Antimicrobial activity of a C-terminal peptide from human extracellular superoxide dismutase.
Pasupuleti, Mukesh LU ; Davoudi, Mina LU
; Malmsten, Martin
LU
and Schmidtchen, Artur
LU
(2009)
In BMC Research Notes
2(Jul 15).
- Abstract
- ABSTRACT: BACKGROUND: Antimicrobial peptides (AMP) are important effectors of the innate immune system. Although there is increasing evidence that AMPs influence bacteria in a multitude of ways, bacterial wall rupture plays the pivotal role in the bactericidal action of AMPs. Structurally, AMPs share many similarities with endogenous heparin-binding peptides with respect to secondary structure, cationicity, and amphipathicity. FINDINGS: In this study, we show that RQA21 (RQAREHSERKKRRRESECKAA), a cationic and hydrophilic heparin-binding peptide corresponding to the C-terminal region of extracellular superoxide dismutase (SOD), exerts antimicrobial activity against Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, Bacillus... (More)
- ABSTRACT: BACKGROUND: Antimicrobial peptides (AMP) are important effectors of the innate immune system. Although there is increasing evidence that AMPs influence bacteria in a multitude of ways, bacterial wall rupture plays the pivotal role in the bactericidal action of AMPs. Structurally, AMPs share many similarities with endogenous heparin-binding peptides with respect to secondary structure, cationicity, and amphipathicity. FINDINGS: In this study, we show that RQA21 (RQAREHSERKKRRRESECKAA), a cationic and hydrophilic heparin-binding peptide corresponding to the C-terminal region of extracellular superoxide dismutase (SOD), exerts antimicrobial activity against Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, Bacillus subtilis and Candida albicans. The peptide was also found to induce membrane leakage of negatively charged liposomes. However, its antibacterial effects were abrogated in physiological salt conditions as well as in plasma. CONCLUSION: The results provide further evidence that heparin-binding peptide regions are multifunctional, but also illustrate that cationicity alone is not sufficient for AMP function at physiological conditions. However, our observation, apart from providing a link between heparin-binding peptides and AMPs, raises the hypothesis that proteolytically generated C-terminal SOD-derived peptides could interact with, and possibly counteract bacteria. Further studies are therefore merited to study a possible role of SOD in host defence. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1453055
- author
- Pasupuleti, Mukesh
LU
; Davoudi, Mina
LU
; Malmsten, Martin
LU
and Schmidtchen, Artur
LU
- organization
- publishing date
- 2009
- type
- Contribution to journal
- publication status
- published
- subject
- in
- BMC Research Notes
- volume
- 2
- issue
- Jul 15
- article number
- 136
- publisher
- BioMed Central (BMC)
- external identifiers
-
- pmid:19604396
- scopus:77049089782
- pmid:19604396
- ISSN
- 1756-0500
- DOI
- 10.1186/1756-0500-2-136
- language
- English
- LU publication?
- yes
- id
- 6ab233a8-6995-41c0-808b-89ef2002ee65 (old id 1453055)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/19604396?dopt=Abstract
- date added to LUP
- 2016-04-04 09:19:13
- date last changed
- 2022-03-23 04:59:08
@article{6ab233a8-6995-41c0-808b-89ef2002ee65,
abstract = {{ABSTRACT: BACKGROUND: Antimicrobial peptides (AMP) are important effectors of the innate immune system. Although there is increasing evidence that AMPs influence bacteria in a multitude of ways, bacterial wall rupture plays the pivotal role in the bactericidal action of AMPs. Structurally, AMPs share many similarities with endogenous heparin-binding peptides with respect to secondary structure, cationicity, and amphipathicity. FINDINGS: In this study, we show that RQA21 (RQAREHSERKKRRRESECKAA), a cationic and hydrophilic heparin-binding peptide corresponding to the C-terminal region of extracellular superoxide dismutase (SOD), exerts antimicrobial activity against Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, Bacillus subtilis and Candida albicans. The peptide was also found to induce membrane leakage of negatively charged liposomes. However, its antibacterial effects were abrogated in physiological salt conditions as well as in plasma. CONCLUSION: The results provide further evidence that heparin-binding peptide regions are multifunctional, but also illustrate that cationicity alone is not sufficient for AMP function at physiological conditions. However, our observation, apart from providing a link between heparin-binding peptides and AMPs, raises the hypothesis that proteolytically generated C-terminal SOD-derived peptides could interact with, and possibly counteract bacteria. Further studies are therefore merited to study a possible role of SOD in host defence.}},
author = {{Pasupuleti, Mukesh and Davoudi, Mina and Malmsten, Martin and Schmidtchen, Artur}},
issn = {{1756-0500}},
language = {{eng}},
number = {{Jul 15}},
publisher = {{BioMed Central (BMC)}},
series = {{BMC Research Notes}},
title = {{Antimicrobial activity of a C-terminal peptide from human extracellular superoxide dismutase.}},
url = {{http://dx.doi.org/10.1186/1756-0500-2-136}},
doi = {{10.1186/1756-0500-2-136}},
volume = {{2}},
year = {{2009}},
}