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Grasspeas are environmentally successful and robust legumes with major traits of interest for food and nutrition security. It is a critical crop in areas prone to drought, overmoisture stress, and famine, hence, regarded as an "insurance crop" because of its inherent resilience of climatic calamities. The current status and prospects of grasspea, as well as various breeding and food processing approaches to improve this crop for integration in diverse and sustainable agrifood systems, are discussed in this review. Grasspeas are often the source of important micronutrients and proteins (18%–34%), saving peoples' lives during famine. Grasspea consumption is increasing in some countries; however, uninterrupted consumption of grasspea should be avoided, especially when they are green or unripe and when they are raw. Effective food processing techniques are essential to reduce the neurotoxic hazards associated with eating grasspea. Several effective processing steps can be used to reduce toxicity in addition to the development of toxin‐free varieties for production and consumption. With advances in the scientific investigation of the grasspea, integration of genetics, processing, and behavioral components has been suggested. [ABSTRACT FROM AUTHOR]

The biological oxidation of ammonia (i.e. nitrification), results in the transformation of relatively immobile NH4+ into a highly mobile NO3-, which is vulnerable to losses through leaching and denitrification, resulting in low nitrogen-use efficiency in agricultural systems. The ability of certain plants to suppress soil nitrifier function by releasing inhibitors from roots is termed 'biological nitrification inhibition' (BNI). Using a recombinant luminescent Nitrosomonas europaea, we developed an assay to detect and quantify the inhibitory effects in plant soil systems termed, 'BNI activity', expressed in ATU (allylthiourea unit). Sorghum roots released (into water-based medium, hereafter referred to as root exudates) substantial amount of BNI activity. The BNI capacity (ATU g-1 root dry wt d-1) of roots changed with growth stage, from 60 ATU at 3 week old to 20 ATU at 45 day stage. In addition, sorghum roots released hydrophobic compounds, which can be recovered by washing with dichloromethane (hereafter referred to as DCM-root wash). One of the active constituents with BNI activity in root exudates, isolated by activity-guided HPLC fractionation, was a flavonoid, identified as sakuranetin. Using a similar approach, the major active constituent with BNI activity in DCM-root wash was isolated and identified as sorgoleone. Both sakuranetin and sorgoleone inhibited Nitrosomonas activity in a dose-response manner. Substantial genetic variability for sorgoleone production capacity was detected in sorghum. Some wild-sorghum species showed high-BNI capacity under field conditions. Potential implications of BNI in inhibiting nitrification and in reducing the nitrogen footprint from agricultural systems will be discussed.

Flagellar motility and its glycosylation are indispensable for the virulence of Pseudomonas syringae pv. tabaci 6605. Six serine residues of the flagellin protein at positions 143, 164, 176, 183, 193 and 201 are glycosylated, and the glycan structure at 201 was determined to consist of a trisaccharide of two L-rhamnosyl residues and a modified 4-amino-4,6-dideoxyglucosyl (viosamine) residue. To investigate the glycan structures attached to the other serine residues and to identify the glycans important for virulence, Ser/Ala-substituted mutants were generated. Six mutant strains that each retained a single glycosylated serine residue were generated by replacing five of the six serine residues with alanine residues. MALDI-TOF mass analysis of flagellin proteins revealed that the major component of each glycan was a trisaccharide basically similar to that at position 201, but with heterogeneity in glycoform distribution. Swarming motility and amounts of acylhomoserine lactones (AHLs) as quorum-sensing signal molecules were significantly reduced, especially in the S143-5S/A, S164-5S/A and S201-5S/A mutants, whereas tolerance to antibiotics was increased in these three mutants. All the mutants showed lower ability to cause disease on host tobacco plants. These results supported our previous finding that glycosylation of the most externally located sites on the surface of the flagellin molecule, such as S176 and S183, is required for virulence in P. syringae pv. tabaci 6605. Furthermore, it is speculated that flagellum-dependent motility might be correlated with quorum sensing and antibiotic resistance. DOI 10.1099/mic.0.030700-0

Flagellins from Pseudomonas syringae pv. glycinea race 4 and Pseudomonas syringae pv. tabaci 6605 have been found to be glycosylated. Glycosylation of flagellin is essential for bacterial virulence and is also involved in the determination of host specificity. Flagellin glycans from both pathovars were characterized, and common sites of glycosylation were identified on six serine residues (positions 143, 164, 176, 183, 193, and 201). The structure of the glycan at serine 201 (S201) of flagellin from each pathovar was determined by sugar composition analysis, mass spectrometry, and [sup.1]H and [sup.13]C nuclear magnetic resonance spectroscopy. These analyses showed that the S201 glycans from both pathovars were composed of a common unique trisaccharide consisting of two rhamnosyl (Rha) residues and one modified 4-amino-4,6-dideoxyglucosyl (Qui4N) residue, [beta]-n-Quip4N(3hydroxy-1-oxobutyl)2Me-(1 [right arrow] 3)-[alpha]-L-Rhap-(1 [right arrow] 2)-[alpha]-L-Rhap. Furthermore, mass analysis suggests that the glycans on each of the six serine residues are composed of similar trisaccharide units. Determination of the enantiomeric ratio of Rha from the flagellin proteins showed that flagellin from P. syringae pv. tabaci 6605 consisted solely of L-Rha, whereas P. syringae pv. glycinea race 4 flagellin contained both L-Rha and D-Rha at a molar ratio of about 4:1. Taking these findings together with those from our previous study, we conclude that these flagellin glycan structures may be important for the virulence and host specificity of P. syringae.