Linked Life Data

15750863

Source:http://linkedlifedata.com/resource/pubmed/id/15750863

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2005-6-23
pubmed:abstractText
The bovine parvovirus (BPV) hemagglutinates human erythrocytes by binding to glycophorin A (GPA). The purpose of this study was to determine which carbohydrate on GPA binds BPV. Treatment of GPA with alpha2,3,-6,-8 neuraminidase eliminated binding of BPV to GPA. Beta-elimination of O-linked sialic acids on GPA eliminated binding, while removal of N-linked carbohydrates using the N-glycosidase PNGase F failed to eliminate binding. Treatment of GPA with a neuraminidase which specifically cleaved alpha2,3 glycosidic bonds eliminated BPV binding and, following this treatment, virus binding to GPA was restored by reconstitution of alpha2,3-linked neuraminic acids. These results indicated the O-linked alpha2,3 neuraminic acids of GPA bind BPV.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0304-8608
pubmed:author
pubmed:issnType
Print
pubmed:volume
150
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1477-84
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Attachment of bovine parvovirus to O-linked alpha 2,3 neuraminic acid on glycophorin A.
pubmed:affiliation
Department of Microbiology and Molecular Biology, Brigham Young University, Provo, Utah 84602, USA.
pubmed:publicationType
Journal Article