Linked Life Data

2001369

Source:http://linkedlifedata.com/resource/pubmed/id/2001369

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1991-4-18
pubmed:abstractText
Infection of T-lymphocytes and macrophages by human immunodeficiency virus (HIV) is mediated by the binding of the HIV envelope glycoprotein to the cell-surface receptor glycoprotein CD4. A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS). In the present study, the structures of the Asn-linked oligosaccharides of soluble rCD4 have been elucidated. The rCD4 molecule has two potential sites for N-glycosylation, Asn-271 and Asn-300. Tryptic glycopeptides containing either of the sites were purified by reversed-phase HPLC, and their oligosaccharides were released enzymatically. The structures of the oligosaccharides were determined by methylation analysis, high-pH anion-exchange chromatography, fast-atom bombardment mass spectrometry, and 1H NMR spectroscopy at 500 MHz. Asn-271 was found to carry diantennary N-acetyllactosamine-type ("complex") oligosaccharides, of which 8% were asialo, 55% were monosialyl, and 37% were disialyl. Approximately 18% of these structures contained fucose alpha(1-->6) linked to the reducing GlcNAc residue. Two different hybrid structures were found to account for 34% of the oligosaccharides attached to Asn-300. The remainder of the oligosaccharides attached to Asn-300 were diantennary N-acetyllactosamine-type, of which 10% were asialo, 61% were monosialyl, and 29% were disialyl. Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2395-406
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:2001369-Amidohydrolases, pubmed-meshheading:2001369-Amino Acid Sequence, pubmed-meshheading:2001369-Animals, pubmed-meshheading:2001369-Antigens, CD4, pubmed-meshheading:2001369-Carbohydrate Conformation, pubmed-meshheading:2001369-Carbohydrate Sequence, pubmed-meshheading:2001369-Cell Line, pubmed-meshheading:2001369-Cricetinae, pubmed-meshheading:2001369-Cricetulus, pubmed-meshheading:2001369-Female, pubmed-meshheading:2001369-Glycopeptides, pubmed-meshheading:2001369-Humans, pubmed-meshheading:2001369-Magnetic Resonance Spectroscopy, pubmed-meshheading:2001369-Molecular Sequence Data, pubmed-meshheading:2001369-Oligosaccharides, pubmed-meshheading:2001369-Ovary, pubmed-meshheading:2001369-Peptide Mapping, pubmed-meshheading:2001369-Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase, pubmed-meshheading:2001369-Recombinant Proteins, pubmed-meshheading:2001369-Transfection, pubmed-meshheading:2001369-Trypsin
pubmed:year
1991
pubmed:articleTitle
Carbohydrate structures of recombinant soluble human CD4 expressed in Chinese hamster ovary cells.
pubmed:affiliation
Department of Medicinal and Analytical Chemistry, Genentech, Inc., South San Francisco, California 94080.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.