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Nucleic Acids Research 2005 33(18):e162; doi:10.1093/nar/gni150
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Published online 19 October 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org

Methods Online

Proximity ligation assays with peptide conjugate ‘burrs’ for the sensitive detection of spores

Supriya Pai, Andrew D. Ellington1 and Matthew Levy1,*

Section of Molecular Genetics and Microbiology, School of Biological Sciences, University of Texas at Austin Austin, TX 78712, USA 1Institute for Cell and Molecular Biology, University of Texas at Austin Austin, TX 78712, USA

*To whom correspondence should be addressed. Tel: + 1 512 471 6445; Fax: +1 512 471 7014; Email: mattlevy{at}mail.utexas.edu

Received April 15, 2005. Revised September 5, 2005. Accepted September 18, 2005.

The proximity ligation assay (PLA) has previously been used for the sensitive and specific detection of single proteins. In order to adapt PLA methods for the detection of cell surfaces, we have generated multivalent peptide–oligonucleotide–phycoerythrin conjugates (‘burrs’) that can bind adjacent to one another on a cell surface and be ligated together to form unique amplicons. Real-time PCR detection of burr ligation events specifically identified as few as 100 Bacillus anthracis, 10 Bacillus subtilis and 1 Bacillus cereus spore. Burrs should prove to be generally useful for detecting and mapping interactions and distances between cell surface proteins.


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