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Biochemical characterization of the neutrophil-specific antigen NB1
DF Stroncek, KM Skubitz and JJ McCullough
Department of Laboratory Medicine, University of Minnesota Medical School,
Minneapolis.
Neutrophil-specific alloantibodies and the antigens they recognize are
important in clinical medicine, but little is known about the structure of
these antigens. Alloimmunization to the antigen NB1 is a clinically
important cause of neonatal neutropenia and febrile transfusion reactions.
To study the immunochemistry of the NB1 antigen, we prepared neutrophil
plasma membranes and granules by nitrogen cavitation and differential
centrifugation and then analyzed them by sodium dodecyl
sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotting
with alloantibodies to several neutrophil-specific antigens. Two different
antisera to the neutrophil-specific antigen NB1 identified an approximately
55-Kd protein by immunoblotting on neutrophil membranes from four
NB1-positive donors but not on neutrophil membranes from five NB1-negative
donors. Four anti-NB1 antisera immunoprecipitated a 58- to 64-Kd protein
from extracts of NB1- positive neutrophils surface-labeled with 125I using
lactoperoxidase, but not from similarly treated NB1-negative neutrophils.
Normal human serum did not immunoprecipitate or immunoblot any proteins
from these same neutrophil preparations. The NB1 antigen was detected by
immunoblotting in secondary granules but was not found in primary granules.
The electrophoretic mobility of the antigen was decreased slightly by
reduction, suggesting that intrachain disulfide bonds were present. After
reduction, the antigen could no longer be recognized by anti-NB1 antisera,
but treatment of the antigen with periodate had no effect on the ability of
anti-NB1 antisera to recognize the antigen, suggesting that it is not a
carbohydrate. The data suggest that the neutrophil-specific antigen NB1 is
present on a 58- to 64-Kd surface glycoprotein that is also present in
secondary granules, and that the NB1 epitope is not a carbohydrate but
probably resides in the tertiary structure of the protein backbone.
Volume 75,
Issue 3,
pp. 744-755,
02/01/1990
Copyright © 1990 by The American Society of Hematology
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