|
|||||||||
|
|
|
|
|
|
|
|
|
|
|
K Thibaudeau, L Borche, JP Soulillou and D Blanchard
Centre Regional de Transfusion Sanguine, Nantes, France.
Human natural "anti-Gal" antibodies are specifically directed to Gal alpha
1-3Gal beta 1-4GlcNAc residues expressed on non-primate mammal and new
world monkey cells. We investigated the relative involvement of purified
IgG and IgM anti-Gal as xenoreactive natural antibodies (XNA). IgG and IgM
were isolated from human plasma, and anti-Gal antibodies were purified by
affinity chromatography on a Synsorb-14 column (Chembiomed, Edmonton,
Alberta, Canada). Anti-Gal of both IgM and IgG classes represent the bulk
of human XNA that bind to porcine platelets in enzyme-linked immunosorbent
assay (ELISA). On immunoblots, normal human sera, as well as purified IgM
and IgG fractions, reacted with 115- , 125-, 135-, 150-, 180-, 210-, and
240-kd) pig platelet proteins, whereas purified anti-Gal antibodies of both
IgM and IgG classes mainly bound to 135-, 150-, 180-, and 210-kD
glycoproteins. A low reactivity was observed in ELISA with anti-Gal free
IgM and IgG, indicating that xenoantibodies are not solely directed to
galactosyl epitopes. These antibodies revealed bands of 115, 125, and 240
kD, alpha-Galactosidase treatment of porcine platelet glycoproteins (gps)
enriched by affinity chromatography abrogated the reactivity of 135- and
210-kD proteins. N- and O-glycosidase treatments demonstrated that
alpha-galactosyl residues are located on the O-glycans of the 135-kD
component. Finally, glycoproteins of 90 and 135 kD were identified by amino
acid sequencing as the pig analogs of the human glycoproteins IIIa and IIb,
respectively, whereas the 240-kD) component was identified as the porcine
fibrinogen, using a new murine monoclonal antibody (naM147-7B6; IgG1)
specific for its beta-chain.
This article has been cited by other articles:
| |||||||||||
 |
 |
 |
|||||||
 |
 |
 |
 |
 |
 |
 |
 |
||
| Copyright © 1996 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||
