02871nas a2200337 4500000000100000008004100001260001300042653001500055653001300070653002400083653003500107653001600142653001100158653001900169653002700188653001200215653002100227653002500248653001600273653002600289100001800315700001700333700001200350700001300362700001600375245008600391300001100477490000700488520202400495022001402519 1989 d c1989 Feb10aAntibodies10aAntigens10aAntigens, Bacterial10aFluorescent Antibody Technique10aGlycolipids10aHumans10aImmunoblotting10aIntermediate Filaments10aleprosy10aMolecular Weight10aMycobacterium leprae10aSpinal Cord10aStaining and Labeling1 aBenjamins J A1 aCallahan R E1 aRunft D1 aGerras G1 aLefford M J00aAnti-neural antibodies in leprosy sera: further characterization of the antigens. a125-350 v213 a

Sera or plasmas from 129 leprosy patients were tested by immunoblotting for antibodies that bound to proteins in a Triton-insoluble fraction enriched in neural intermediate filaments (IF fraction) from human or bovine spinal cord. Sixty samples (47%) showed positive staining of proteins at 35 kDa, 42 kDa or both. The presence of these antibodies appeared to be evenly distributed across the spectrum of disease. The frequency of these antibodies in samples from 12 healthy Ethiopians was similar to that in the leprosy group. Similar antibodies were found in only three of 28 samples from U.S. patients with neurologic diseases and in seven of 35 normal U.S. sera. Sera from U.S. tuberculosis patients stained multiple bands in the 50-30 kDa region of the blots; 11 of 16 stained bands corresponding to the 35 kDa or 42 kDa bands along with a number of other bands in this region. The 35 kDa and 42 kDa antigens do not appear to be breakdown products of neural filaments or glial fibrillary acidic protein, since antibodies to these proteins do not react with the 35 kDa or 42 kDa antigen. Further, the staining pattern with the leprosy sera is unchanged following Ca2+-mediated proteolysis of the IF-enriched fraction. The two antigens differ from one another in isoelectric point: the pI of the 35 kDa antigen is 5.9, and the pI of the 42 kDa antigen is 4.8. Staining of the immunoblots with antibodies against a number of known neural antigens failed to identify the 35 kDa and 42 kDa antigens. The 42 kDa antigen appears to be a component of axolemma, since 42 kDa-positive leprosy sera stained a protein with identical migration in preparations of bovine peripheral nervous system and human central nervous system axolemma. In some sera, antibodies reacting with the 35 kDa antigen were adsorbed by D-O bovine serum albumin, a synthetic analogue of the terminal disaccharide portion of the phenolic glycolipid 1 of Mycobacterium leprae. Antibodies to the 42 kDa antigen were not removed by this treatment.

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