Linked Life Data

15501399

Source:http://linkedlifedata.com/resource/pubmed/id/15501399

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2004-10-25
pubmed:abstractText
Treatment-resistant Lyme arthritis, which may result from infection-induced autoimmunity, is associated with reactivity to a T cell epitope of outer-surface protein A (OspA(161-175)) of Borrelia burgdorferi sensu stricto (Bb). This syndrome has been noted primarily in the United States where only Bb is present, and rarely in Europe where Borrelia garinii (Bg) and Borrelia afzelii (Ba) predominate. To gain a better understanding of this epitope, we identified its species-specific polymorphisms, determined their immunogenicity, and characterized the contribution of individual amino acids. Based on published sequences the Bb peptide differed from the Ba peptide in six of the nine core residues (amino acids 165-173), whereas the Bg peptide usually differed in three of the nine residues. Lymphocytes from seven patients with treatment-resistant Lyme arthritis proliferated in response to the Bb peptide, but not to the Ba or Bg peptide. Substitution analysis showed that valine166 and threonine172 were critical for the immunogenicity of the Bb peptide. Thus, consistent with the geographic distribution of the illness, the European causative agents of Lyme borreliosis usually lack the putative pathogenic OspA epitope. These observations are consistent with the hypothesis that T cell recognition of this epitope is important in the induction of autoimmunity in treatment-resistant Lyme arthritis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0896-8411
pubmed:author
pubmed:issnType
Print
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
281-92
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:15501399-Amino Acid Sequence, pubmed-meshheading:15501399-Amino Acid Substitution, pubmed-meshheading:15501399-Antigens, Surface, pubmed-meshheading:15501399-Arthritis, Infectious, pubmed-meshheading:15501399-Bacterial Outer Membrane Proteins, pubmed-meshheading:15501399-Bacterial Vaccines, pubmed-meshheading:15501399-Borrelia burgdorferi, pubmed-meshheading:15501399-Cell Proliferation, pubmed-meshheading:15501399-Cells, Cultured, pubmed-meshheading:15501399-Cytokines, pubmed-meshheading:15501399-Drug Resistance, Bacterial, pubmed-meshheading:15501399-Epitopes, T-Lymphocyte, pubmed-meshheading:15501399-Humans, pubmed-meshheading:15501399-Lipoproteins, pubmed-meshheading:15501399-Lyme Disease, pubmed-meshheading:15501399-Lymphocyte Activation, pubmed-meshheading:15501399-Molecular Sequence Data, pubmed-meshheading:15501399-Peptide Fragments, pubmed-meshheading:15501399-Sequence Alignment, pubmed-meshheading:15501399-T-Lymphocytes
pubmed:year
2004
pubmed:articleTitle
Molecular characterization of the OspA(161-175) T cell epitope associated with treatment-resistant Lyme arthritis: differences among the three pathogenic species of Borrelia burgdorferi sensu lato.
pubmed:affiliation
Center for Immunology and Inflammatory Diseases, Division of Rheumatology, Allergy and Immunology, Massachusetts General Hospital, Harvard Medical School, Boston, MA 02114, USA. edrouin@partners.org
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't