NDLI: Characterization of N-linked oligosaccharides in chorion peroxidase of Aedes aegypti mosquito.

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Characterization of N-linked oligosaccharides in chorion peroxidase of Aedes aegypti mosquito.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Li, Jianyong Li, Junsuo S.
Description	Country affiliation: United States Author Affiliation: Li JS ( Department of Pathobiology, University of Illinois, 2001 South Lincoln Avenue, Urbana, IL 61802, USA.)
Abstract	A peroxidase is present in the chorion of Aedes aegypti eggs and catalyzes chorion protein cross-linking during chorion hardening, which is critical for egg survival in the environment. The unique chorion peroxidase (CPO) is a glycoprotein. This study deals with the N-glycosylation site, structures, and profile of CPO-associated oligosaccharides using mass spectrometric techniques and enzymatic digestion. CPO was isolated from chorion by solubilization and several chromatographic methods. Mono-saccharide composition was analyzed by HPLC with fluorescent detection. Our data revealed that carbohydrate (D-mannose, N-acetyl D-glucosamine, D-arabinose, N-acetyl D-galactosamine, and L-fucose) accounted for 2.24% of the CPO molecular weight. A single N-glycosylation site (Asn328-Cys- Thr) was identified by tryptic peptide mapping and de novo sequencing of native and PNGase A-deglycosylated CPO using matrix-assisted laser/desorption/ionization time-of-flight mass spectrometry (MALDI/TOF/MS) and liquid chromatography/tandem mass spectrometry (LC/MS/MS). The Asn328 was proven to be a major fully glycosylated site. Potential tryptic glycopeptides and profile were first assessed by MALDI/TOF/MS and then by precursor ion scanning during LC/MS/MS. The structures of N-linked oligosaccharides were elucidated from the MS/MS spectra of glycopeptides and exoglycosidase sequencing of PNGase A-released oligosaccharides. These CPO-associated oligosaccharides had dominant Man3GlcNAc2 and Man3 (Fuc) GlcNAc2 and high mannose-type structures (Man(4-8)GlcNAc2). The truncated structures, Man2GlcNAc2 and Man2 (Fuc) GlcNAc2, were also identified. Comparison of CPO activity and Stokes radius between native and deglycosylated CPO suggests that the N-linked oligosaccharides influence the enzyme activity by stabilizing its folded state.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	9
Volume Number	14
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2005-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Aedes Enzymology Chorion Oligosaccharides Chemistry Peroxidase Metabolism Amino Acid Sequence Animals Carbohydrate Conformation Carbohydrate Sequence Glycosylation Mass Spectrometry Molecular Sequence Data Monosaccharides Isolation & Purification Polysaccharides Research Support, N.i.h., Extramural Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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