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id:"swepub:oai:lup.lub.lu.se:8c7e40d1-16a3-4736-b012-fa9ac5daaac6"
 

Sökning: id:"swepub:oai:lup.lub.lu.se:8c7e40d1-16a3-4736-b012-fa9ac5daaac6" > In Vitro Selection ...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004950naa a2200553 4500
001oai:lup.lub.lu.se:8c7e40d1-16a3-4736-b012-fa9ac5daaac6
003SwePub
008160401s2014 | |||||||||||000 ||eng|
024a https://lup.lub.lu.se/record/44314862 URI
024a https://doi.org/10.1007/s12033-014-9749-x2 DOI
040 a (SwePub)lu
041 a engb eng
042 9 SwePub
072 7a art2 swepub-publicationtype
072 7a ref2 swepub-contenttype
100a Barfod, Andersu Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)orgk-aba
2451 0a In Vitro Selection of RNA Aptamers Directed Against Protein E: A Haemophilus influenzae Adhesin. : a Haemophilus influenzae adhesin
264 c 2014-03-29
264 1b Springer Science and Business Media LLC,c 2014
300 a 12 s.
520 a Protein E (PE) of Haemophilus influenzae is a highly conserved ubiquitous surface protein involved in adhesion to and activation of epithelial cells. The host proteins-vitronectin, laminin, and plasminogen are major targets for PE-dependent interactions with the host. To identify novel inhibitory molecules of PE, we used an in vitro selection method based on systematic evolution of ligands by exponential enrichment known as SELEX in order to select 2'F-modified RNA aptamers that specifically bind to PE. Fourteen selection cycles were performed with decreasing concentrations of PE. Sequencing of clones from the 14th selection round revealed the presence of semiconserved sequence motifs in loop regions of the RNA aptamers. Among these, three aptamers showed the highest affinity to PE in electrophoretic mobility shift assays and in dot blots. These three aptamers also inhibited the interaction of PE with vitronectin as revealed by ELISA. Moreover, pre-treatment of H. influenzae with the aptamers significantly inhibited binding of vitronectin to the bacterial surface. Biacore experiments indicated that one of the aptamers had a higher binding affinity for PE as compared to the other aptamers. Our results show that it is possible to select RNA inhibitors against bacterial adhesins using SELEX in order to inhibit interactions with target proteins.
650 7a MEDICIN OCH HÄLSOVETENSKAPx Medicinsk bioteknologix Medicinsk bioteknologi0 (SwePub)304012 hsv//swe
650 7a MEDICAL AND HEALTH SCIENCESx Medical Biotechnologyx Medical Biotechnology0 (SwePub)304012 hsv//eng
653 a Adhesins, Bacterial
653 a Aptamers, Nucleotide
653 a Base Sequence
653 a Biotechnology
653 a DNA, Bacterial
653 a Haemophilus influenzae
653 a Humans
653 a In Vitro Techniques
653 a Molecular Sequence Data
653 a Nucleic Acid Conformation
653 a Protein Binding
653 a SELEX Aptamer Technique
653 a Surface Plasmon Resonance
653 a Vitronectin
653 a Journal Article
653 a Research Support, Non-U.S. Gov't
700a Singh, Birendrau Lund University,Lunds universitet,Klinisk mikrobiologi, Malmö,Forskargrupper vid Lunds universitet,Clinical Microbiology, Malmö,Lund University Research Groups4 aut0 (Swepub:lu)med-bas
700a Johanson, Urbanu Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)pbio-ujo
700a Riesbeck, Kristianu Lund University,Lunds universitet,Klinisk mikrobiologi, Malmö,Forskargrupper vid Lunds universitet,Clinical Microbiology, Malmö,Lund University Research Groups4 aut0 (Swepub:lu)mikr-kri
700a Kjellbom, Peru Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)pbio-pkj
710a Biokemi och Strukturbiologib Centrum för Molekylär Proteinvetenskap4 org
773t Molecular Biotechnologyd : Springer Science and Business Media LLCg 56:8, s. 714-725q 56:8<714-725x 1559-0305x 1073-6085
856u http://www.ncbi.nlm.nih.gov/pubmed/24682699?dopt=Abstracty FULLTEXT
856u http://dx.doi.org/10.1007/s12033-014-9749-xx freey FULLTEXT
8564 8u https://lup.lub.lu.se/record/4431486
8564 8u https://doi.org/10.1007/s12033-014-9749-x

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