Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1993-9-7
pubmed:abstractText
Lyme disease is a chronic, multisystemic infection caused by the tick-borne spirochete Borrelia burgdorferi. Attachment of the spirochete to host cells via specific receptors is likely to be important in the establishment of infection. B. burgdorferi have previously been shown to bind to a variety of mammalian cells in vitro. Here we demonstrate that binding of B. burgdorferi to human platelets is mediated by the integrin alpha IIb beta 3 (glycoprotein IIb-IIIa), a critical receptor in thrombosis and hemostasis. Functional expression of this receptor requires platelet activation, and binding of the spirochete was observed only to activated platelets. Binding was inhibited by a synthetic Arg-Gly-Asp peptide that blocks ligand interaction with many integrins and by a synthetic peptide based on the gamma chain of fibrinogen that blocks binding to alpha IIb beta 3. In addition, attachment of the spirochete to platelets was inhibited by monoclonal antibodies directed against alpha IIb beta 3 that are known to block ligand-receptor interaction. No inhibition was seen with control peptides or with antibodies directed against other platelet receptors. B. burgdorferi bound efficiently to purified alpha IIb beta 3 but did not bind to platelets deficient in this integrin. Efficient platelet binding was displayed by a cloned, infectious B. burgdorferi strain, whereas a cloned noninfectious strain did not bind to platelets. Binding to integrins may be important for the ability of B. burgdorferi to establish infection in the diverse tissues affected by Lyme disease.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-1398992, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-1527418, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-1555235, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-1560445, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-1672265, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-1674624, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-1693333, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-1716609, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-1730504, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-1830294, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-1867318, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-2164050, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-2298482, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-2332509, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-2387841, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-2442581, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-2537530, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-2569162, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-2665870, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-2668764, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-2716523, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-2722830, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-2742818, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-2925254, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-2952653, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-3143807, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-3161896, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-3326133, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-3404544, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-3577473, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-3693538, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-3966535, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-4013743, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-4473996, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-574143, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-6270087, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-6572380, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-6746643, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-6746667, http://linkedlifedata.com/resource/pubmed/commentcorrection/8394007-845165
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
90
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7059-63
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Integrin alpha IIb beta 3 mediates binding of the Lyme disease agent Borrelia burgdorferi to human platelets.
pubmed:affiliation
Division of Rheumatology and Immunology, Tufts-New England Medical Center, Boston, MA 02111.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't