Recombinant expression of human cathelicidin (hCAP18/LL-37) in Pichia pastoris
- Authors
- Hong, In-Pyo; Lee, Sung-Jae; Kim, Yong-Seok; Choi, Shin-Geon
- Issue Date
- Jan-2007
- Publisher
- SPRINGER
- Keywords
- cathelicidin; LL-37; heterologous expression; Pichia pastoris
- Citation
- BIOTECHNOLOGY LETTERS, v.29, no.1, pp.73 - 78
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOTECHNOLOGY LETTERS
- Volume
- 29
- Number
- 1
- Start Page
- 73
- End Page
- 78
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/180591
- DOI
- 10.1007/s10529-006-9202-8
- ISSN
- 0141-5492
- Abstract
- The constitutive expression of human cathelicidin LL-37 antimicrobial peptide was achieved using the methylotrophic yeast, Pichia pastoris. An LL-37 cDNA clone was amplified by PCR using human fetal cDNA library as template. The 111 bp fragment encoding mature LL-37 gene was subcloned into pGAPZ-E, an episomal form of the pGAPZB vector incorporating PARS1. It was then transformed into the P. pastoris X-33 strain for intracellular expression. A small peptide with a molecular mass of about 5 kDa was detected by 17% peptide-PAGE analysis. The recombinant LL-37 peptide was purified from the gel and its amino acid sequence was determined by LC-ESI-MS/MS analysis. The initiating amino acid, methionine, was still attached to the N-terminal region of recombinant LL-37. LL-37 crude extract from P. pastoris showed an antimicrobial activity against Micrococcus luteus as the test strain. The successful expression of human LL-37 indicates that the system may be applicable to the expression of other human defensins without resorting to fusion protein constructions.
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