Linked Life Data

9973445

Source:http://linkedlifedata.com/resource/pubmed/id/9973445

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1999-4-13
pubmed:abstractText
Autoantibodies to nuclear and smooth muscle are common in hepatitis B virus (HBV) infection. To understand their origin, we scanned protein databases and found that HBV-DNA polymerase (HBV-pol) shares 7-9 amino acid sequences with nuclear (MHC II trans-activator, nuclear pore core protein, nuclear mitotic apparatus, and polymyositis sclerosis Ag) and smooth muscle proteins (caldesmon and myosin). Twenty-mer peptides with relevant homologues and an irrelevant control peptide were constructed and ELISAs were established. Sixty-five children with chronic HBV infection, 104 patients with other chronic liver diseases (CLD), 36 patients with extrahepatic autoimmune diseases, and 24 healthy controls were investigated. Double reactivity to HBV-pol peptides and corresponding self homologues was observed in 40% of HBV-positive patients as compared with four (4%) with other chronic liver diseases, two (6%) with extrahepatic autoimmune diseases, and in none of the healthy controls (p < 0.001 for all). Double reactivity to myosin or caldesmon peptides and their HBV-pol homologues was associated with anti-smooth muscle Ab positivity by immunofluorescence (p < 0.05 for both). HBV-positive sera double reactive for myosin or caldesmon and their homologous HBV-pol peptides also reacted with the native proteins on immunoblot. Fifty to ninety percent Ab inhibition to individual HBV-pol and HBV-pol99-118 peptides was noted by preincubation with individual HBV-pol/self homologue peptide and native proteins, respectively, but not with control peptide. Our results show that cross-reactive immunity targeting homologous sequences of viral and self proteins may partly account for autoantibody production in HBV infection.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
162
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1802-10
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9973445-Adolescent, pubmed-meshheading:9973445-Adult, pubmed-meshheading:9973445-Aged, pubmed-meshheading:9973445-Amino Acid Sequence, pubmed-meshheading:9973445-Antibodies, Antinuclear, pubmed-meshheading:9973445-Antibodies, Viral, pubmed-meshheading:9973445-Antigens, Viral, pubmed-meshheading:9973445-Autoantibodies, pubmed-meshheading:9973445-Autoantigens, pubmed-meshheading:9973445-Case-Control Studies, pubmed-meshheading:9973445-Child, pubmed-meshheading:9973445-Child, Preschool, pubmed-meshheading:9973445-DNA-Directed DNA Polymerase, pubmed-meshheading:9973445-Female, pubmed-meshheading:9973445-Gene Products, pol, pubmed-meshheading:9973445-Hepatitis B, Chronic, pubmed-meshheading:9973445-Hepatitis B virus, pubmed-meshheading:9973445-Humans, pubmed-meshheading:9973445-Male, pubmed-meshheading:9973445-Middle Aged, pubmed-meshheading:9973445-Molecular Mimicry, pubmed-meshheading:9973445-Molecular Sequence Data, pubmed-meshheading:9973445-Muscle, Smooth, pubmed-meshheading:9973445-Muscle Proteins, pubmed-meshheading:9973445-Nuclear Proteins, pubmed-meshheading:9973445-Sequence Homology, Amino Acid
pubmed:year
1999
pubmed:articleTitle
Mimicry between the hepatitis B virus DNA polymerase and the antigenic targets of nuclear and smooth muscle antibodies in chronic hepatitis B virus infection.
pubmed:affiliation
Institute of Hepatology, University College London Medical School, London, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't