Molecular mimicry in Lyme disease: monoclonal antibody H9724 to B. burgdorferi flagellin specifically detects chaperonin-HSP60.
Level 5 - mechanism / opinion, no new human data
In vitro laboratory study with no clinical trial or human patient cohort data
PubMed 8096152 · doi:10.1016/0925-4439(93)90096-j
What was done
Researchers investigated the cross-reactivity of monoclonal antibody H9724 (specific for the 41-kDa flagellar protein of Borrelia burgdorferi), which cross-reacts with human axons and a major protein in human neuroblastoma cell extracts. The homologous cross-reacting protein was purified from calf adrenal tissue and characterized using N-terminal sequencing.
What was found
The cross-reactive protein recognized by antibody H9724 was identified as chaperonin-HSP60. The abstract provides no numerical data, binding affinities, or quantitative metrics.
Why it matters
Identifying HSP60 as a cross-reactive target of anti-flagellin antibodies provides a specific biochemical candidate for molecular mimicry in Lyme disease.
Limits
This is strictly an in vitro bench investigation; the abstract does not demonstrate whether this cross-reactivity causes clinical pathology in human Lyme disease. No quantitative assay results, sample sizes, or error estimates are provided in the abstract.
Cited by
- partial Lyme infection induces molecular mimicry via flagella, causing autoantibodies against dopamine receptors, thyroid tissue, cardiolipin, and myelin.