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Characterization of novel endo-β-N-acetylglucosaminidases from Sphingobacterium species, Beauveria bassiana and Cordyceps militaris that specifically hydrolyze fucose-containing oligosaccharides and human IgG
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Characterization of novel endo-β-N-acetylglucosaminidases from Sphingobacterium species, Beauveria bassiana and Cordyceps militaris that specifically hydrolyze fucose-containing oligosaccharides and human IgG
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Characterization of novel endo-β-N-acetylglucosaminidases from Sphingobacterium species, Beauveria bassiana and Cordyceps militaris that specifically hydrolyze fucose-containing oligosaccharides and human IgG
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Journal Article
Characterization of novel endo-β-N-acetylglucosaminidases from Sphingobacterium species, Beauveria bassiana and Cordyceps militaris that specifically hydrolyze fucose-containing oligosaccharides and human IgG
2018
Overview
Endo-β-
N
-acetylglucosaminidase (ENGase) catalyzes hydrolysis of
N
-linked oligosaccharides. Although many ENGases have been characterized from various organisms, so far no fucose-containing oligosaccharides-specific ENGase has been identified in any organism. Here, we screened soil samples, using dansyl chloride (Dns)-labeled sialylglycan (Dns-SG) as a substrate, and discovered a strain that exhibits ENGase activity in the culture supernatant; this strain, named here as strain HMA12, was identified as a
Sphingobacterium
species by 16S ribosomal RNA gene analysis. By draft genome sequencing, five candidate ENGase encoding genes were identified in the genome of this strain. Among them, a recombinant protein purified from
Escherichia coli
expressing the candidate gene ORF1188 exhibited fucose-containing oligosaccharides-specific ENGase activity. The ENGase exhibited optimum activities at very acidic pHs (between pH 2.3–2.5). A BLAST search using the sequence of ORF1188 identified two fungal homologs, one in
Beauveria bassiana
and the other in
Cordyceps militaris
. Recombinant ORF1188,
Beauveria
and
Cordyceps
ENGases released the fucose-containing oligosaccharides residues from rituximab (immunoglobulin G) but not the high-mannose-containing oligosaccharides residues from RNase B, a result that not only confirmed the substrate specificity of these novel ENGases but also suggested that natural glycoproteins could be their substrates.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 82
/ 82/29
/ 82/58
/ 82/80
/ 82/83
/ E coli
/ Fucose
/ Genomes
/ Humanities and Social Sciences
/ Humans
/ Immunoglobulin G - metabolism
/ Mannose
/ Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - chemistry
/ Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - genetics
/ Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - metabolism
/ Oligosaccharides - chemistry
/ Oligosaccharides - metabolism
/ rRNA 16S
/ Science
/ Sphingobacterium - classification
