Zalygin, A., Solovyeva, D., Vaskan, I., Henry, S., Schaefer, M., Volynsky, P., Tuzikov, A., Korchagina, E., Ryzhov, I., Nizovtsev, A., Mochalov, K., Efremov, R., Shtykova, E., Oleinikov, V. and Bovin, N.
Summary: Synthesis of Forssman glycolipid FSL-FS-5. Kodeyctes and native FORS1+ donor used to compare reactivity toward monoclonal anti-Forssman antibody
Inna S. Popova,Elena Yu. Korchagina, Marina A. Sablina, Alexander S. Paramonov, Annika K. Hult, Stephen M. Henry and Nicolai V. Bovin, Mendeleev Commun., (2019) 29, 578-580
Summary: Cells are highly decorated with glycans (carbohydrates) and this complex and dominating coating on cells, which also carries the glycan blood group antigens, is critically important to immunology and many related clinical practices such as transfusion, transplantation and immunotherapy. The ability to modify this glycan coat is difficult to achieve with standard techniques like molecular biology or direct chemical ligation, particularly as glycosylation is probably the most complex secondary gene event in a cell. However, the natural ability of lipid-linked structures to self-insert and hydrophobically anchor into cell membranes opened up the opportunity to develop synthetic Function-Spacer-Lipid technology for cell surface modification. From this glycan modification aspect Kode Technology has been used to add glycan related blood group antigens such as ABO, Lewis, P, FORS, as well as sialooligosaccharides and hyaluronic acid onto cells to study immunology and cell glycosylation and more recently as a potential immuno-oncotherapeutic therapy.
Stephen M. Henry & Nicolai V. Bovin, Journal of the Royal Society of New Zealand (2018), 49:2, 100-113
Summary: We describe a rapid one-step method to biotinylate virtually any biological or non-biological surface. Contacting a solution of biotin-spacer-lipid constructs with a surface will form a coating within seconds on non-biological surfaces or within minutes on most biological membranes including membrane viruses. The resultant biotinylated surface can then be used to interact with avidinylated conjugates, beads, vesicles, surfaces or cells.
Stephen Henry, Eleanor Williams, Katie Barr, Elena Korchagina, Alexandr Tuzikov, Natalia Ilyushin, Sidahmed A. Abayzeed, Kevin F. Webb & Nicolai Bovin, Scientific Reports (2018), 8:2845
A simplistic overview
The presence of a blood group A and B antigens on the outside of a red cell starts with the presence of a blood group A or B gene and a variety of different glycolipid and glycoprotein blood group H antigen precursors. When the gene is transcribed it results in a glycosyltransferase, which in the endoplasmic reticulum and Golgi is able to transfer in specific alpha 1-3 linkage an activated N-acetyl galactosamine or galactose sugar for blood group A or B, respectively, onto blood group H antigen precursors. The resultant blood group antigen, when present on the surface of a red cell membrane can then react with antibodies. The amount, structure (length and branching) and to some extent the type of antigen, present at the red cell surface, determine its ability to react with specific antibodies. Thus creating serologic variants that can be defined as specific blood group ABO phenotypes. Essentially the dominating factor in determining the phenotypic variants of A and B is genetic variants that result in enzymes which have reduced enzyme activity which affect the level of antigen present at the red cell surface. A detailed review of this process follows.
Lola Svensson, Serge Pérez & Stephen Henry. “Blood Group ABO and its variants” Glycopedia (2017)