (1995) 456-464
15. Shine N., Konopka K., and Duzgunes N. The anti-HIV-1 activity associated with saliva. J. Dent. Res. 76 (1997) 634-640
16. Ma G., Greenwell-Wild T., Lei K., Jin W., Swisher J., Hardegen N., Wild C.T., and Wahl S.M. Secretory leukocyte protease inhibitor binds to annexin II, a cofactor for macrophage HIV-1 infection. J. Exp. Med. 200 (2004) 1337-1346
17. Grutter M.G., Fendrich G., Huber R., and Bode W. The 2.5 A X-ray crystal structure of the acid-stable proteinase inhibitor from human mucous secretions analysed in its complex with bovine alpha-chymotrypsin. EMBO J. 7 (1988) 345-351
18. Lin C.C., and Chang J.Y. Pathway of oxidative folding of secretory leucocyte protease inhibitor: an 8-disulfide protein exhibits a unique mechanism of folding. Biochemistry 45 (2006) 6231-6240
19. Eisenberg S.P., Hale K.K., Heimdal P., and Thompson R.C. Location of the protease-inhibitory region of secretory leukocyte protease inhibitor. J. Biol. Chem. 265 (1990) 7976-7981
20. Kramps J.A., van Twisk C., Appelhans H., Meckelein B., Nikiforov T., and Dijkman J.H. Proteinase inhibitory activities of antileukoprotease are represented by its second COOH-terminal domain. Biochim. Biophys. Acta 1038 (1990) 178-185
21. Lin C.C., Lu B.Y., and Chang J.Y. Conformational stability of secretory leucocyte protease inhibitor: a protein with no hydrophobic core and very little secondary structure. Biochim. Biophys. Acta 1764 (2006) 1286-1291
22. Gibbons A.M., McElvaney N.G., Taggart C.C., and Cryan S.A. Delivery of rSLPI in a liposomal carrier for inhalation provides protection against cathepsin L degradation. J. Microencapsul. (2008) 1-10
23. Nakamura K., Takamoto N., Hongo A., Kodama J., Abrzua F., Nasu Y., Kumon H., and Hiramatsu Y. Secretory leukoprotease inhibitor inhibits cell growth through apoptotic pathway on ovarian cancer. Oncol. Rep. 19 (2008) 1085-1091
24. ClinicalTrials.gov., Bethesda (MD): National Institute of Dental and Craniofacial Research (US). 2000 April - Identifier NCT00005569, Effect of topical SLPI on skin wounds, July 2003. Available from: http://clinicaltrials.gov/ct2/show/NCT00005569.
25. Schneeberger S., Hautz T., Wahl S.M., Brandacher G., Sucher R., Steinmassl O., Steinmassl P., Wright C.D., Obrist P., Werner E.R., Mark W., Troppmair J., Margreiter R., and Amberger A. The effect of secretory leukocyte protease inhibitor (SLPI) on ischemia/reperfusion injury in cardiac transplantation. Am. J. Transplant. 8 (2008) 773-782
26. Verani A., Sironi F., Siccardi A.G., Lusso P., and Vercelli D. Inhibition of CXCR4-tropic HIV-1 infection by lipopolysaccharide: evidence of different mechanisms in macrophages and T lymphocytes. J. Immunol. 168 (2002) 6388-6395
27. Hamaker K.H., Liu J., Seely R.J., Ladisch C.M., and Ladisch M.R. Chromatography for rapid buffer exchange and refolding of secretory leukocyte protease inhibitor. Biotechnol. Prog. 12 (1996) 184-189
28. Harcum S., and Dale B. Renaturation of recombinant secretory leukocyte protease inhibitor: aspects of disulfide bond formation kinetics. Biotech. Lett. 15 (1993) 943-948
29. Shugars D.C., Sauls D.L., and Weinberg J.B. Secretory leukocyte protease inhibitor blocks infectivity of primary monocytes and mononuclear cells with both monocytotropic and lymphocytotropic strains of human immunodeficiency virus type I. Oral Dis. 3 Suppl. 1 (1997) S70-S72
30. Turpin J.A., Schaeffer C.A., Bu M., Graham L., Buckheit Jr. R.W., Clanton D., and Rice W.G. Human immunodeficiency virus type-1 (HIV-1) replication is unaffected by human secretory leukocyte protease inhibitor. Antiviral Res. 29 (1996) 269-277
31. Konopka K., Shine N., Pretzer E., and Duzgunes N. Secretory leukocyte protease inhibitor (SLPI): oxidation of SLPI does not explain its variable anti-HIV activity. J. Dent. Res. 78 (1999) 1773-1776
32. Shine N.R., Wang S.C., Konopka K., Burks E.A., Duzgunes N., and Whitman C.P. Secretory leukocyte protease inhibitor: inhibition of human immunodeficiency virus-1 infection of monocytic THP-1 cells by a newly cloned protein. Bioorg. Chem. 30 (2002) 249-263
33. Gray L.R., Alexander A.L., and Shugars D.C. Construction, non-denaturing affinity purification, and characterization of baculovirally expressed human secretory leukocyte protease inhibitor. Protein Expr. Purif. 26 (2002) 179-186
34. Lin Cereghino J., and Cregg J.M. Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol. Rev. 24 (2000) 45-66
35. Macauley-Patrick S., Fazenda M.L., McNeil B., and Harvey L.M. Heterologous protein production using the Pichia pastoris expression system. Yeast 22 (2005) 249-270
36. Cregg J.M., Madden K.R., Barringer K.J., Thill G.P., and Stillman C.A. Functional characterization of the two alcohol oxidase genes from the yeast Pichia pastoris. Mol. Cell. Biol. 9 (1989) 1316-1323
37. Cregg J.M., Barringer K.J., Hessler A.Y., and Madden K.R. Pichia pastoris as a host system for transformations. Mol. Cell. Biol. 5 (1985) 3376-3385
38. Sambrook J., Fritsch E.F., and Maniatis T. Molecular Cloning: A Laboratory Handbook (1989), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
39. Cregg J.M., and Russell K.A. Transformation. In: Higgins D.R., and Cregg J.M. (Eds). Pichia Protocols (1998), Humana Press, Totowa, NJ 27-39
40. Lin-Cereghino J., Wong W.W., Xiong S., Giang W., Luong L.T., Vu J., Johnson S.D., and Lin-Cereghino G.P. Condensed protocol for competent cell preparation and transformation of the methylotrophic yeast Pichia pastoris. Biotechniques 38 (2005) 44-48
41. Thor D., Xiong S., Orazem C., Kwan A.-C., Cregg J., Lin-Cereghino J., and Lin-Cereghino G. Cloning and characterization of the Pichia pastoris MET2 gene as a selectable marker. FEMS Yeast Res. 5 (2005) 935-942
42. Sunga A.J., Tolstorukov I., and Cregg J.M. Posttransformational vector amplification in the yeast Pichia pastoris. FEMS Yeast Res. 8 (2008) 870-876
43. Muller P.Y., Janovjak H., Miserez A.R., and Dobbie Z. Processing of gene expression data generated by quantitative real-time RT-PCR. Biotechniques 32 (2002) 1372-1374 1376, 1378, 1379
44. Stratton J., Chiruvolu V., and Meagher M. High cell-density fermentation. Methods Mol. Biol. 103 (1998) 107-120
45. Whittaker M.M., and Whittaker J.W. Expression of recombinant galactose oxidase by Pichia pastoris. Protein Expr. Purif. 20 (2000) 105-111
46. Lin-Cereghino G.P., Leung W., and Lin-Cereghino J. Expression of protein in Pichia pastoris. In: Dyson M., and Durocher Y. (Eds). Expression Systems: Methods Express (2007), Scion Publishing Limited, Oxfordshire 123-145
47. Cregg J.M., Vedvick T.S., and Raschke W.C. Recent advances in the expression of foreign genes in Pichia pastoris. Bio/Technology 11 (1993)
48. Tsai C.W., Duggan P.F., Shimp Jr. R.L., Miller L.H., and Narum D.L. Overproduction of Pichia pastoris or Plasmodium falciparum protein disulfide isomerase affects expression, folding and O-linked glycosylation of a malaria vaccine candidate expressed in P. pastoris. J. Biotechnol. 121 (2006) 458-470