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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03884naa a2200469 4500 | |
| 001 | oai:DiVA.org:liu-127057 | |
| 003 | SwePub | |
| 008 | 160413s2016 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-1270572 URI |
| 024 | 7 | a https://doi.org/10.1111/mmi.132692 DOI |
| 040 | a (SwePub)liu | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a art2 swepub-publicationtype |
| 100 | 1 | a Bednarska, Natalia G.u KULeuven, Belgium; VIB, Belgium4 aut |
| 245 | 1 0 | a Protein aggregation as an antibiotic design strategy |
| 264 | c 2015-12-09 | |
| 264 | 1 | b WILEY-BLACKWELL,c 2016 |
| 338 | a print2 rdacarrier | |
| 500 | a Funding Agencies|VIB; University of Leuven; Funds for Scientific Research Flanders (FWO); Flanders Institute for Science and Technology (IWT); Federal Office for Scientific Affairs of Belgium (Belspo) [IUAP P7/16]; Swedish Foundation for Strategic Research; Swedish Research Council; ERC Starting Independent Researcher Grant (Project: MUMID) from the European Research Council | |
| 520 | a Taking advantage of the xenobiotic nature of bacterial infections, we tested whether the cytotoxicity of protein aggregation can be targeted to bacterial pathogens without affecting their mammalian hosts. In particular, we examined if peptides encoding aggregation-prone sequence segments of bacterial proteins can display antimicrobial activity by initiating toxic protein aggregation in bacteria, but not in mammalian cells. Unbiased in vitro screening of aggregating peptide sequences from bacterial genomes lead to the identification of several peptides that are strongly bactericidal against methicillin-resistant Staphylococcus aureus. Upon parenteral administration in vivo, the peptides cured mice from bacterial sepsis without apparent toxic side effects as judged from histological and hematological evaluation. We found that the peptides enter and accumulate in the bacterial cytosol where they cause aggregation of bacterial polypeptides. Although the precise chain of events that leads to cell death remains to be elucidated, the ability to tap into aggregation-prone sequences of bacterial proteomes to elicit antimicrobial activity represents a rich and unexplored chemical space to be mined in search of novel therapeutic strategies to fight infectious diseases. | |
| 650 | 7 | a NATURVETENSKAPx Kemi0 (SwePub)1042 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Chemical Sciences0 (SwePub)1042 hsv//eng |
| 700 | 1 | a van Eldere, Johanu KULeuven, Belgium4 aut |
| 700 | 1 | a Gallardo, Rodrigou VIB, Belgium; KULeuven, Belgium4 aut |
| 700 | 1 | a Ganesan, Ashoku VIB, Belgium; KULeuven, Belgium4 aut |
| 700 | 1 | a Ramakers, Meineu VIB, Belgium; KULeuven, Belgium4 aut |
| 700 | 1 | a Vogel, Isabelu KULeuven, Belgium4 aut |
| 700 | 1 | a Baatsen, Pieteru VIB11, Belgium; KULeuven, Belgium4 aut |
| 700 | 1 | a Staes, Anu VIB, Belgium; University of Ghent, Belgium4 aut |
| 700 | 1 | a Goethals, Marcu VIB, Belgium; University of Ghent, Belgium4 aut |
| 700 | 1 | a Hammarström, Peru Linköpings universitet,Kemi,Tekniska fakulteten4 aut0 (Swepub:liu)perha81 |
| 700 | 1 | a Nilsson, Peter,d 1970-u Linköpings universitet,Kemi,Tekniska fakulteten4 aut0 (Swepub:liu)petni61 |
| 700 | 1 | a Gevaert, Krisu VIB, Belgium; University of Ghent, Belgium4 aut |
| 700 | 1 | a Schymkowitz, Joostu VIB, Belgium; KULeuven, Belgium4 aut |
| 700 | 1 | a Rousseau, Fredericu VIB, Belgium; KULeuven, Belgium4 aut |
| 710 | 2 | a KULeuven, Belgium; VIB, Belgiumb KULeuven, Belgium4 org |
| 773 | 0 | t Molecular Microbiologyd : WILEY-BLACKWELLg 99:5, s. 849-865q 99:5<849-865x 0950-382Xx 1365-2958 |
| 856 | 4 | u https://onlinelibrary.wiley.com/doi/pdfdirect/10.1111/mmi.13269 |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-127057 |
| 856 | 4 8 | u https://doi.org/10.1111/mmi.13269 |
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