Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1991-10-8
pubmed:abstractText
Intercellular adhesion molecule-1 (ICAM-1) has been shown to interact with the integrin leukocyte function associated antigen-1 (LFA-1) in a variety of cell-cell adhesion phenomena. Furthermore, it serves as a receptor for the majority of the Rhinoviruses and for Plasmodium falciparum-infected human erythrocytes. We generated recombinant, carbohydrate-free ICAM-1 and several ICAM-1 fragments by expression in Escherichia coli using the fusion protein expression system pUEX1-3. In Western blot and dot blot analyses we tested mAbs (7F7, 8B9, P3.58-BA3, -BA11, -BA14, -BA19, -BA21, -BA23, -BA24, -BA26, CL203.4 and 84H10) and a polyclonal antiserum directed against native ICAM-1 for their reactivity with these constructs. We were able to localize the binding site for the mAbs P3.58-BA3, -BA11, -BA14, -BA19, -BA21, -BA23, -BA24 and -BA26 at domain 5, whereas the mAbs 7F7, 8B9, CL203.4 and 84H10 did not recognize the recombinant, carbohydrate-free ICAM-1. Our findings suggest the presence of an immunodominant epitope on domain 5 of ICAM-1.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0165-2478
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
237-43
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Generation of recombinant, carbohydrate-free intercellular adhesion molecule-1 (ICAM-1) and ICAM-1 fragments in Escherichia coli and mapping of epitopes recognized by anti-ICAM-1 monoclonal antibodies.
pubmed:affiliation
Institut für Hygiene, University of Innsbruck, Austria.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't