Thymic stromal lymphopoietin exerts antimicrobial activities.
(2011) In Experimental Dermatology 20(12). p.1004-1010- Abstract
- Thymic stromal lymphopoietin (TSLP) is an interleukin-7-like cytokine expressed by epithelial cells and reported to be involved in allergic diseases and atopic eczema. The presence of several predicted α-helical regions in TSPL, a structure characterizing many classical antimicrobial peptides (AMPs), prompted us to investigate whether TSLP exerts antimicrobial activities. Recombinant human TSLP exerted antimicrobial activity, particularly against Gram-negative bacteria. Using synthetic overlapping peptide 20-mers of TSLP, it was demonstrated that the antimicrobial effect is primarily mediated by the C-terminal region of the protein. MKK34 (MKKRRKRKVTTNKCLEQVSQLQGLWRRFNRPLLK), a peptide spanning a C-terminal α-helical region in TSLP, showed... (More)
- Thymic stromal lymphopoietin (TSLP) is an interleukin-7-like cytokine expressed by epithelial cells and reported to be involved in allergic diseases and atopic eczema. The presence of several predicted α-helical regions in TSPL, a structure characterizing many classical antimicrobial peptides (AMPs), prompted us to investigate whether TSLP exerts antimicrobial activities. Recombinant human TSLP exerted antimicrobial activity, particularly against Gram-negative bacteria. Using synthetic overlapping peptide 20-mers of TSLP, it was demonstrated that the antimicrobial effect is primarily mediated by the C-terminal region of the protein. MKK34 (MKKRRKRKVTTNKCLEQVSQLQGLWRRFNRPLLK), a peptide spanning a C-terminal α-helical region in TSLP, showed potent antimicrobial activities, in physiological salt conditions and in the presence of human plasma. Fluorescent studies of peptide-treated bacteria, electron microscopy and liposome leakage models showed that MKK34 exerted membrane-disrupting effects comparable to those of the classical AMP LL-37. Moreover, TSLP was degraded into multiple fragments by staphylococcal V8 proteinase. One major antimicrobial degradation fragment was found to encompass the C-terminal antimicrobial region defined by the MKK34 peptide. We here describe a novel antimicrobial role for TSLP. The antimicrobial activity is primarily mediated by the C-terminal part of the protein. In combination with the previously known cytokine function of TSLP, our result indicates dual functions of the molecule and a previously unknown role in host defense. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2220676
- author
- Sonesson, Andreas LU ; Kasetty, Gopinath LU ; Olin, Anders LU ; Malmsten, Martin LU ; Mörgelin, Matthias LU ; Sørensen, Ole E LU and Schmidtchen, Artur LU
- organization
- publishing date
- 2011
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Experimental Dermatology
- volume
- 20
- issue
- 12
- pages
- 1004 - 1010
- publisher
- Wiley-Blackwell
- external identifiers
-
- wos:000297154000008
- pmid:22092577
- scopus:81455139902
- pmid:22092577
- ISSN
- 0906-6705
- DOI
- 10.1111/j.1600-0625.2011.01391.x
- language
- English
- LU publication?
- yes
- id
- 5248d733-7e47-4fc9-ba6d-7d2b984dcd70 (old id 2220676)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/22092577?dopt=Abstract
- date added to LUP
- 2016-04-04 07:34:23
- date last changed
- 2022-02-28 03:46:05
@article{5248d733-7e47-4fc9-ba6d-7d2b984dcd70,
abstract = {{Thymic stromal lymphopoietin (TSLP) is an interleukin-7-like cytokine expressed by epithelial cells and reported to be involved in allergic diseases and atopic eczema. The presence of several predicted α-helical regions in TSPL, a structure characterizing many classical antimicrobial peptides (AMPs), prompted us to investigate whether TSLP exerts antimicrobial activities. Recombinant human TSLP exerted antimicrobial activity, particularly against Gram-negative bacteria. Using synthetic overlapping peptide 20-mers of TSLP, it was demonstrated that the antimicrobial effect is primarily mediated by the C-terminal region of the protein. MKK34 (MKKRRKRKVTTNKCLEQVSQLQGLWRRFNRPLLK), a peptide spanning a C-terminal α-helical region in TSLP, showed potent antimicrobial activities, in physiological salt conditions and in the presence of human plasma. Fluorescent studies of peptide-treated bacteria, electron microscopy and liposome leakage models showed that MKK34 exerted membrane-disrupting effects comparable to those of the classical AMP LL-37. Moreover, TSLP was degraded into multiple fragments by staphylococcal V8 proteinase. One major antimicrobial degradation fragment was found to encompass the C-terminal antimicrobial region defined by the MKK34 peptide. We here describe a novel antimicrobial role for TSLP. The antimicrobial activity is primarily mediated by the C-terminal part of the protein. In combination with the previously known cytokine function of TSLP, our result indicates dual functions of the molecule and a previously unknown role in host defense.}},
author = {{Sonesson, Andreas and Kasetty, Gopinath and Olin, Anders and Malmsten, Martin and Mörgelin, Matthias and Sørensen, Ole E and Schmidtchen, Artur}},
issn = {{0906-6705}},
language = {{eng}},
number = {{12}},
pages = {{1004--1010}},
publisher = {{Wiley-Blackwell}},
series = {{Experimental Dermatology}},
title = {{Thymic stromal lymphopoietin exerts antimicrobial activities.}},
url = {{http://dx.doi.org/10.1111/j.1600-0625.2011.01391.x}},
doi = {{10.1111/j.1600-0625.2011.01391.x}},
volume = {{20}},
year = {{2011}},
}