6533b856fe1ef96bd12b2901

RESEARCH PRODUCT

Cross-Reactivity of Antibodies Immunoadsorbed to Laminin with Recombinant Human La (SS-B) Protein

M. S. HuhImre SemseiSooghee ChangHang Rae KimS. KimDaniel GrölzJiyoun LeeMichael BachmannI. S. Kim

subject

Recombinant Fusion ProteinsMolecular Sequence DataImmunologyPeptideCross ReactionsBiologyAutoantigensEpitopeAutoimmune Diseaseslaw.inventionEpitopesMiceSpecies SpecificityAntigenAntibody SpecificitylawLamininConsensus SequenceAnimalsHumansImmunology and AllergyAmino Acid SequenceElméleti orvostudományokPeptide sequenceImmunosorbent TechniquesAutoantibodieschemistry.chemical_classificationOrvostudományokMolecular biologyPeptide FragmentsAmino acidRibonucleoproteinschemistryRecombinant DNAbiology.proteinKidney DiseasesLamininAntibody

description

Anti-La (SS-B) antibodies cross-reacting with mouse B1 laminin were reported in sera of patients with systemic lupus erythematosus. However, the common epitope had not been characterized. Immunoblotting conditions were established, allowing detection and elution of anti-La (SS-B)/laminin cross-reacting antibodies. Antibodies adsorbed to mouse B1 laminin represented a subclass of anti-La antibodies. They strongly reacted with human full length recombinant La protein. However, they failed to react with either an N-terminal La peptide consisting of amino acids 1-192 or a C-terminal La peptide starting at methionine 223, while they still reacted with recombinant La peptides consisting of the amino acids 1-341 or starting at 192. These data indicate that the La (SS-B)/laminin epitope is located between amino acids 192-223 of human La protein, which includes the amino acids EAKLRA, common to the nuclear autoantigen La (SS-B) and the human or mouse B1 laminin.

https://doi.org/10.1006/jaut.1997.0181