Production and evaluation of the utility of novel phage display-derived peptide ligands to Salmonella spp. for magnetic separation

J Appl Microbiol. 2013 Jul;115(1):271-81. doi: 10.1111/jam.12207. Epub 2013 Apr 15.

Abstract

Aims: The objectives of this study were to produce Salmonella-specific peptide ligands by phage display biopanning and evaluate their use for magnetic separation (MS).

Methods and results: Four-phage display biopanning rounds were performed, and the peptides expressed by the two most Salmonella-specific (on the basis of phage-binding ELISA results) phage clones, MSal020401 and MSal020417, were chemically synthesized and coupled to MyOne™ tosylactivated Dynabeads(®). Peptide capture capability for whole Salmonella cells from nonenriched broth cultures was quantified by MS + plate counts and MS + Greenlight™ detection and compared to capture capability of anti-Salmonella (antibody-coated) Dynabeads(®). MS + Greenlight™ gave a more comprehensive picture of capture capability than MS + plate counts and showed that Peptide MSal020417-coated beads exhibited at least similar, if not better, capture capability to anti-Salmonella Dynabeads(®) (mean capture values of 36·0 ± 18·2 and 31·2 ± 20·1%, respectively, over Salmonella spp. concentration range 3 × 10(1) -3 × 10(6) CFU ml(-1)) with cross-reactivity of ≤1·9% to three other foodborne pathogens: Escherichia coli, Listeria monocytogenes and Campylobacter jejuni.

Conclusions: One of the phage display-derived peptide ligands was demonstrated by MS + Greenlight™ to be a viable antibody alternative for MS of Salmonella spp.

Significance and impact of the study: This study demonstrates an antibody-free approach to Salmonella detection and opens substantial possibilities for more rapid tests for this bacterium.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Surface Display Techniques*
  • Ligands
  • Magnetic Phenomena
  • Peptides / chemistry
  • Peptides / metabolism*
  • Salmonella / isolation & purification*

Substances

  • Ligands
  • Peptides