scholarly journals The SARS-CoV-2 receptor-binding domain preferentially recognizes blood group A

2021 ◽  
Vol 5 (5) ◽  
pp. 1305-1309 ◽  
Author(s):  
Shang-Chuen Wu ◽  
Connie M. Arthur ◽  
Jianmei Wang ◽  
Hans Verkerke ◽  
Cassandra D. Josephson ◽  
...  
Keyword(s):  
Blood Group ◽  
Sequence Similarity ◽  
Blood Group Antigens ◽  
Receptor Binding Domain ◽  
Respiratory Epithelial Cells ◽  
Blood Group A ◽  
Key Points ◽  
Group A ◽  
Lectin Family ◽  
Respiratory Epithelial

Key Points The RBD of SARS-CoV-2 shares sequence similarity with an ancient lectin family known to bind blood group antigens. SARS-CoV-2 RBD binds the blood group A expressed on respiratory epithelial cells, directly linking blood group A and SARS-CoV-2.

scholarly journals Heterogeneic expression of blood group A and H isoantigens in bladder tumors: association with nuclear volume.

1989 ◽  
Vol 37 (7) ◽  
pp. 1153-1155 ◽  
Author(s):  
T F Orntoft ◽  
K Nielsen
Keyword(s):  
Blood Group ◽  
Transitional Cell ◽  
Antigen Expression ◽  
Nuclear Volume ◽  
Intratumor Heterogeneity ◽  
Blood Group Antigens ◽  
Pathological Grade ◽  
Blood Group A ◽  
Group A ◽  
The Mean

Intratumor heterogeneity is a major problem in immunodiagnosis and treatment of carcinomas. To elucidate the well-known heterogeneity in transitional-cell carcinomas of the ability to express blood group ABO isoantigens, a stereological estimate of the mean nuclear volume in areas expressing blood group antigens was compared to the estimate from areas of identical pathological grade at which antigen expression was deleted. Four microscopic fields were examined from antigen-positive and four from antigen-negative areas in sections from 21 blood group O and 20 blood group A individuals. The sections were stained before examination by an indirect peroxidase method using monoclonal anti-H and anti-A antibodies. The mean nuclear volume increased, as expected, with increasing pathological grade. In blood group O individuals the mean nuclear volume was 241.5 microns 3 in antigen-positive areas and 338.2 microns 3 in antigen-negative areas (2p less than 0.0005) of identical pathological grade. In group A individuals the mean nuclear volume was 217.1 microns 3 in positive areas and 351.1 microns 3 in corresponding negative areas (2p less than 0.0025). The variation in volume parameter was essentially caused by a true variation between tumors (greater than 82%). The results indicate a complex biological mechanism associated with the cellular ability to express blood group antigens.

scholarly journals Blood Group A Antigen Is a Coreceptor inPlasmodium falciparum Rosetting

2000 ◽  
Vol 68 (5) ◽  
pp. 2971-2975 ◽  
Author(s):  
Antonio Barragan ◽  
Peter G. Kremsner ◽  
Mats Wahlgren ◽  
Johan Carlson
Keyword(s):  
Blood Group ◽  
Blood Cells ◽  
Malaria Parasite ◽  
General Feature ◽  
Enzymatic Digestion ◽  
Clinical Isolates ◽  
Rosette Formation ◽  
Blood Group Antigens ◽  
Blood Group A ◽  
Group A

ABSTRACT The malaria parasite Plasmodium falciparum utilizes molecules present on the surface of uninfected red blood cells (RBC) for rosette formation, and a dependency on ABO antigens has been previously shown. In this study, the antirosetting effect of immune sera was related to the blood group of the infected human host. Sera from malaria-immune blood group A (or B) individuals were less prone to disrupt rosettes from clinical isolates of blood group A (or B) patients than to disrupt rosettes from isolates of blood group O patients. All fresh clinical isolates and laboratory strains exhibited distinct ABO blood group preferences, indicating that utilization of blood group antigens is a general feature of P. falciparumrosetting. Soluble A antigen strongly inhibited rosette formation when the parasite was cultivated in A RBC, while inhibition by glycosaminoglycans decreased. Furthermore, a soluble A antigen conjugate bound to the cell surface of parasitized RBC. Selective enzymatic digestion of blood group A antigen from the uninfected RBC surfaces totally abolished the preference of the parasite to form rosettes with these RBC, but rosettes could still form. Altogether, present data suggest an important role for A and B antigens as coreceptors in P. falciparum rosetting.

scholarly journals The human gut symbiont Ruminococcus gnavus shows specificity to blood group A antigen during mucin glycan foraging: Implication for niche colonisation in the gastrointestinal tract

PLoS Biology ◽  
2021 ◽  
Vol 19 (12) ◽  
pp. e3001498
Author(s):  
Haiyang Wu ◽  
Emmanuelle H. Crost ◽  
C David Owen ◽  
Wouter van Bakel ◽  
Ana Martínez Gascueña ◽  
...  
Keyword(s):  
Blood Group ◽  
Sequence Similarity ◽  
Glycoside Hydrolases ◽  
Site Directed Mutagenesis ◽  
Titration Calorimetry ◽  
Directed Mutagenesis ◽  
Human Gut ◽  
Blood Group A ◽  
Group A

The human gut symbiont Ruminococcus gnavus displays strain-specific repertoires of glycoside hydrolases (GHs) contributing to its spatial location in the gut. Sequence similarity network analysis identified strain-specific differences in blood-group endo-β-1,4-galactosidase belonging to the GH98 family. We determined the substrate and linkage specificities of GH98 from R. gnavus ATCC 29149, RgGH98, against a range of defined oligosaccharides and glycoconjugates including mucin. We showed by HPAEC-PAD and LC-FD-MS/MS that RgGH98 is specific for blood group A tetrasaccharide type II (BgA II). Isothermal titration calorimetry (ITC) and saturation transfer difference (STD) NMR confirmed RgGH98 affinity for blood group A over blood group B and H antigens. The molecular basis of RgGH98 strict specificity was further investigated using a combination of glycan microarrays, site-directed mutagenesis, and X-ray crystallography. The crystal structures of RgGH98 in complex with BgA trisaccharide (BgAtri) and of RgGH98 E411A with BgA II revealed a dedicated hydrogen network of residues, which were shown by site-directed mutagenesis to be critical to the recognition of the BgA epitope. We demonstrated experimentally that RgGH98 is part of an operon of 10 genes that is overexpresssed in vitro when R. gnavus ATCC 29149 is grown on mucin as sole carbon source as shown by RNAseq analysis and RT-qPCR confirmed RgGH98 expression on BgA II growth. Using MALDI-ToF MS, we showed that RgGH98 releases BgAtri from mucin and that pretreatment of mucin with RgGH98 confered R. gnavus E1 the ability to grow, by enabling the E1 strain to metabolise BgAtri and access the underlying mucin glycan chain. These data further support that the GH repertoire of R. gnavus strains enable them to colonise different nutritional niches in the human gut and has potential applications in diagnostic and therapeutics against infection.

Normal Human Serum Contains Natural Antibodies Reactive With Autologous ABO Blood Group Antigens

Blood ◽  
1999 ◽  
Vol 93 (12) ◽  
pp. 4418-4424 ◽  
Author(s):  
Sergio H. Spalter ◽  
Srini V. Kaveri ◽  
Emmanuelle Bonnin ◽  
Jean-Claude Mani ◽  
Jean-Pierre Cartron ◽  
...  
Keyword(s):  
Human Serum ◽  
Blood Group ◽  
Autologous Blood ◽  
Natural Antibodies ◽  
Normal Human Serum ◽  
Abo Blood Group ◽  
Blood Group Antigens ◽  
Blood Group A ◽  
Group A ◽  
Normal Human

Abstract It is widely accepted that the serum of healthy individuals contains natural antibodies only against those blood group A or B antigens that are not expressed on the individual’s red blood cells. The mechanisms involved in tolerance to autologous blood group antigens remain unclear. In the present study, we show that IgM and IgG antibodies reactive with autologous blood group antigens are present in the immunoglobulin fraction of normal human serum. Natural IgG anti-A antibodies purified by affinity chromatography from IgG of individuals of blood group A exhibited an affinity for A trisaccharide antigen in the micromolar range and agglutinated A red cells at sixfold higher concentrations than those required for agglutination with affinity-purified anti-A IgG of individuals of blood group B. Whereas autoantibodies reactive with self A and B antigens are readily detected in purified IgG and IgM fractions, their expression is restricted in whole serum as a result of complementary interactions between variable regions of antibodies. These observations suggest that tolerance to autologous ABO blood group antigens is dependent on peripheral control of antibody autoreactivity.

scholarly journals Relationships between gastrointestinal microbiota and blood group antigens

2017 ◽  
Vol 49 (9) ◽  
pp. 473-483 ◽  
Author(s):  
Anuhya Gampa ◽  
Phillip A. Engen ◽  
Rima Shobar ◽  
Ece A. Mutlu
Keyword(s):  
Blood Group ◽  
Healthy Subjects ◽  
Antigen Expression ◽  
Blood Group Antigens ◽  
Gastrointestinal Microbiota ◽  
Fecal Microbiome ◽  
Blood Group A ◽  
Group A ◽  
Blood Specimens ◽  
The Impact

FUT2 is a gene for a fucosyltransferase that encodes expression of ABO blood group antigens found on gastrointestinal mucosa and secretions. We hypothesized that the fecal microbiomes of healthy subjects, with blood group antigens A, B, and O, have differing compositions. We analyzed 33 fecal and blood specimens from healthy subjects for FUT2 genotype, and the fecal microbiome was determined by 454 pyrosequencing. Our data show that being a blood group secretor is associated with less diversity at higher orders of taxonomy; and the presence of blood group A antigens in the secretor subjects are associated with an expansion families of bacteria within the gut. Furthermore, our study confirms the previous findings that secretors and nonsecretors have differing bacterial taxa. This extends the previous findings by demonstrating that the impact of being a nonsecretor is higher than that of individual blood group antigens. Additionally, we demonstrate that both secretor status and blood group antigen expression especially affect the Lachnospiraceae family of bacteria within the gut microbiome, with lower abundances noted in nonsecretors and higher abundances in secretors of various blood groups. We further note specific differences in blood group A-secretors demonstrating that the genus Blautia is lower in the group A-secretors compared with the non-A-secretors and that this reduction is accompanied by higher abundances of members of the Rikenellaceae, Peptostreptococcaceae, Clostridiales, and Turicibacter. This study offers a first insight into the relationship between the fecal microbiome and blood group antigens in secretors.

scholarly journals Blood group ABO gene–encoded A transferase catalyzes the biosynthesis of FORS1 antigen of FORS system upon Met69Thr/Ser substitution

2018 ◽  
Vol 2 (12) ◽  
pp. 1371-1381 ◽  
Author(s):  
Emili Cid ◽  
Miyako Yamamoto ◽  
Fumiichiro Yamamoto
Keyword(s):  
Blood Group ◽  
Blood Group A ◽  
Key Points ◽  
Group A

Key Points Met69Thr/Ser substitutions conferred blood group A glycosyltransferase with weak FS activity to produce FORS1 antigen of the FORS system. Met69Thr and LeuGlyGly266-268GlyGlyAla substitutions synergistically increase the acquired FS activity of A glycosyltransferase.

scholarly journals Cytochemical localization of blood group substances in human salivary glands using lectin-gold complexes.

1988 ◽  
Vol 36 (4) ◽  
pp. 337-348 ◽  
Author(s):  
M Nakajima ◽  
N Ito ◽  
K Nishi ◽  
Y Okamura ◽  
T Hirota
Keyword(s):  
Blood Group ◽  
Secretory Granules ◽  
Helix Pomatia ◽  
Staining Procedure ◽  
Blood Group Antigens ◽  
Gold Complexes ◽  
Cytochemical Localization ◽  
Blood Group A ◽  
Group A ◽  
In Cells

We investigated localization of blood group antigens and their related substances in human labial salivary and submandibular glands by application of a post-embedding cytochemical staining procedure using lectin- or glycoprotein-gold complexes. Surgical tissue was obtained from 10 patients. Blood group-specific lectins, such as Dolichos biflorus agglutinin or Helix pomatia agglutinin (group A-specific), Griffonia simplicifolia agglutinin-I B4 (group B-specific), and Ulex europaeus agglutinin I (group H-specific) could recognize A, B, and H antigens, respectively, only in mature secretory granules (mature SG), which were found preferentially in cells in the late phase of the maturation cycle. In immature secretory granules (immature SG), which were found in cells in the early or middle phase of the maturation cycle, no binding with these lectins was observed. The Golgi complexes and endoplasmic reticula also were not labeled with these lectins. In blood group O and B secretors, blood group antigens were uniformly distributed throughout all the mature SG examined. However, in blood group A secretors, the distribution was heterogeneous, i.e., in some granules only H antigen was demonstrated, whereas in others both A antigens and a small amount of H antigens were detected. Among the blood group-nonspecific lectins, wheat germ agglutinin (WGA) was found to bind more preferentially to immature SG than to mature SG. This was demonstrated irrespective of the blood group and secretor status of the tissue donor, except that in blood group A secretors WGA bound strongly to some mature SG which possessed A antigen. We discuss the significance of cellular and subcellular mosaic distribution of blood group antigens in connection with morphological differences of secretory granules and the maturation cycle of mucous cells.

scholarly journals Blockade of invariant TCR-CD1d interaction specifically inhibits antibody production against blood group A carbohydrates

Blood ◽  
2013 ◽  
Vol 122 (15) ◽  
pp. 2582-2590 ◽  
Author(s):  
Hirofumi Tazawa ◽  
Toshimitsu Irei ◽  
Yuka Tanaka ◽  
Yuka Igarashi ◽  
Hirotaka Tashiro ◽  
...  
Keyword(s):  
Peripheral Blood Mononuclear Cell ◽  
Blood Group ◽  
Mononuclear Cell ◽  
Antibody Production ◽  
Peripheral Blood ◽  
Human Peripheral Blood ◽  
Peripheral Blood Mononuclear ◽  
Blood Group A ◽  
Key Points ◽  
Group A

Key PointsAdministration of anti-mouse CD1d blocking mAb prior to A-RBC immunization abolished IL-5 production and anti-A Ab production in mice. In human peripheral blood mononuclear cell–NOD/SCID mice, administration of anti-human CD1d mAb prior to A-RBC immunization completely inhibited anti-A Ab production.

scholarly journals Inhibition of the Transcription Factor RUNX1 Causes Glycosyltransferase a Repression

Blood ◽  
2017 ◽  
Vol 130 (Suppl_1) ◽  
pp. 925-925
Author(s):  
Romy Kronstein-Wiedemann ◽  
Laura Schmidt ◽  
Jörn Lausen ◽  
Erhard Seifried ◽  
Torsten Tonn
Keyword(s):  
Transcription Factor ◽  
Transcription Factors ◽  
Blood Group ◽  
Receptor Expression ◽  
Abo Blood Group ◽  
Blood Group Antigens ◽  
Hematopoietic Stem ◽  
Blood Group A ◽  
Homozygous Genotype ◽  
Group A

Abstract Background: The ABO blood group system is unequivocally the most important in clinical transfusion medicine. Furthermore ABO is implicated in the development of a number of human diseases. The ABO antigens are not confined to RBCs but are widely expressed in a variety of human cells and tissues. Thus, ABO matching is critical not only in blood transfusion but also in cell, tissue and organ transplantation. The molecular genetic basis of the ABO system has been known since 1990. However, despite extensive investigations about regulation of ABO blood group receptor expression, the mechanism is not fully resolved. Previously we found that miRNAs plays a critical role in regulation of ABO blood group antigen. Numerous miRNAs which were up- or downregulated in RBCs of blood group O and of heterozygous genotypes as compared to homozygous genotype possess potential binding sites in the 3'UTR of several transcription factors, such as SP1 and RUNX1. Here we show that silencing of the transcription factor RUNX1 leads to downregulation of blood group A antigen. Methods: We performed knockdown experiments for RUNX1 by lentiviral gene transfer of shRNA in primary hematopoietic stem cells (HSCs) and analyzed blood group A-antigen expression using different method, including flow cytometry, western blot and qPCR. Result: Knockdown of RUNX1 in HSCs leads to a 10-20% reduction of blood group A positive erythroid cells and a 30-40% reduction of blood group A antigens per cell in differentiated RBCs. Furthermore, microarray analysis showed a significant increase of miR-215-5p and miR-192-5p in RBCs of blood group O as compared to homozygous genotype. RUNX1 is known to be a target gene for these miRNAs. Conclusion: Glycosyltransferase A and B expression is regulated by different miRNAs, via simultaneously targeting of the transcription factors SP1 and Runx1 and glycosyltransferase A and B mRNA. The knowledge of the role of microRNAs and the transcription factors SP1 and RUNX1 in the expression of blood group antigens may be extended to other blood groups (Rhesus, Kell, Duffy) and may open the door for therapeutic interventions in diseases where blood group receptors promote disease pathology. Disclosures No relevant conflicts of interest to declare.

Sign in / Sign up

Export Citation Format

Share Document