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Microbiology 149 (2003), 3493-3505; DOI  10.1099/mic.0.26530-0
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Microbiology 149 (2003), 3493-3505; DOI  10.1099/mic.0.26530-0
© 2003 Society for General Microbiology

Phage display reveals 52 novel extracellular and transmembrane proteins from Lactobacillus reuteri DSM 20016T

Torun Wall, Stefan Roos, Karin Jacobsson, Anna Rosander and Hans Jonsson

Department of Microbiology, Swedish University of Agricultural Sciences, Box 7025, SE-750 07 Uppsala, Sweden

Correspondence
Hans Jonsson
Hans.Jonsson{at}mikrob.slu.se

Extracellular and transmembrane proteins are important for the binding of bacteria to intestinal surfaces and for their interaction with the host. The aim of this study was to identify genes encoding extracellular and transmembrane proteins from the probiotic bacterium Lactobacillus reuteri by construction and screening of a phage display library. This library was constructed by insertion of randomly fragmented DNA from L. reuteri into the phagemid vector pG3DSS, which was previously developed for screening for extracellular proteins. After affinity selection of the library, the L. reuteri inserts were sequenced and analysed with bioinformatic tools. The screening resulted in the identification of 52 novel genes encoding extracellular and transmembrane proteins. These proteins were classified as: transport proteins; enzymes; sensor–regulator proteins; proteins involved in host/microbial interactions; conserved hypothetical proteins; and unconserved hypothetical proteins. Further characterization of the extracellular and transmembrane proteins identified should contribute to the understanding of the probiotic properties of L. reuteri.


The GenBank accession numbers for the sequences determined in this study are given in Table 2.




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