FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2175031806> ?p ?o ?g. }

• W2175031806 abstract "Some oomycetes species are severe pathogens of fish or crops. As such, they are responsible for important losses in the aquaculture industry as well as in agriculture. Saprolegnia parasitica is a major concern in aquaculture as there is currently no method available for controlling the diseases caused by this microorganism. The cell wall is an extracellular matrix composed essentially of polysaccharides, whose integrity is required for oomycete viability. Thus, the enzymes involved in the biosynthesis of cell wall components, such as cellulose and chitin synthases, represent ideal targets for disease control. However, the biochemical properties of these enzymes are poorly understood, which limits our capacity to develop specific inhibitors that can be used for blocking the growth of pathogenic oomycetes.In our work, we have used Saprolegnia monoica as a model species for oomycetes to characterize two types of domains that occur specifically in oomycete carbohydrate synthases: the Pleckstrin Homology (PH) domain of a cellulose synthase and the so-called ‘Microtubule Interacting and Trafficking’ (MIT) domain of chitin synthases. In addition, the chitin synthase activity of the oomycete phytopathogen Aphanomyces euteiches was characterized in vitro using biochemical approaches.The results from our in vitro investigations revealed that the PH domain of the oomycete cellulose synthase binds to phosphoinositides, microtubules and F-actin. In addition, cell biology approaches were used to demonstrate that the PH domain co-localize with F-actin in vivo. The structure of the MIT domain of chitin synthase (CHS) 1 was solved by NMR. In vitro binding assays performed on recombinant MIT domains from CHS 1 and CHS 2 demonstrated that both proteins strongly interact with phosphatidic acid in vitro. These results were further supported by in silico data where biomimetic membranes composed of different phospholipids were designed for interaction studies. The use of a yeast-two-hybrid approach suggested that the MIT domain of CHS 2 interacts with the delta subunit of Adaptor Protein 3, which is involved in protein trafficking. These data support a role of the MIT domains in the cellular targeting of CHS proteins. Our biochemical data on the characterization of the chitin synthase activity of A. euteiches suggest the existence of two distinct enzymes responsible for the formation of water soluble and insoluble chitosaccharides, which is consistent with the existence of two putative CHS genes in the genome of this species.Altogether our data support a role of the PH domain of cellulose synthase and MIT domains of CHS in membrane trafficking and cellular location." @default.
• W2175031806 created "2016-06-24" @default.
• W2175031806 creator A5060235730 @default.
• W2175031806 creator A5062275510 @default.
• W2175031806 creator A5069007800 @default.
• W2175031806 creator A5088210859 @default.
• W2175031806 date "2015-01-01" @default.
• W2175031806 modified "2023-09-27" @default.
• W2175031806 title "The phytopathogenic oomycete Aphanomyces euteiches contains two distinct N-acetylglucosaminyltransferase activities that form chitin-like saccharides in vitro" @default.
• W2175031806 hasPublicationYear "2015" @default.
• W2175031806 type Work @default.
• W2175031806 sameAs 2175031806 @default.
• W2175031806 citedByCount "0" @default.
• W2175031806 crossrefType "journal-article" @default.
• W2175031806 hasAuthorship W2175031806A5060235730 @default.
• W2175031806 hasAuthorship W2175031806A5062275510 @default.
• W2175031806 hasAuthorship W2175031806A5069007800 @default.
• W2175031806 hasAuthorship W2175031806A5088210859 @default.
• W2175031806 hasConcept C104317684 @default.
• W2175031806 hasConcept C124743340 @default.
• W2175031806 hasConcept C125235067 @default.
• W2175031806 hasConcept C181199279 @default.
• W2175031806 hasConcept C22802001 @default.
• W2175031806 hasConcept C2777537739 @default.
• W2175031806 hasConcept C2779732960 @default.
• W2175031806 hasConcept C2780992308 @default.
• W2175031806 hasConcept C2781088250 @default.
• W2175031806 hasConcept C55493867 @default.
• W2175031806 hasConcept C59822182 @default.
• W2175031806 hasConcept C86803240 @default.
• W2175031806 hasConcept C89423630 @default.
• W2175031806 hasConcept C95444343 @default.
• W2175031806 hasConceptScore W2175031806C104317684 @default.
• W2175031806 hasConceptScore W2175031806C124743340 @default.
• W2175031806 hasConceptScore W2175031806C125235067 @default.
• W2175031806 hasConceptScore W2175031806C181199279 @default.
• W2175031806 hasConceptScore W2175031806C22802001 @default.
• W2175031806 hasConceptScore W2175031806C2777537739 @default.
• W2175031806 hasConceptScore W2175031806C2779732960 @default.
• W2175031806 hasConceptScore W2175031806C2780992308 @default.
• W2175031806 hasConceptScore W2175031806C2781088250 @default.
• W2175031806 hasConceptScore W2175031806C55493867 @default.
• W2175031806 hasConceptScore W2175031806C59822182 @default.
• W2175031806 hasConceptScore W2175031806C86803240 @default.
• W2175031806 hasConceptScore W2175031806C89423630 @default.
• W2175031806 hasConceptScore W2175031806C95444343 @default.
• W2175031806 hasLocation W21750318061 @default.
• W2175031806 hasOpenAccess W2175031806 @default.
• W2175031806 hasPrimaryLocation W21750318061 @default.
• W2175031806 hasRelatedWork W132587321 @default.
• W2175031806 hasRelatedWork W156656317 @default.
• W2175031806 hasRelatedWork W1976024911 @default.
• W2175031806 hasRelatedWork W2008794157 @default.
• W2175031806 hasRelatedWork W2020648116 @default.
• W2175031806 hasRelatedWork W2022732661 @default.
• W2175031806 hasRelatedWork W2025248900 @default.
• W2175031806 hasRelatedWork W2033274933 @default.
• W2175031806 hasRelatedWork W2038100335 @default.
• W2175031806 hasRelatedWork W2058320449 @default.
• W2175031806 hasRelatedWork W2084102313 @default.
• W2175031806 hasRelatedWork W2098320231 @default.
• W2175031806 hasRelatedWork W2123683450 @default.
• W2175031806 hasRelatedWork W2148409103 @default.
• W2175031806 hasRelatedWork W2165811315 @default.
• W2175031806 hasRelatedWork W2601590724 @default.
• W2175031806 hasRelatedWork W2807237104 @default.
• W2175031806 hasRelatedWork W3013159127 @default.
• W2175031806 hasRelatedWork W340375137 @default.
• W2175031806 hasRelatedWork W2965182897 @default.
• W2175031806 isParatext "false" @default.
• W2175031806 isRetracted "false" @default.
• W2175031806 magId "2175031806" @default.
• W2175031806 workType "article" @default.