On-resin cleavage of bacterially expressed fusion proteins for purification of active recombinant peptides SK-29, KR-20, LL-29, and LL-23 from human sweat or skin

Protein Expression and Purification

Volumn 55, Issue 2, 2007, Pages 395-405

  Li, Yifeng ^a   Li, Xia ^a   Wang, Guangshun ^a  

^a UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

Author keywords

Antimicrobial peptides; Double cleavage; Escherichia coli; HPLC; LL 37; NMR; On resin cleavage; Peptide aggregation; Target identification

Indexed keywords

HYBRID PROTEIN; PRIMER DNA;

ARTICLE; ESCHERICHIA COLI; GENETICS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; ISOLATION AND PURIFICATION; METABOLISM; NUCLEAR MAGNETIC RESONANCE; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; SKIN; SWEAT;

BASE SEQUENCE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DNA PRIMERS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; HUMANS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; RECOMBINANT FUSION PROTEINS; SKIN; SWEAT;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 34548487515     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2007.04.023     Document Type: Article

References (30)

1. Agerberth B., Gunne H., Odeberg J., Kogner P., Boman H.G., and Gudmundsson G.H. FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis. Proc. Natl. Acad. Sci. USA 92 (1995) 195-199
2. Zanetti M. Cathelicidins, multifunctional peptides of the innate immunity. J. Leukoc. Biol. 75 (2004) 39-48
3. Wang G. Tool developments for structure-function studies of host defense peptides. Protein Pept. Lett. 14 (2007) 57-69
4. Putsep K., Carlsson G., Boman H.G., and Andersson M. Deficiency of antibacterial peptides in patients with morbus Kostmann: an observation study. Lancet 360 (2002) 1144-1149
5. Nizet V., Ohtake T., Lauth X., Trowbridge J., Rudisill J., Dorschner R.A., Pestonjamasp V., Piraino J., Huttner K., and Gallo R.L. Innate antimicrobial peptide protects the skin from invasive bacterial infection. Nature 414 (2001) 454-457
6. Lee P.H., Ohtake T., Zaiou M., Murakami M., Rudisill J.A., Lin K.H., and Gallo R.L. Expression of an additional cathelicidin antimicrobial peptide protects against bacterial skin infection. Proc. Natl. Acad. Sci. USA 102 (2005) 3750-3755
7. Sorensen O.E., Gram L., Johnsen A.H., Andersson E., Bangsboll S., Tjabringa G.S., Hiemstra P.S., Malm J., Egesten A., and Borregaard N. Processing of seminal plasma hCAP-18 to ALL-38 by gastricsin: a novel mechanism of generating antimicrobial peptides in vagina. J. Biol. Chem. 278 (2003) 28540-28546
8. Murakami M., Lopez-Garcia B., Braff M., Dorschner R.A., and Gallo R.L. Postsecretory processing generates multiple cathelicidins for enhanced topical antimicrobial defense. J. Immunol. 172 (2004) 3070-3077
9. Yamasaki K., Schauber J., Coda A., Lin H., Dorschner R.A., Schechter N.M., Bonnart C., Descargues P., Hovnanian A., and Gallo R.L. Kallikrein-mediated proteolysis regulates the antimicrobial effects of cathelicidins in skin. FASEB J. 20 (2006) 2068-2080
10. Li Y., Li X., and Wang G. Cloning, expression, isotope labeling, and purification of human antimicrobial peptide LL-37 in Escherichia coli for NMR studies. Protein Expr. Purif. 47 (2006) 498-505
11. Li Y., Li X., Li H., Lockridge O., and Wang G. A novel method for purifying human host defense cathelicidin LL-37 by utilizing its inherent property of aggregation. Protein Expr. Purif. 54 (2007) 157-165
12. Kay L.E., Keifer P.A., and Saarinen T. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114 (1992) 10663-10665
13. Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., and Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6 (1995) 277-293
14. Wang G. Structural biology of antimicrobial peptides by NMR. Curr. Org. Chem. 10 (2006) 569-581
15. Wang G., Li Y., and Li X. Correlation of three-dimensional structures with antibacterial activity of a group of peptides designed based on a nontoxic bacterial membrane anchor. J. Biol. Chem. 280 (2005) 5803-5811
16. Hong I.P., Lee S.J., Kim Y.S., and Choi S.G. Recombinant expression of human cathelicidin (hCAP18/LL-37) in Pichia pastoris. Biotechnol. Lett. 29 (2006) 73-78
17. Yang Y., Zheng G., Li G., Zhang X., Cao Z., Rao Q., and Wu K. Expression of bioactive recombinant GSLL-39, a variant of human antimicrobial peptide LL-37, in Escherichia coli. Protein Expr. Purif. 37 (2004) 229-235
18. Moon J.Y., Henzler-Wildman K.A., and Ramamoorthy A. Expression and purification of a recombinant LL-37 from Escherichia coli. Biochim. Biophys. Acta 1758 (2006) 1351-1358
19. Guo L.-W., Assadi-Porter F.M., Grant J.E., Wu H., Markley J.L., and Ruoho A.E. One-step purification of bacterially expressed recombinant transducin α-subunit and isotopically labeled PDE6 γ-subunit for NMR analysis. Protein Expr. Purif. 51 (2007) 187-197
20. Wang Z., and Wang G. APD: the antimicrobial peptide database. Nucleic Acids Res. 32 (2004) D590-D592
21. Li X., Li Y., Han H., Miller D., and Wang G. Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region. J. Am. Chem. Soc. 128 (2006) 5776-5785
22. Zasloff M. Antimicrobial peptides of multicellullar organisms. Nature 415 (2002) 359-365
23. Hancock R.E.W., and Sahl H.-G. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 24 (2006) 1551-1557
24. Oren Z., Lerman J.C., Gudmundsson G.H., Agerberth B., and Shai Y. Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell-selective activity. Biochem. J. 341 (1999) 501-513
25. Wang Y., Agerberth B., Lothgren A., Almstedt A., and Johansson J. Apolipoprotein A-I binds and inhibits the human antibacterial/cytotoxic peptide LL-37. J. Biol. Chem. 273 (1998) 33115-33118
26. Weiner D.J., Bucki R., and Janmey P.A. The antimicrobial activity of the cathelicidin LL-37 is inhibited by F-actin bundles and restored by gelsolin. Am. J. Respir. Cell Mol. Biol. 28 (2003) 738-745
27. R. Bucki, F.J. Byfield, P.A. Janmey, Release of the antimicrobial LL37 peptide from DNA/F-actin bundles in CF sputum, Eur. Respir. J. In press (2007).
28. Ciornei C.D., Sigurdardottir T., Schmidtchen A., and Bodelsson M. Antimicrobial and chemoattractant activity, lipopolysacharide neutralization, cytotoxicity, and inhibition by serum of analogs of human cathelicidin LL-37. Antimicrob. Agents Chemother. 49 (2005) 2845-2850
29. Sorensen O.E., Follin P., Johnsen A.H., Calafat J., Tjabringa G.S., Hiemstra P.S., and Borregaard N. Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Blood 97 (2001) 3951-3959
30. Waddell W.J. A simple ultraviolet spectrophotometric method for the determination of protein. J. Lab. Clin. Med. 48 (1956) 311-314