Open AccessAn anti‐peptide antibody that recognizes a neo‐antigen in the CR1 stump remaining on erythrocytes after proteolysis
Author(s) -
BARBOSA J. E.,
HARRISON R. A.,
BARKER P. J.,
LACHMANN P. J.
Publication year - 1992
Publication title -
clinical & experimental immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.329
H-Index - 135
eISSN - 1365-2249
pISSN - 0009-9104
DOI - 10.1111/j.1365-2249.1992.tb06428.x
Subject(s) - proteolysis , antibody , biology , immunology , antigen , trypsinization , antiserum , transmembrane protein , ex vivo , in vivo , blocking antibody , microbiology and biotechnology , complement system , biochemistry , receptor , trypsin , enzyme
SUMMARY Previous studies of erythrocyte CR1 levels in systemic lupus erythematosus (SLE) and other diseases with in vovo complement activation have led lo the conclusion that CR1 levels fall because of loss of CR1 from erythrocytes by proteolysis —predominantly in the liver. In order to measure the existence of proteolysed CR1 remnants on erythrocytes an antibody was raised to a peptide corresponding to the CR1 sequence between the proximal standard consensus repeat (SCR) and the transmembrane segment. This antipeptide antibody recognizes a neo‐antigen found on trypsinized erythrocytes which has been demonstrated to represent the “CRI‐stump”, The anti‐ ‘CR1‐stump’ antiserum detects proteolysed CR1 on the ex vivo erythrocytes of a patient with cold haemolytic antibody disease (CHAD). However, higher affinity antibodies will be needed to make anti‐ CR1 ‐stump a satisfactory diagnostic reagent.