Affinity Entrapment of Oligosaccharides and Glycopeptides Using Free Lectin Solution

Yodoshi, Masahiro; Oyama, Takehiro; Masaki, Ken; Kakehi, Kazuaki; Hayakawa, Tetsuo; Suzuki, Shigeo

doi:10.2116/analsci.27.395

Cited by 13 publications

(9 citation statements)

References 22 publications

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“…WGA reacts strongly with the chitobiose core of bisected hybrid-type N-glycans, specifically with the oligosaccharide GlcNAcβ1-4Manβ1-4GlcNAcβ1-4GlcNAc (Yamamoto et al, 1981, Yodoshi et al, 2011), which was proposed in the candidate glycan structure of peak 10 (Fig. 2B, m/z 1306.91).…”

Section: Resultsmentioning

confidence: 95%

N-glycosylation profiling of porcine reproductive and respiratory syndrome virus envelope glycoprotein 5

Tao

Orlando

et al. 2015

Virology

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Porcine reproductive and respiratory syndrome virus (PRRSV) is a positive-sense ssRNA virus whose envelope contains four glycoproteins and three nonglycosylated proteins. Glycans of major envelope glycoprotein 5 (GP5) are proposed as important for virus assembly and entry into permissive cells. Structural characterization of GP5 glycans would facilitate the mechanistic understanding of these processes. Thus, we purified the PRRSV type 2 prototype strain, VR2332, and analyzed the virion-associated glycans by both biochemical and mass spectrometric methods. Endoglycosidase digestion showed that GP5 was the primary protein substrate, and that the carbohydrate moieties were primarily complex-type N-glycans. Mass spectrometric analysis (HPLC-ESI-MS/MS) of GP5 N-glycans revealed an abundance of N-acetylglucosamine (GlcNAc) and N-acetyllactosamine (LacNAc) oligomers in addition to sialic acids. GlcNAc and LacNAc accessibility to ligands was confirmed by lectin co-precipitation. Our findings help to explain PRRSV infection of cells lacking sialoadhesin and provide a glycan database to facilitate molecular structural studies of PRRSV.

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Section: Resultsmentioning

confidence: 95%

N-glycosylation profiling of porcine reproductive and respiratory syndrome virus envelope glycoprotein 5

Tao

Orlando

et al. 2015

Virology

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show abstract

“…Strategies for lectin-immobilization, including covalent and non-covalent binding techniques, as well as its applications in LAC, serial LAC, multi-LAC and affinity electrophoresis have been reviewed [43]. Interestingly, there is also the possibility of glycoconjugate enrichment by using free lectin solutions, where lectins are not immobilized on a support but put in contact with the sample in aqueous medium, and the complex further separated through precipitation or filtration [44].…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Cancer serum biomarkers based on aberrant post-translational modifications of glycoproteins: Clinical value and discovery strategies

Silva

2015

Biochimica et Biophysica Acta (BBA) - Reviews on Cancer

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“…Yodoshi et al reported the specific entrapment of oligosaccharides and glycopeptides as lectin complexes using ultramembrane filters. 69 Lectin affinity columns have been applied to determine cancer-related glycans in human plasma. 70,71 Lectin-immobilized nanoparticles have been used to entrap glycoproteins in human body fluids.…”

Section: Specific Entrapment Of Glycansmentioning

confidence: 99%

Affinity Entrapment of Oligosaccharides and Glycopeptides Using Free Lectin Solution

Cited by 13 publications

References 22 publications

N-glycosylation profiling of porcine reproductive and respiratory syndrome virus envelope glycoprotein 5

N-glycosylation profiling of porcine reproductive and respiratory syndrome virus envelope glycoprotein 5

Cancer serum biomarkers based on aberrant post-translational modifications of glycoproteins: Clinical value and discovery strategies

Recent Developments in Liquid Chromatography and Capillary Electrophoresis for the Analysis of Glycoprotein Glycans

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