The Sinorhizobium meliloti MsbA2 protein is essential for the legume symbiosis.
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.
Beck
Sebastian
S
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.
Marlow
Victoria L
VL
School of Medicine, Department of Medicine and Therapeutics, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, UK.|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.
Woodall
Katy
K
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.
Doerrler
William T
WT
Department of Biological Sciences, Louisiana State University, 202 Life Sciences Building, Baton Rouge, LA 70803, USA.
James
Euan K
EK
College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.
Ferguson
Gail P
GP
School of Medicine, Department of Medicine and Therapeutics, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, UK.|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.
D018528:ATP-Binding Cassette Transporters; D001426:Bacterial Proteins; D005656:Fungal Proteins / Q000235:genetics / Q000502:physiology*; D005798:Genes, Bacterial; D020043:Genes, Essential; D008070:Lipopolysaccharides / Q000378:metabolism; D000455:Medicago sativa / Q000166:cytology / Q000382:microbiology* / Q000648:ultrastructure; D008853:Microscopy; D046529:Microscopy, Electron, Transmission; D010743:Phospholipids / Q000378:metabolism; D010802:Phylogeny; D011134:Polysaccharides / Q000032:analysis; D017386:Sequence Homology, Amino Acid; D016962:Sinorhizobium meliloti / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D013559:Symbiosis
D018528:ATP-Binding Cassette Transporters; D001426:Bacterial Proteins; D005656:Fungal Proteins; D008070:Lipopolysaccharides; C079726:MsbA protein, Bacteria; D010743:Phospholipids; D011134:Polysaccharides