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Microbiology 154 (2008), 1258-1270; DOI  10.1099/mic.0.2007/014894-0
© 2008 Society for General Microbiology

The Sinorhizobium meliloti MsbA2 protein is essential for the legume symbiosis

Sebastian Beck1,{dagger}, Victoria L. Marlow1,2,{dagger}, Katy Woodall1, William T. Doerrler3, Euan K. James4 and Gail P. Ferguson1,2

1 Institute of Cell Biology and Centre for Science at Extreme Conditions, School of Biological Sciences, King's Buildings, University of Edinburgh, Edinburgh EH9 3JR, UK
2 School of Medicine, Department of Medicine and Therapeutics, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, UK
3 Department of Biological Sciences, Louisiana State University, 202 Life Sciences Building, Baton Rouge, LA 70803, USA
4 College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK

Correspondence
Gail P. Ferguson
g.ferguson{at}abdn.ac.uk

Sinorhizobium meliloti is a beneficial legume symbiont, closely related to Brucella species, which are chronic mammalian pathogens. We discovered that the S. meliloti MsbA2 protein is essential to ensure the symbiotic interaction with the host plant, alfalfa. S. meliloti invades plant cells via plant-derived structures known as infection threads. However, in the absence of MsbA2, S. meliloti remains trapped within abnormally thickened infection threads and induces a heightened plant defence response, characterized by a substantial thickening of the nodule endodermis layer and the accumulation of polyphenolic compounds. The S. meliloti MsbA2 protein is homologous to the Escherichia coli lipopolysaccharide/phospholipid trafficking protein MsbA. However, MsbA2 was not essential for the membrane transport of either lipopolysaccharide or phospholipids in S. meliloti. We determined that the msbA2 gene is transcribed in free-living S. meliloti and that in the absence of MsbA2 the polysaccharide content of S. meliloti is altered. Consequently, we propose a model whereby the altered polysaccharide content of the S. meliloti msbA2 mutant could be responsible for its symbiotic defect by inducing an inappropriate host response.


Abbreviations: DOC, deoxycholate; EPS, exopolysaccharide; GUS, β-glucuronidase; TEM, transmission electron microscopy; VLCFA, very-long-chain fatty acid

{dagger}These authors contributed equally to this work.







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