Linked Life Data

2677404

Source:http://linkedlifedata.com/resource/pubmed/id/2677404

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1989-11-9
pubmed:abstractText
The synthesis of the extensively O-glycosylated attachment protein, G, of human respiratory syncytial virus and its expression on the cell surface were examined in a mutant Chinese hamster ovary (CHO) cell line, ldlD, which has a defect in protein O glycosylation. These cells, used in conjunction with an inhibitor of N-linked oligosaccharide synthesis, can be used to establish conditions in which no carbohydrate addition occurs or in which either N-linked or O-linked carbohydrate addition occurs exclusively. A recombinant vaccinia virus expression vector for the G protein was constructed which, as well as containing the human respiratory syncytial virus G gene, contained a portion of the cowpox virus genome that circumvents the normal host range restriction of vaccinia virus in CHO cells. The recombinant vector expressed high levels of G protein in both mutant ldlD and wild-type CHO cells. Several immature forms of the G protein were identified that contained exclusively N-linked or O-linked oligosaccharide side chains. Metabolic pulse-chase studies indicated that the pathway of maturation for the G protein proceeds from synthesis of the 32-kilodalton (kDa) polypeptide accompanied by cotranslational attachment of high-mannose N-linked sugars to form an intermediate with an apparent mass of 45 kDa. This step is followed by the Golgi-associated conversion of the N-linked sugars to the complex type and the completion of the O-linked oligosaccharides to achieve the mature 90-kDa form of G. Maturation from the 45-kDa N-linked form to the mature 90-kDa form occurred only in the presence of O-linked sugar addition, confirming that O-linked oligosaccharides constitute a significant proportion of the mass of the mature G protein. In the absence of O glycosylation, forms of G bearing galactose-deficient truncated N-linked and fully mature N-linked oligosaccharides were observed. The effects of N- and O-linked sugar addition on the transport of G to the cell surface were measured. Indirect immunofluorescence and flow cytometry showed that G protein could be expressed on the cell surface in the absence of either O glycosylation or N glycosylation. However, cell surface expression of G lacking both N- and O-linked oligosaccharides was severely depressed.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-202393, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-2715331, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-2831390, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-3264879, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-3316707, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-3369089, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-3373568, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-3380796, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-3455762, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-3476951, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-3571485, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-3655746, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-3754878, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-3773052, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-3858865, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-3896128, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-3919149, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-3948246, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-4009147, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-4031826, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-4069997, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-4204552, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-6299584, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-6415065, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-6636537, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-6767809, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-6886679, http://linkedlifedata.com/resource/pubmed/commentcorrection/2677404-7061468
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-538X
pubmed:author
pubmed:issnType
Print
pubmed:volume
63
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4767-76
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Structure and cell surface maturation of the attachment glycoprotein of human respiratory syncytial virus in a cell line deficient in O glycosylation.
pubmed:affiliation
Department of Microbiology, University of Alabama Medical School, Birmingham 35294.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't