Review: ABO blood group system—ABH oligosaccharide antigens, anti-A and anti-B, A and B glycosyltransferases, and <i>ABO</i> genes

Yamamoto, Fumiichiro

doi:10.21307/immunohematology-2019-418

Cited by 103 publications

(24 citation statements)

References 121 publications

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“…Only the differences of the nucleotide and deduced amino acid sequences from the A101 allele are shown. Similar tables have been published previously [ 20 , 34 , 41 , 42 ] …”

Section: Our Characterization Of Additional Abo Allelessupporting

confidence: 72%

“…Over 250 ABO alleles were deposited into the database, including alleles specifying A1, A2, A3, Ael, Aint, Am, Aw, Ax, cis -AB, B(A), B (B1), B3, Bel, Bw, Bx, and O phenotypes. Many missense mutations, nonsense mutations, and frameshift mutations (insertions and deletions) identified in the coding sequence of the ABO gene have been extensively reviewed and therefore are not duplicated in this review (see review articles [ 33 , 34 ] for detailed information on individual alleles and their references). Mutations have also been discovered that changed the mRNA splicing pattern of the ABO gene [ 35 – 37 ] or that altered the promoter/enhancer activity in the transcription of the ABO gene [ 31 , 38 , 39 ].…”

Section: Characterization Of Additional Abo Alleles In the Era Of Geneticsmentioning

confidence: 99%

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A historical overview of advances in molecular genetic/genomic studies of the ABO blood group system

Yamamoto

2021

Glycoconj J

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“…Only the differences of the nucleotide and deduced amino acid sequences from the A101 allele are shown. Similar tables have been published previously [ 20 , 34 , 41 , 42 ] …”

Section: Our Characterization Of Additional Abo Allelessupporting

confidence: 72%

Section: Characterization Of Additional Abo Alleles In the Era Of Geneticsmentioning

confidence: 99%

A historical overview of advances in molecular genetic/genomic studies of the ABO blood group system

Yamamoto

2021

Glycoconj J

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“…Glycans also act as a marker to interact with microbes. ABO blood group typing serves the best example of glycans as immunogenic response markers [ 47 ]. Group A and B have α1,3- N -acetylglucosamine (GalNAc) and α1,3-Gal attached to the H antigen's galactose residue, respectively.…”

Section: N-glycans In Immunological Aspect (Vaccine and Anti...mentioning

confidence: 99%

N-glycosylation, a leading role in viral infection and immunity development

Pandey¹,

Sharma

Prajapati³

et al. 2022

Mol Biol Rep

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N- linked protein glycosylation is an essential co-and posttranslational protein modification that occurs in all three domains of life; the assembly of N- glycans follows a complex sequence of events spanning the (Endoplasmic Reticulum) ER and the Golgi apparatus. It has a significant impact on both physicochemical properties and biological functions. It plays a significant role in protein folding and quality control, glycoprotein interaction, signal transduction, viral attachment, and immune response to infection. Glycoengineering of protein employed for improving protein properties and plays a vital role in the production of recombinant glycoproteins and struggles to humanize recombinant therapeutic proteins. It considers an alternative platform for biopharmaceuticals production. Many immune proteins and antibodies are glycosylated. Pathogen’s glycoproteins play vital roles during the infection cycle and their expression of specific oligosaccharides via the N -glycosylation pathway to evade detection by the host immune system. This review focuses on the aspects of N -glycosylation processing, glycoengineering approaches, their role in viral attachment, and immune responses to infection. Supplementary Information The online version contains supplementary material available at 10.1007/s11033-022-07359-4.

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“…The ABH(O) blood group antigens are specific carbohydrate structures attached to glycoproteins and glycolipids present on the surface of human erythrocytes, epithelial and endothelial cells of different tissues ( Yamamoto, 2004 ; Cooling, 2015 ). Responsible for blood group A biosynthesis is an N-acetylgalactosaminyltransferase (ABO A enzyme) that transfers an N-acetylgalactosamine (GalNAc) in α1,3-linkage to a precursor structure called the H antigen (Fucα1,2-Galβ-R) resulting in the trisaccharide GalNAcα1-3-(Fucα1,2)-Galβ-R ( Figure 1 ).…”

Section: Introductionmentioning

confidence: 99%

In Planta Production of the Receptor-Binding Domain From SARS-CoV-2 With Human Blood Group A Glycan Structures

et al. 2022

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Glycosylation of viral envelope proteins is important for infectivity and immune evasion. The SARS-CoV-2 spike protein is heavily glycosylated and host-derived glycan modifications contribute to the formation of specific immunogenic epitopes, enhance the virus-cell interaction or affect virus transmission. On recombinant viral antigens used as subunit vaccines or for serological assays, distinct glycan structures may enhance the immunogenicity and are recognized by naturally occurring antibodies in human sera. Here, we performed an in vivo glycoengineering approach to produce recombinant variants of the SARS-CoV-2 receptor-binding domain (RBD) with blood group antigens in Nicotiana benthamiana plants. SARS-CoV-2 RBD and human glycosyltransferases for the blood group ABH antigen formation were transiently co-expressed in N. benthamiana leaves. Recombinant RBD was purified and the formation of complex N-glycans carrying blood group A antigens was shown by immunoblotting and MS analysis. Binding to the cellular ACE2 receptor and the conformation-dependent CR3022 antibody showed that the RBD glycosylation variants carrying blood group antigens were functional. Analysis of sera from RBD-positive and RBD-negative individuals revealed further that non-infected RBD-negative blood group O individuals have antibodies that strongly bind to RBD modified with blood group A antigen structures. The binding of IgGs derived from sera of non-infected RBD-negative blood group O individuals to blood group A antigens on SARS-CoV-2 RBD suggests that these antibodies could provide some degree of protection from virus infection.

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Review: ABO blood group system—ABH oligosaccharide antigens, anti-A and anti-B, A and B glycosyltransferases, and ABO genes

Cited by 103 publications

References 121 publications

A historical overview of advances in molecular genetic/genomic studies of the ABO blood group system

A historical overview of advances in molecular genetic/genomic studies of the ABO blood group system

N-glycosylation, a leading role in viral infection and immunity development

In Planta Production of the Receptor-Binding Domain From SARS-CoV-2 With Human Blood Group A Glycan Structures

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