Publications by authors named "Julie Beneteau"

Chitosans, β-1,4-linked partially N-acetylated linear polyglucosamines, are very versatile and promising functional biopolymers. Understanding their structure-function relationships requires sensitive and accurate structural analyses to determine parameters like degree of polymerization (DP), fraction of acetylation (F), or pattern of acetylation (P). NMR, the gold standard for F analysis, requires large amounts of sample.

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The biological activities of partially acetylated chitosan oligosaccharides (paCOS) depend on their degree of polymerization (DP), fraction of acetylation (F), and potentially their pattern of acetylation (P). Therefore, analyzing structure-function relationships require fully defined paCOS, but these are currently unavailable. A promising approach for obtaining at least partially defined paCOS is using chitosanolytic enzymes.

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Article Synopsis
  • The molecular interactions between gut bacteria and humans, particularly with the bacterium Bacteroides thetaiotaomicron, are not well understood despite their physiological relevance.
  • Recent research highlights the role of sulfatases in helping this bacterium adapt to and flourish in the human gut by metabolizing complex sugars known as glycosaminoglycans (GAGs).
  • This study identifies and characterizes four specific GAG sulfatases for the first time, revealing that B. thetaiotaomicron possesses a unique endosulfatase that operates on these complex sugars at a polymer level, indicating a more intricate bacterial capability in processing host glycans than previously thought.
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Phloem sieve elements are highly differentiated cells involved in the long-distance transport of photoassimilates. These cells contain both aggregated phloem-proteins (P-proteins) and soluble proteins, which are also translocated by mass flow. We used liquid chromatography-tandem mass spectrometry (LC-MS/MS) to carry out a proteomic survey of the phloem exudate of Arabidopsis thaliana, collected by the ethylenediaminetetraacetic acid (EDTA)-facilitated method.

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Phloem Protein2 (PP2) is a component of the phloem protein bodies found in sieve elements. We describe here the lectin properties of the Arabidopsis (Arabidopsis thaliana) PP2-A1. Using a recombinant protein produced in Escherichia coli, we demonstrated binding to N-acetylglucosamine oligomers.

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Phloem is the major route for transport of carbohydrates, amino acids, and other nutrients from source to sink tissues. Hormones, mRNAs, small RNAs and proteins also are transported by the phloem, and potentially play pivotal roles in communication between organs to coordinate plant development and physiology. A comprehensive understanding of the mechanisms involved in phloem transport and signalling is still lacking.

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