scholarly journals The structure of a family 110 glycoside hydrolase provides insight into the hydrolysis of α-1,3-galactosidic linkages in λ-carrageenan and blood group antigens

2020 ◽  
Vol 295 (52) ◽  
pp. 18426-18435
Author(s):  
Bailey E. McGuire ◽  
Andrew G. Hettle ◽  
Chelsea Vickers ◽  
Dustin T. King ◽  
David J. Vocadlo ◽  
...  
Keyword(s):  
Blood Group ◽  
Catalytic Mechanism ◽  
Glycoside Hydrolases ◽  
Structural Basis ◽  
Blood Group Antigens ◽  
Genes Encoding ◽  
Tissue Antigens ◽  
Marine Algal ◽  
Group B ◽  
Insight Into

α-Linked galactose is a common carbohydrate motif in nature that is processed by a variety of glycoside hydrolases from different families. Terminal Galα1–3Gal motifs are found as a defining feature of different blood group and tissue antigens, as well as the building block of the marine algal galactan λ-carrageenan. The blood group B antigen and linear α-Gal epitope can be processed by glycoside hydrolases in family GH110, whereas the presence of genes encoding GH110 enzymes in polysaccharide utilization loci from marine bacteria suggests a role in processing λ-carrageenan. However, the structure–function relationships underpinning the α-1,3-galactosidase activity within family GH110 remain unknown. Here we focus on a GH110 enzyme (PdGH110B) from the carrageenolytic marine bacterium Pseudoalteromonas distincta U2A. We showed that the enzyme was active on Galα1–3Gal but not the blood group B antigen. X-ray crystal structures in complex with galactose and unhydrolyzed Galα1–3Gal revealed the parallel β-helix fold of the enzyme and the structural basis of its inverting catalytic mechanism. Moreover, an examination of the active site reveals likely adaptations that allow accommodation of fucose in blood group B active GH110 enzymes or, in the case of PdGH110, accommodation of the sulfate groups found on λ-carrageenan. Overall, this work provides insight into the first member of a predominantly marine clade of GH110 enzymes while also illuminating the structural basis of α-1,3-galactoside processing by the family as a whole.

scholarly journals Human Group C Rotavirus VP8*s Recognize Type A Histo-Blood Group Antigens as Ligands

2018 ◽  
Vol 92 (11) ◽  
Author(s):  
Xiaoman Sun ◽  
Lihong Wang ◽  
Jianxun Qi ◽  
Dandi Li ◽  
Mengxuan Wang ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Binding Site ◽  
Blood Group ◽  
Specific Interaction ◽  
Type A ◽  
Host Susceptibility ◽  
Structural Basis ◽  
Receptor Interaction ◽  
Blood Group Antigens ◽  
Group Species

ABSTRACTGroup/species C rotaviruses (RVCs) have been identified as important pathogens of acute gastroenteritis (AGE) in children, family-based outbreaks, as well as animal infections. However, little is known regarding their host-specific interaction, infection, and pathogenesis. In this study, we performed serial studies to characterize the function and structural features of a human G4P[2] RVC VP8* that is responsible for the host receptor interaction. Glycan microarrays demonstrated that the human RVC VP8* recognizes type A histo-blood group antigens (HBGAs), which was confirmed by synthetic glycan-/saliva-based binding assays and hemagglutination of red blood cells, establishing a paradigm of RVC VP8*-glycan interactions. Furthermore, the high-resolution crystal structure of the human RVC VP8* was solved, showing a typical galectin-like structure consisting of two β-sheets but with significant differences from cogent proteins of group A rotaviruses (RVAs). The VP8* in complex with a type A trisaccharide displays a novel ligand binding site that consists of a particular set of amino acid residues of the C-D, G-H, and K-L loops. RVC VP8* interacts with type A HBGAs through a unique mechanism compared with that used by RVAs. Our findings shed light on the host-virus interaction and the coevolution of RVCs and will facilitate the development of specific antivirals and vaccines.IMPORTANCEGroup/species C rotaviruses (RVCs), members ofReoviridaefamily, infect both humans and animals, but our knowledge about the host factors that control host susceptibility and specificity is rudimentary. In this work, we characterized the glycan binding specificity and structural basis of a human RVC that recognizes type A HBGAs. We found that human RVC VP8*, the rotavirus host ligand binding domain that shares only ∼15% homology with the VP8* domains of RVAs, recognizes type A HBGA at an as-yet-unknown glycan binding site through a mechanism distinct from that used by RVAs. Our new advancements provide insights into RVC-cell attachment, the critical step of virus infection, which will in turn help the development of control and prevention strategies against RVs.

scholarly journals Histochemical reactivity of the Geodia cydonium agglutinin (GCA) in human tissues.

1991 ◽  
Vol 39 (4) ◽  
pp. 491-505 ◽  
Author(s):  
M Vierbuchen ◽  
G Uhlenbruck ◽  
F G Hanisch ◽  
W E Müller ◽  
M Ortmann ◽  
...  
Keyword(s):  
Binding Site ◽  
Blood Group ◽  
Lectin Binding ◽  
Blood Group Antigens ◽  
Group Status ◽  
Geodia Cydonium ◽  
Group A ◽  
Complex Carbohydrates ◽  
Group B ◽  
Inhibition Studies

We applied a peroxidase-antiperoxidase technique to study the distribution pattern and binding characteristics of the lectin from the marine sponge Geodia cydonium (Geodia cydonium agglutinin; GCA) in various human tissues. This lectin has been shown to possess a broad reactivity, but there was a distinct distribution of binding sites within the different organs. In the histochemical system GCA displayed no blood group specificity and labeled red blood cells, the vascular endothelium, and epithelial cells showing blood group antigen expression independent of the ABH blood group status. However, inhibition of GCA reactivity by simple sugars and complex carbohydrates demonstrated tissue-specific differences of lectin binding related to the ABH blood group status of the tissue and revealed information on the structural requirements of the histological lectin binding site. Tissues that totally lacked blood group antigens or that expressed only the H-antigen disclosed a GCA reactivity which was completely inhibited by lactose. In contrast, tissues that expressed blood group A- or blood group B-antigen exhibited a lactose-resistant lectin binding which was inhibited only by water-soluble blood group substance A from peptone A and by bovine glycophorin but not by other complex carbohydrates, including human glycophorin and human asialoglycophorin. Competitive inhibition studies in situ revealed that GCA binding was not inhibited by blood group type I/II carbohydrate sequence-specific lectins or by lectins with other sugar specificities. Inhibition by lactose of GCA binding to some histological sites indicates that the binding site consists of a beta-linked galactose-containing disaccharide. However, periodate oxidation of tissue sections had no effect on lectin binding, pointing to a subterminal location of the relevant sequence. The results obtained from inhibition studies with simple saccharides and complex carbohydrates in relation to the expression of ABH blood group antigens suggest a complex lectin combining site(s) in histological specimens. The lectin may possess either one binding site with a range of affinities for different carbohydrates (besides beta-linked disaccharides the GCA binding site accommodates to carbohydrate determinants carrying the blood group A or blood group B determinant), or may possess two different binding sites. Besides an acceptor site for beta-linked disaccharides, an additional binding site may exist accommodating to extended carbohydrate sequences related to A or B blood group structures. In conclusion, GCA represents a blood group-nonspecific lectin whose binding affinities are determined by the ABH blood group status of the tissue.

scholarly journals IMMUNOLOGICAL STUDIES IN ULCERATIVE COLITIS

1965 ◽  
Vol 122 (6) ◽  
pp. 1075-1086 ◽  
Author(s):  
Sten Hammarström ◽  
Rutger Lagercrantz ◽  
Peter Perlmann ◽  
Bengt E. Gustafsson
Keyword(s):  
Ulcerative Colitis ◽  
Blood Group ◽  
Hemagglutination Inhibition ◽  
Fluorescent Antibody ◽  
Slight Reduction ◽  
Blood Group Antigens ◽  
Antibody Staining ◽  
Human Sera ◽  
Group B ◽  
Germfree Rats

Sera from patients with ulcerative colitis contain antibodies which hemagglutinate sheep red cells, sensitized with phenol-water extracts from. colon, cecum, or feces of germfree rats. Minor concentrations of such antibodies are also present in a certain fraction of normal human sera. Hemagglutination and hemagglutination inhibition experiments with human erythrocytes and with the rat extracts showed that the latter contained an antigen similar to human blood group A antigen. In contrast, a blood group B-like antigen could not be detected in these extracts. However, experiments with eel serum indicated that these extracts also contained an antigen similar to the H antigen of the human ABO system. Absorption of ulcerative colitis sera with human A1 erythrocytes but not that with B or O erythrocytes gave, in a few cases, a slight reduction of the hemagglutinating titers against rat cecum-sensitized sheep erythrocytes. In contrast, this treatment considerably reduced such titers when found in sera from healthy persons or from patients with unrelated diseases. It could be concluded that the rat extracts also contained a "colon" antigen, detected with antibodies, present at elevated titers, in the sera of ulcerative colitis patients, but not in those of the controls. This colon antigen is immunologically distinct from the blood group antigens studied. Hemagglutination inhibition experiments indicated that A, H and colon antigen were widely distributed throughout the gastrointestinal tract of the germfree rats. The colon antigen was found to be enriched in the extracts from colon, cecum, and feces. Fluorescent antibody staining provided evidence that both the colon antigen and the A antigen were present in similar sites of the colon and cecum mucosa, particularly in goblet cells of the crypts, and in the mucus.

scholarly journals Association of ABO and Rh Blood Group Phenotypes with Type 2 Diabetes Mellitus at Felege Hiwot Comprehensive Referral Hospital Bahir Dar, Northwest Ethiopia

2020 ◽  
Vol 2020 ◽  
pp. 1-9
Author(s):  
Biruk Legese ◽  
Molla Abebe ◽  
Alebachew Fasil
Keyword(s):  
Diabetes Mellitus ◽  
Type 2 Diabetes ◽  
Type 2 Diabetes Mellitus ◽  
Blood Group ◽  
Blood Groups ◽  
Blood Group Antigens ◽  
Chi Square ◽  
Group B ◽  
Rh Blood Group

Background. ABO and Rh blood group antigens are thought to be among genetic determinants of type 2 diabetes mellitus. Identification of blood group phenotypes are more associated with type 2 diabetes mellitus. It will be helpful for individuals who are susceptible blood groups to take care of themselves by avoiding other predisposing factors and taking preventive measures. Methods. Hospital-based comparative cross-sectional study was carried out from February to April 2019 at Felege Hiwot Comprehensive Referral Hospital. Sociodemographic and clinical data were collected with a semistructured pretested questionnaire. ABO and Rh Blood group were determined by slide and test tube methods. Biochemical parameters were determined with Mindray BS-200E fully automated clinical chemistry analyzer. Data were analyzed by IBM SPSS version 20 statistical software. Chi-square test and logistic regression analysis were employed for data analysis. A P value of < 0.05 was considered statistically significant. Results. From a total of 424 participants included for this study, blood group O was found higher in frequency with 74 (34.9%) and 97 (45.75%) for cases and healthy controls, respectively. ABO blood groups showed significant association with T2DM, a chi-square value of 12.163 and P value of 0.007. However, the Rh blood group was not associated with T2DM. Binary logistic regression analysis revealed that blood group B had a higher risk (OR: 2.12, 95% CI: 1.33-3.32) and blood group O had decreased risk (OR: 0.636, 95% CI: 0.43-0.94) of T2DM as compared to other blood groups. Conclusion. ABO blood group antigens showed significant association with type 2 diabetes mellitus. Blood group B was associated with an increased risk and O blood group with decreased risk of type 2 diabetes mellitus.

Synthetic Peptide Mimotopes of blood Group Antigens for Red Cell Antibody Screening

Blood ◽  
2008 ◽  
Vol 112 (11) ◽  
pp. 291-291
Author(s):  
Evelyn J A Tait ◽  
Robin Fraser ◽  
Michael Moss ◽  
Stanislaw J Urbaniak
Keyword(s):  
Blood Group ◽  
Test System ◽  
Blood Group Antigens ◽  
Optimal Test ◽  
Screening Assay ◽  
Antibody Screening ◽  
Random Peptide ◽  
Antibody Recognition ◽  
Genes Encoding ◽  
Clinically Significant

Abstract Background: Antibody screening is performed both routinely in the blood group typing procedures for donors and patients and in more detail as part of special investigations for transfusion-dependent patients such as those suffering from Sickle Cell Disease and Thalassaemia. However, despite the care taken, intrinsic limitations of traditional serological diagnostic tests mean that alloimmunisation of pregnant women and multiply transfused patient may still go undetected, resulting in Hemolytic Disease of the Newborn or Hemolytic Transfusion Reactions, respectively. Furthermore, although the genes encoding the majority of blood group antigens have been characterised, the expression of recombinant gene products and the subsequent determination of protein structure that might lead to novel diagnostic reagents have proved more difficult to achieve. Methods: Phage Display libraries that express random peptide sequences (~1015) on the virion surface were screened using a series of monoclonal antibodies and an anti-RhD polyclonal preparation to identify peptides that mimic epitopes of clinically important blood group antigens. The peptides thus identified, were then synthesised in macroarrays and evaluated using SPOTs (Simple Precise Optimal Test system) in a step towards development of a novel diagnostic antibody-screening assay. Results: The combined approach of phagepeptide display and SPOTs proved powerful. From 490 phage-peptides selected by biopanning, 86 mimotopes bound their cognate antibody in SPOTs assays and represented the clinically important blood group antigens RhD (including epitopes 1.1, 3.1 and 6.3), RhE, Rhe, Fya and Fyb. These peptides ranged in size from 7 to 15 residues and included 7-mers that were constrained at their termini by a di-sulphide bridge. Further SPOTs analyses showed 26 of these phage-peptides (12 RhD, 3 RhE, 1 Rhe, 2 Fya and 8 Fyb) have the appropriate strength of signal and binding specificity for inclusion in any future diagnostic antibody-screening assay. A subset of these peptides has been further tested. These peptides were immobilised on polystyrene microspheres and shown to specifically bind their cognate antibodies in both (1) monoplex gel agglutination immunoassays and (2) microsphere-based, multiplex suspension arrays. Conclusions: We have shown that, regardless of whether or not the mimotopes resemble the original antigen sequence, they bind their cognate antibodies specifically and are therefore genuine mimics of the natural antigenic epitopes. It has also been demonstrated that the context in which a peptide is presented is fundamentally important for antibody recognition. The value of the phage-peptide approach in identifying mimotopes to clinically significant blood group antigens has also been established. Moreover, these peptides could be used in a single, comprehensive screening assay and eliminate many of the problems associated with agglutination assays and may herald the possibility of a synthetic, diagnostic array for routine antibody screening for all patients and donors and patients in the near future.

scholarly journals Structural Basis for Norovirus Inhibition by Human Milk Oligosaccharides

2016 ◽  
Vol 90 (9) ◽  
pp. 4843-4848 ◽  
Author(s):  
Stefan Weichert ◽  
Anna Koromyslova ◽  
Bishal K. Singh ◽  
Satoko Hansman ◽  
Stefan Jennewein ◽  
...  
Keyword(s):  
Human Milk ◽  
Blood Group ◽  
Structural Basis ◽  
Blood Group Antigens ◽  
Human Milk Oligosaccharides ◽  
Milk Oligosaccharides ◽  
X Ray ◽  
X Ray Crystallography ◽  
Naturally Occurring

Histo-blood group antigens (HBGAs) are important binding factors for norovirus infections. We show that two human milk oligosaccharides, 2′-fucosyllactose (2′FL) and 3-fucosyllactose (3FL), could block norovirus from binding to surrogate HBGA samples. We found that 2′FL and 3FL bound at the equivalent HBGA pockets on the norovirus capsid using X-ray crystallography. Our data revealed that 2′FL and 3FL structurally mimic HBGAs. These results suggest that 2′FL and 3FL might act as naturally occurring decoys in humans.

Structural basis for red cell phenotypic changes in newly identified, naturally occurring subgroup mutants of the human blood group B glycosyltransferase

Transfusion ◽  
2007 ◽  
Vol 47 (5) ◽  
pp. 864-875 ◽  
Author(s):  
Bahram Hosseini-Maaf ◽  
James A. Letts ◽  
Mattias Persson ◽  
Elizabeth Smart ◽  
Pierre-Yves LePennec ◽  
...  
Keyword(s):  
Blood Group ◽  
Human Blood ◽  
Structural Basis ◽  
Red Cell ◽  
Phenotypic Changes ◽  
Human Blood Group ◽  
Naturally Occurring ◽  
Group B

ABO Blood Groups And Their Link With The Risk of Pre-Eclampsia

BioSight ◽  
2020 ◽  
Vol 1 (1) ◽  
pp. 21-25
Author(s):  
Sana Shahid ◽  
Syed Sadia Fatima ◽  
Seema Ghani
Keyword(s):  
Blood Group ◽  
Tertiary Care ◽  
Fetal Mortality ◽  
Blood Group Antigens ◽  
Care Hospital ◽  
Multiple Risk Factors ◽  
Associated Conditions ◽  
Group B ◽  
Blood Grouping ◽  
Distressing Condition

ABO blood group antigens have been identified as pathological agent in different disease conditions. For some time, the association of blood group with pregnancy associated conditions like pre-eclampsia is extensively under debate. Preeclampsia is a distressing condition of pregnancy which commonly causes maternal and fetal mortality around the globe. Multiple risk factors are found to be associated with preeclamptic occurrence. In this study our aim was to delineate a specific blood group which could be implicated as a risk factor for pre-eclampsia. Methods: This retrospective study was conducted in a tertiary care hospital of Karachi and retrieved obstetric data including blood group was from medical record files of 368 patients. Obtained data was analyzed by IBM SPSS version 21. Results: The prevalence of B group was recorded to be 41.3% as compared to O (26.1%), A (22.8%) and AB (9.8%). So, it can be concluded that women having blood group B are more prone to develop pre-eclampsia. Conclusion: Blood grouping of pregnant women in early weeks of pregnancy could assist in prediction or better management of pre-eclampsia.

Antibody response to group B streptococcus type III and AB blood group antigens induced by pneumococcal vaccine

1981 ◽  
Vol 98 (3) ◽  
pp. 374-378 ◽  
Author(s):  
Kenneth M. Boyer ◽  
Jutharat Theeravuthichai ◽  
Lawrence C. Vogel ◽  
Armando Orlina ◽  
Samuel P. Gotoff
Keyword(s):  
Antibody Response ◽  
Blood Group ◽  
Pneumococcal Vaccine ◽  
Group B Streptococcus ◽  
Blood Group Antigens ◽  
Type Iii ◽  
Group B

scholarly journals Genotypic and Alelicas Frequencies of the ABO and Rh Systems in the State of Rio Grande Do Norte, Northeast of Brazil

Blood ◽  
2019 ◽  
Vol 134 (Supplement_1) ◽  
pp. 4990-4990
Author(s):  
Linduarte Varela Morais ◽  
Aldair Sousa Paiva ◽  
Valéria SF Sales ◽  
Geraldo Barroso Cavalcanti
Keyword(s):  
Blood Group ◽  
Blood Donors ◽  
Conflicts Of Interest ◽  
Statistical Significance ◽  
Cross Sectional Study ◽  
Blood Group Antigens ◽  
Chi Square ◽  
Cross Sectional ◽  
Chi Square Test ◽  
Group B

Objective: To determine the immunophenotyping of a population of blood donors, intended to build a database for transfusion medicine. 2) To make available to patients with chronic diseases that are systematically dependent on blood transfusions as compatible as possible in ABH, Rh (DCcEe) and Kell 1 antigen systems. Method: A cross-sectional study was carried out on 11,664 blood donors for the ABH system typing and of these, 1255 blood donors were selected randomly for the determination of blood group antigens of the Rh system and Kell antigen. Blood centrifugation methods, centrifuge hemolysis tube test and indirect Coombs test were used for blood typing. The results obtained were compared by the Chi-square test. A level of statistical significance of p ≤ 0.05 was considered. Results: Antigenic frequencies for the ABH system found: the frequency found for the blood group O 48.8%, the frequency found for the blood group A 35.4%; the frequency found for the blood group B 10.6% and the frequency found for the blood group AB 3.2%. In the Rh-Hr system the most frequent antigens found: e 94.5%, D 88.9%; c 80.6; C 56.4%; E 26.3%. For the Kell antigen, the frequency found was 6.7%. The most frequent phenotypes found were DCcee 23.3%; ddccee 18.1%, DCCee 16.7%; Dccee 11.0%; DCcEe 10.2% and DccEe 8.8%. The lowest frequency was found: DCcEE 0.64% and ddCcEe 0.08% Conclusion: The antigenic and phenotypic frequencies found show the great importance and necessity of the immunophenotyping of these antigens of blood groups in order to transfuse them, making them as compatible as possible, thus reducing the risk of alloimmunization. Due to the great miscegenation of our population, we find different frequencies in each region, making initiatives in this regard more relevant. Disclosures No relevant conflicts of interest to declare.

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