Taxonomic group: fungi /
Organ / tissue: cell wall
NCBI PubMed ID: 26688467Publication DOI: 10.1016/j.fgb.2015.12.004Journal NLM ID: 9607601Publisher: Orlando, FL : Academic Press / Elsevier
Correspondence: azuccaro
uni-koeln.de
Institutions: Botanical Institute, Cluster of Excellence on Plant Sciences (CEPLAS), University of Cologne, Cologne, Germany
Plant innate immunity relies in first place on the detection of invading microbes. Thus, plants evolved receptors to sense unique molecules of the microbe, the so called microbe-associated molecular patterns or MAMPs. The best studied fungal MAMP is chitin, an important structural building block of the fungal cell wall. Over the past years several plant receptors for chitin have been characterized as well as different strategies adopted by fungi to evade chitin recognition. Despite its strong activity as an elicitor of plant defense chitin represents only a small percentage of the cell wall of most fungi compared to other complex sugars. β-glucan, the most abundant fungal cell wall polysaccharide, also serves as a MAMP, but the mechanisms of β-glucan perception and signaling in plants are largely unknown. In contrast to that the β-glucan recognition and signaling machineries are well characterized in mammals. The C-type lectin receptor Dectin-1 is a key component of these machineries. In this review we describe valuable knowledge about the existence of at least one β-glucan receptor in plants and about the hindrances in β-glucan research. Additionally we discuss possible future perspectives of glucan research and the possibility to transfer the gathered knowledge from mammalian systems to plants.
β-glucan, chitin, Dectin-1, fungal MAMPs, pattern recognition receptor, plant immune system
Structure type: structural motif or average structure ; n=1500
Location inside paper: p. 53, column 2, paragraph 2
Trivial name: chitin
Compound class: cell wall polysaccharide, glucan
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_153212,IEDB_241099,IEDB_423114,IEDB_423150,SB_74,SB_85
Biological activity: binds to LYK1, LYK3, LYK4, LYK5. Takes the role of MAMP in plants
Enzymes that release or process the structure: chitin synthase
Biosynthesis and genetic data: biochemical data
Related record ID(s): 42400, 42401, 42402, 49501, 49523, 49564, 49568, 50015
NCBI Taxonomy refs (TaxIDs): 4751Reference(s) to other database(s): GTC:G97099AY
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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