Plant lectin-like antibacterial proteins from phytopathogens Pseudomonas syringae and Xanthomonas citri
Article first published online: 20 FEB 2012
© 2012 Society for Applied Microbiology and Blackwell Publishing Ltd
Environmental Microbiology Reports
Special Issue: Ecology, Evolution and Population Genetics of Pathogenic Microbes
Volume 4, Issue 4, pages 373–380, August 2012
How to Cite
Ghequire, M. G. K., Li, W., Proost, P., Loris, R. and De Mot, R. (2012), Plant lectin-like antibacterial proteins from phytopathogens Pseudomonas syringae and Xanthomonas citri. Environmental Microbiology Reports, 4: 373–380. doi: 10.1111/j.1758-2229.2012.00331.x
- Issue published online: 16 JUL 2012
- Article first published online: 20 FEB 2012
- Received 17 November, 2011; revised 15 January, 2012; accepted 30 January, 2012.
Fig. S1. Multiple-sequence alignment of LlpA from Pseudomonas putida BW11M1 and LlpA1 and LlpA2 from P. fluorescens Pf-5 with hypothetical proteins from P. syringae pv. aptata DSM 50252 (PSYAP_13445), P. syringae pv. syringae (Pss642), Xanthomonas axonopodis pv. citri (XAC0868*), Burkholderia ambifaria MEX-5 (Bamb_0926*), Burkholderia cenocepacia AU 1054 (Bcen_1092* and Bcen_1091*) and Arthrobacter sp. FB24 (Arth_4524). For proteins labelled with an asterisk, the respective predicted N-terminal signal sequence was removed. Differential shading reflects the extent of sequence conservation.
Table S1. List of primers used in this study.
Table S2. List of additional Pseudomonas strains tested for sensitivity to recombinant proteins LlpABW11M1, LlpA1Pf-5, LlpAPss642 and LlpAXcm761. Strains with an identical sensitivity pattern are grouped (see Table 1).
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