Intracellular processing, glycosylation, and cell surface expression of human metapneumovirus attachment glycoprotein.

Intracellular processing, glycosylation, and cell surface expression of human metapneumovirus attachment glycoprotein. Research Abstract Details 

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Intracellular processing, glycosylation, and cell surface expression of human metapneumovirus attachment glycoprotein. Abstract Text:

Li Liu,Nathalie Bastien,Yan Li,Li Liu,Nathalie Bastien,Yan Li,

The biosynthesis and posttranslational processing of human metapneumovirus attachment G glycoprotein were investigated. After pulse-labeling, the G protein accumulated as three species with molecular weights of 45,000, 50,000, and 53,000 (45K, 50K, and 53K, respectively). N-Glycosidase digestion indicated that these forms represent the unglycosylated precursor and N-glycosylated intermediate products, respectively. After an appropriate chase, these three naive forms were further processed to a mature 97K form. The presence of O-linked sugars in mature G protein was confirmed by O-glycanase digestion and lectin-binding assay using Arachis hypogaea (peanut agglutinin), an O-glycan-specific lectin. In addition, in the O-glycosylation-deficient cell line (CHO ldlD cell), the G protein could not be processed to the mature form unless the exogenous Gal and GalNAc were supplemented, which provided added evidence supporting the O-linked glycosylation of G protein. The maturation of G was completely blocked by monensin but was partially sensitive to brefeldin A (BFA), suggesting the O-linked glycosylation of G initiated in the trans-Golgi compartment and terminated in the trans-Golgi network. Enzymatic deglycosylation analysis confirmed that the BFA-G was a partial mature form containing N-linked oligosaccharides and various amounts of O-linked carbohydrate side chains. The expression of G protein at the cell surface could be detected by indirect immunofluorescence staining assay. Furthermore, cell surface immunoprecipitation displayed an efficient intracellular transport of G protein.

Intracellular processing, glycosylation, and cell surface expression of human metapneumovirus attachment glycoprotein. Publishing Authors By Initials

L Liu,N Bastien,Y Li,L Liu,N Bastien,Y Li,

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Intracellular processing, glycosylation, and cell surface expression of human metapneumovirus attachment glycoprotein. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of virology

VOLUME: 81

Page Numbers: 13435-43

Journal Abbreviation: J. Virol.

ISSN: 1098-5514

DAY: 3

MONTH: 10

YEAR: 2007

Intracellular processing, glycosylation, and cell surface expression of human metapneumovirus attachment glycoprotein. Information

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LANGUAGE: eng

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Grant and Affiliation Information for Intracellular processing, glycosylation, and cell surface expression of human metapneumovirus attachment glycoprotein.

AFFILIATION: Department of Medical Microbiology and Infectious Diseases, the University of Manitoba, Winnipeg, Manitoba, Canada.

Country: United States

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MEDLINETA: J Virol

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