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The plot involved a female soldier involved in a war in deep space against a formidable alien species. The woman has a space suit that is like a symbiotic partner that helps her survive in hard vacuum, it uses photosynthesis to feed her and the story presents the protagonist as almost being an alien herself. The suit had the ability to change shape which helped her fight in space and I vaguely recall that the feet turned into almost alpine ski-like appendages.



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MST assays reveal the EPR3a ectodomain binds the repeating EPS octasaccharide unit from symbiotically compatible and incompatible rhizobia. The EPR3a ectodomain bind the EPS from (A)M. loti and (B)R. leguminosarum with affinities similar to that of EPR3, as previously reported [22]. EPR3a, however, was observed to bind (C)S. meliloti EPS with at least 2-fold lower affinity compared to EPR3 [22]. (D) No binding was observed for the negative control Maltodextrin. See S1 Data for underlying data. EPS, exopolysaccharide; MST, microscale thermophoresis.


Epr3a expression remains low in root tissues throughout the rhizobial infection process, yet IT and nodulation are impaired in epr3a mutant alleles. In contrast, EPR3 is strongly induced by compatible rhizobia, initially in epidermal cells and later within cortical and nodule primordia cells associated with the infecting rhizobia. This expression pattern matches the symbiotic phenotypes of epr3 mutants, reduced IT formation, and impaired colonisation of nodule primordia [19,21]. However, the reduction in IT formation is more pronounced in epr3a than epr3 mutants. The alleviated symbiotic impairment following inoculation with M. loti exoU is comparable in epr3 and epr3a single mutants with no significant enhancement of this in the double mutant. This indicates that although both EPR3 and EPR3a participate in the perception of truncated EPS, they are not exclusively responsible for the symbiotic impairment resulting from the production of incompatible EPS. Our interpretation of these results is that EPR3a, even expressed at low levels, is important for modulating rhizobial infection, potentially through stabilising receptor complex signalling.


Ligand-binding assays support the involvement of EPR3a in monitoring rhizobial EPS during infection, with the EPR3a ectodomain having binding affinities for rhizobial EPS comparable to those reported for the EPR3 ectodomain [22]. The similar binding affinities for EPS ligands isolated from symbiotically compatible M. loti R7A and incompatible S. meliloti and R. leguminosarum suggests that perception of EPS by EPR-type receptors acts in surveillance, rather than specifically recognising compatible symbionts.


Interestingly, the epr3a epr3 double mutant appears less affected than the respective single mutant alleles in symbiotic events with M. loti R7A. This suggests that the downstream signalling from these receptors is altered in the presence/absence of one and other. LysM-RLKs are known to form receptor complexes to mediate signalling activity [48,49]. Whether or not EPR3 and EPR3a function as a receptor complex remains to be resolved. Our analysis of EPR3 and EPR3a intracellular kinase domains reveals that both are catalytic active kinases, which may be of importance when considering the possibility that EPR3 and EPR3a form individual receptor complexes with as-yet unknown co-receptors. Identified LysM-RLK co-receptor pairings generally consist of one catalytically active kinase paired with an inactive kinase, e.g., NFR1 and NFR5 [49,50] or LYK3 and NFP [51].


(A) Principal component analysis of RNA-seq data obtained from roots of wild-type and mutant plants inoculated with M. loti R7A. RNA-seq was performed on root samples harvested 3 and 7 dpi. (B) Expression of known symbiotic genes was comparable in wild-type and receptor mutant plants. (C) qRT-PCR analysis showed the NIN expression profile was comparable in wild-type and receptor mutant plants. (D) The 25 Lotus genes that show the highest transcriptional response to pathogenic Ralstonia were chosen to represent defence-related genes. No significant difference in the expression of the genes was identified between wild-type and mutant plants. See S2 and S3 Information, NCBI BioProject accession: PRJNA953045 for underlying data.


Thank you for submitting your manuscript entitled "A Lotus japonicus glycan receptor kinase facilitates intracellular accommodation of arbuscular mycorrhiza and symbiotic rhizobia." for consideration as a Research Article by PLOS Biology.






However, before we can send your manuscript to reviewers, we need you to complete your submission by providing the metadata that is required for full assessment. To this end, please login to Editorial Manager where you will find the paper in the 'Submissions Needing Revisions' folder on your homepage. Please click 'Revise Submission' from the Action Links and complete all additional questions in the submission questionnaire.


Thank you for your patience while your manuscript "A Lotus japonicus glycan receptor kinase facilitates intracellular accommodation of arbuscular mycorrhiza and symbiotic rhizobia." was peer-reviewed at PLOS Biology. Your manuscript has been evaluated by the PLOS Biology editors, an Academic Editor with relevant expertise, and by several independent reviewers.


Reviewer #1: In the manuscript entitled "A Lotus japonicus glycan receptor kinase facilitates intracellular accommodation of arbuscular mycorrhiza and symbiotic rhizobia" Kelly et al. identified a novel LysM-RLK protein EPR3a from L. japonicus. They performed biochemical, molecular, and functional characterization of EPR3a in arbuscular and legume-rhizobia symbioses. In this manuscript, the authors investigated the binding of EPR3a to branched glycans and the perception of rhizobial exopolysaccharide, which is one of the determinants of the specificity of plant-microbe interaction. The authors used LORE1 mutant lines of EPR3a for functional characterization of this protein in arbuscular mycorrhiza association. Finally, the authors used kinase assays to validate in vitro kinase activity of EPR3 and EPR3a. In my opinion, this manuscript suffers from significant flaws.


* The authors performed binding assays between EPR3a ectodomain and glycans obtained from algae (E. bicyclis and L. digitata)... and a fungus irrelevant to the biology of L. japonicus. Since they try to make a case for the role of EPR3a protein in AM symbiosis, the authors should have used fungal extracts from AM fungi and possibly pathogenic fungi relevant to L. japonicus. Using biologically relevant fungal cell wall extracts, the authors would have addressed whether the EPR3a activity is conserved across fungi, involving symbiotic and pathogenic interactions and whether symbiotic or pathogenic interaction dominates in virtue of EPR3a activity.


* EPR3a binds with a stronger affinity to S. indica decasaccharide (Kd:51.2 μM) compared to E. bicyclis glycan (Kd:247.7 μM), which again indicates that more assays are required to determine the binding affinity of EPR3a with pathogenic or symbiotic signals.


Thank you for your patience while we considered your revised manuscript "A Lotus japonicus glycan receptor kinase facilitates intracellular accommodation of arbuscular mycorrhiza and symbiotic rhizobia." for publication as a Research Article at PLOS Biology. This revised version of your manuscript has been evaluated by the PLOS Biology editors, the Academic Editor and one of the original reviewers.


2. We suggest a change in the title to include that Lotus japonicus is a legume: "A glycan receptor kinase facilitates intracellular accommodation of arbuscular mycorrhiza and symbiotic rhizobia in the legume Lotus japonicus".


Thank you for the submission of your revised Research Article "A glycan receptor kinase facilitates intracellular accommodation of arbuscular mycorrhiza and symbiotic rhizobia in the legume Lotus japonicus" for publication in PLOS Biology. On behalf of my colleagues and the Academic Editor, Cara Haney, I am pleased to say that we can in principle accept your manuscript for publication, provided you address any remaining formatting and reporting issues. These will be detailed in an email you should receive within 2-3 business days from our colleagues in the journal operations team; no action is required from you until then. Please note that we will not be able to formally accept your manuscript and schedule it for publication until you have completed any requested changes.


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