{
"type": "article-journal",
"id": "https://doi.org/10.6084/m9.figshare.4714618.v146",
"categories": [
"Cancer"
],
"author": [
{
"family": "Arend",
"given": "Peter"
}
],
"issued": {
"date-parts": [
[
2017
]
]
},
"abstract": "Prokaryotic\n\"blood group A/B-like\" antigenic structures basically induce\ncross-reactive anti-A/B immunoglobulins, which neither\narise in blood group A nor in B individuals due to clonal selection but occur predominantly or exclusively\nin blood group O. While bacterial endotoxins non-specifically stimulate the\nformation of all immunoglobulins, involving the anti-A/B isoagglutinins, a\ndefinite, adaptive immunological induction of these agglutinins appears to be restricted\nto blood group O(H) individuals. In the non-O blood groups, anti-A/B reactivity\nis exerted by a primarily polyreactive, thymus-independent non-immune IgM\nmolecule that has undergone the phenotype-specific, glycosidic accommodation of\nplasma proteins, which reduces or excludes anti-self reactivity and even explains\nthe survival of highly nucleated ABO incompatible transplants, however,\nnecessarily involves impairment of immunity. While blood group A phenotype\ndevelopment thus is associated with impaired formation of adaptive and innate immunoglobulins,\nit promotes susceptibility to malaria infection via its intrinsic enzyme\nfunctions, initiating a self-destructive glycosidic, phenotypic accommodation\nof a \"wrong eukaryote\". Indeed, blood group A phenotype-specific\nGalNAc transferase activities, expressed by both cell surfaces and plasma\nproteins, and serine/threonine kinases from Plasmodium falciparum, which\nover the parasite's life cycle get into the red blood cell (RBC) of the human\nhost, might provide the metabolic condition for adhesion protein and RBC rosette\nformation, assumingly based on heterologous O-glycosylation, breaking a\nspecies barrier and completing the \"serine repeat\nantigen\". Thus, the obvious protection of human blood group O(H)\nindividuals from severe malaria infection may be explained by the lack of blood\ngroup A phenotype-specific GalNAc glycosylation(s), and suggests a new\nmolecular definition of the immunological (therapeutic) target. In fact, the\nhuman histo (blood) group O finally represents the worldwide most common blood\ntype, associated with a superior complex immunity, which in the non-O blood\ngroups is reduced through phenotypic, identical glycosylation of cell surfaces\nand plasma proteins.",
"container-title": "Figshare",
"DOI": "10.6084/M9.FIGSHARE.4714618.V146",
"publisher": "Figshare",
"title": "Central immunological position of the human histo (blood) group O(H).",
"URL": "https://figshare.com/articles/Central_immunological_position_of_the_human_histo_blood_group_O_H_/4714618/146",
"copyright": "CC BY 4.0"
}