Binding of human natural antibodies to nonalphaGal xenoantigens on porcine erythrocytes.
BACKGROUND
Xenotransplantation is considered one of possible solutions for the serious shortage of organs and cells in transplantation. Although the alphaGal epitope (Gal alpha1,3Gal beta1,4GlcNAc-R) has been identified as being a major xenoantigen responsible for hyperacute rejection, the removal of anti-alphaGal antibody alone from human serum is insufficient to circumvent antibody-mediated immune responses.


RESULTS
We report here the characterization of xenoreactive human natural antibodies against antigens without the alphaGal epitope (nonalphaGal xenoantigens) on porcine erythrocytes using flow cytometry and the evidence for their involvement in complement-mediated hemolysis. Furthermore, a novel protein of 45-kDa has been isolated from the porcine erythrocyte membrane as a major protein antigen recognized by human anti-nonalphaGal.


CONCLUSIONS
The data presented here will add to our knowledge of xenoantigens on porcine red cells and be important for developing strategies to produce modified red cells immunologically compatible to humans.
Zhu
A
A
The Lindsley F. Kimball Research Institute, The New York Blood Center, New York 10021, USA. azhu@nybc.org
D000818:Animals; D000906:Antibodies / Q000276:immunology*; D015478:Antigens, Heterophile / Q000737:chemistry / Q000276:immunology*; D003165:Complement System Proteins / Q000502:physiology; D004910:Erythrocyte Membrane / Q000276:immunology; D004912:Erythrocytes / Q000187:drug effects / Q000276:immunology*; D005434:Flow Cytometry; D006026:Glycoside Hydrolases / Q000494:pharmacology; D006461:Hemolysis / Q000502:physiology; D006801:Humans; D008970:Molecular Weight; D013552:Swine / Q000097:blood
D000906:Antibodies; D015478:Antigens, Heterophile; D003165:Complement System Proteins; D006026:Glycoside Hydrolases