Forssman expression on human erythrocytes: biochemical and genetic evidence of a new histo-blood group system
(2013) In Blood 121(8). p.1459-1468- Abstract
- In analogy with histo-blood group A antigen, Forssman (Fs) antigen terminates with alpha 3-N-acetylgalactosamine and can be used by pathogens as a host receptor in many mammals. However, primates including humans lack Fs synthase activity and have naturally occurring Fs antibodies in plasma. We investigated individuals with the enigmatic ABO subgroup A(pae) and found them to be homozygous for common O alleles. Their erythrocytes had no A antigens but instead expressed Fs glycolipids. The unexpected Fs antigen was confirmed in structural, serologic, and flow-cytometric studies. The Fs synthase gene, GBGT1, in A(pae) individuals encoded an arginine to glutamine change at residue 296. Gln296 is present in lower mammals, whereas Arg296 was... (More)
- In analogy with histo-blood group A antigen, Forssman (Fs) antigen terminates with alpha 3-N-acetylgalactosamine and can be used by pathogens as a host receptor in many mammals. However, primates including humans lack Fs synthase activity and have naturally occurring Fs antibodies in plasma. We investigated individuals with the enigmatic ABO subgroup A(pae) and found them to be homozygous for common O alleles. Their erythrocytes had no A antigens but instead expressed Fs glycolipids. The unexpected Fs antigen was confirmed in structural, serologic, and flow-cytometric studies. The Fs synthase gene, GBGT1, in A(pae) individuals encoded an arginine to glutamine change at residue 296. Gln296 is present in lower mammals, whereas Arg296 was found in 6 other primates, > 250 blood donors and A(pae) family relatives without the A(pae) phenotype. Transfection experiments and molecular modeling showed that Agr296Gln reactivates the human Fs synthase. Uropathogenic E coli containing prsG-adhesin-encoding plasmids agglutinated A(pae) but not group O cells, suggesting biologic implications. Predictive tests for intravascular hemolysis with crossmatch-incompatible sera indicated complement-mediated destruction of Fs-positive erythrocytes. Taken together, we provide the first conclusive description of Fs expression in normal human hematopoietic tissue and the basis of a new histo-blood group system in man, FORS. (Blood. 2013;121(8):1459-1468) (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3979324
- author
- Svensson, Lola ; Hult, Annika LU ; Stamps, Robert ; Angstrom, Jonas ; Teneberg, Susann ; Storry, Jill LU ; Jorgensen, Rene ; Rydberg, Lennart ; Henry, Stephen M. and Olsson, Martin L LU
- organization
- publishing date
- 2013
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Blood
- volume
- 121
- issue
- 8
- pages
- 1459 - 1468
- publisher
- American Society of Hematology
- external identifiers
-
- wos:000321750000032
- scopus:84874402159
- pmid:23255552
- ISSN
- 1528-0020
- DOI
- 10.1182/blood-2012-10-455055
- language
- English
- LU publication?
- yes
- id
- f7cdbd90-4338-41df-9a26-30da9b78fe0a (old id 3979324)
- date added to LUP
- 2016-04-01 10:27:33
- date last changed
- 2022-04-04 18:19:22
@article{f7cdbd90-4338-41df-9a26-30da9b78fe0a, abstract = {{In analogy with histo-blood group A antigen, Forssman (Fs) antigen terminates with alpha 3-N-acetylgalactosamine and can be used by pathogens as a host receptor in many mammals. However, primates including humans lack Fs synthase activity and have naturally occurring Fs antibodies in plasma. We investigated individuals with the enigmatic ABO subgroup A(pae) and found them to be homozygous for common O alleles. Their erythrocytes had no A antigens but instead expressed Fs glycolipids. The unexpected Fs antigen was confirmed in structural, serologic, and flow-cytometric studies. The Fs synthase gene, GBGT1, in A(pae) individuals encoded an arginine to glutamine change at residue 296. Gln296 is present in lower mammals, whereas Arg296 was found in 6 other primates, > 250 blood donors and A(pae) family relatives without the A(pae) phenotype. Transfection experiments and molecular modeling showed that Agr296Gln reactivates the human Fs synthase. Uropathogenic E coli containing prsG-adhesin-encoding plasmids agglutinated A(pae) but not group O cells, suggesting biologic implications. Predictive tests for intravascular hemolysis with crossmatch-incompatible sera indicated complement-mediated destruction of Fs-positive erythrocytes. Taken together, we provide the first conclusive description of Fs expression in normal human hematopoietic tissue and the basis of a new histo-blood group system in man, FORS. (Blood. 2013;121(8):1459-1468)}}, author = {{Svensson, Lola and Hult, Annika and Stamps, Robert and Angstrom, Jonas and Teneberg, Susann and Storry, Jill and Jorgensen, Rene and Rydberg, Lennart and Henry, Stephen M. and Olsson, Martin L}}, issn = {{1528-0020}}, language = {{eng}}, number = {{8}}, pages = {{1459--1468}}, publisher = {{American Society of Hematology}}, series = {{Blood}}, title = {{Forssman expression on human erythrocytes: biochemical and genetic evidence of a new histo-blood group system}}, url = {{http://dx.doi.org/10.1182/blood-2012-10-455055}}, doi = {{10.1182/blood-2012-10-455055}}, volume = {{121}}, year = {{2013}}, }