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1.
BMC Public Health ; 21(1): 2262, 2021 12 11.
Artículo en Inglés | MEDLINE | ID: mdl-34895179

RESUMEN

BACKGROUND: A cross-sectional study was performed to examine life satisfaction differences between university students from nine countries during the first wave of the COVID-19 pandemic. A cross-national comparison of the association between life satisfaction and a set of variables was also conducted. METHODS: Participants in the study were 2349 university students with a mean age of 23 years (M = 23.15, SD = 4.66). There was a predominance of women (69.26%) and individuals studying at the bachelor level (78%). The research was conducted between May and July 2020 in nine countries: Slovenia (n=209), the Czech Republic (Czechia)(n=308), Germany (n=267), Poland (n=301), Ukraine (n=310), Russia (n=285), Turkey (n=310), Israel (n=199), and Colombia (n=153). Participants completed an online survey involving measures of satisfaction with life (SWLS), exposure to COVID-19, perceived negative impact of coronavirus (PNIC) on students' well-being, general self-reported health (GSRH), physical activity (PA), and some demographics (gender, place of residence, level of study). A one-way ANOVA was used to explore cross-national differences in life satisfaction. The χ2 independence test was performed separately in each country to examine associations between life satisfaction and other variables. Bivariate and multivariate logistic regressions were used to identify life satisfaction predictors among a set of demographic and health-related variables in each of the nine countries. RESULTS: The level of life satisfaction varied between university students from the nine countries. The results for life satisfaction and the other variables differed between countries. Numerous associations were noted between satisfaction with life and several variables, and these showed cross-national differences. Distinct predictors of life satisfaction were observed for each country. However, poor self-rated physical health was a predictor of low life satisfaction independent of the country. CONCLUSIONS: The association between life satisfaction and subjective assessment of physical health seems to be universal, while the other variables are related to cross-cultural differences. Special public health attention should be focused on psychologically supporting people who do not feel healthy.


Asunto(s)
COVID-19 , Adulto , Estudios Transversales , Humanos , Pandemias , Satisfacción Personal , SARS-CoV-2 , Universidades , Adulto Joven
2.
Chembiochem ; 20(2): 131-133, 2019 01 18.
Artículo en Inglés | MEDLINE | ID: mdl-30019804

RESUMEN

Agglutination of red blood cells (RBCs) remains the only practical method for routine use for ABH typing in clinical practice. However, exact mechanistic details of agglutination are not yet thoroughly studied. In this research, RBCs of blood group O were converted to blood group A through two approaches: by chemical ligation of the cells' glycocalyx with synthetic blood group A tetrasaccharide, and by insertion of synthetic glycolipid carrying the same A antigen into the cells' membranes. The O→A ligated RBCs and natural A RBCs showed comparable agglutination characteristics with antibodies. As expected, RBCs with inserted glycolipid showed lower agglutination scores. This approach could help cell biologists in site-specific and cell-friendly modification of glycocalyx by other ligands.


Asunto(s)
Sistema del Grupo Sanguíneo ABO/metabolismo , Eritrocitos/metabolismo , Humanos , Ligandos , Estructura Molecular
3.
Biochem Biophys Res Commun ; 470(1): 168-174, 2016 Jan 29.
Artículo en Inglés | MEDLINE | ID: mdl-26773500

RESUMEN

Human Gb3/CD77 synthase (α1,4-galactosyltransferase, P(k) synthase), encoded by A4GALT gene, is known for synthesis of Gal(α1-4)Gal moiety in globotriaosylceramide (Gb3Cer, CD77, P(k) blood group antigen), a glycosphingolipid of the globo series. Recently, it was shown that c.631C > G mutation in A4GALT, which causes p.Q211E substitution in the open reading frame of the enzyme, broadens the enzyme specificity, making it able also to synthesize Gal(α1-4)GalNAc moiety, which constitutes the defining terminal disaccharide of the NOR antigen (carried by two glycosphingolipids: NOR1 and NOR2). Terminal Gal(α1-4)Gal disaccharide is also present in another glycosphingolipid blood group antigen, called P1, which together with P(k) and NOR comprises the P1PK blood group system. Despite several attempts, it was never clearly shown that P1 antigen is synthesized by Gb3/CD77 synthase, leaving open an alternative hypothesis that there are two homologous α1,4-galactosyltransferases in humans. In this study, using recombinant Gb3/CD77 synthase produced in insect cells, we show that the consensus enzyme synthesizes both the P(k) and P1 antigens, while its p.Q211E variant additionally synthesizes the NOR antigen. This is the first direct biochemical evidence that Gb3/CD77 synthase is able to synthesize two different glycosphingolipid antigens: P(k) and P1, and when p.Q211E substitution is present, the NOR antigen is also synthesized.


Asunto(s)
Aminoácidos/química , Antígenos Nucleares/biosíntesis , Galactosiltransferasas/química , Galactosiltransferasas/metabolismo , Aminoácidos/metabolismo , Animales , Antígenos Nucleares/química , Sitios de Unión , Línea Celular , Activación Enzimática , Estabilidad de Enzimas , Insectos , Unión Proteica , Células Sf9 , Spodoptera , Relación Estructura-Actividad , Especificidad por Sustrato
4.
Biopolymers ; 105(11): 787-94, 2016 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-27388774

RESUMEN

A rapid and simple method of biofunctionalising nylon, cellulose acetate, and polyvinyl butyral electrospun nanofibers with blood group glycans was achieved by preparing function-spacer-lipid constructs and simply contacting them to fibers with a piezo inkjet printer. A series of water dispersible amphipathic glycan-spacer constructs were synthesized representing a range ABO and related blood group antigens. After immediate contact of the amphipathic glycan-spacer constructs with nanofiber surfaces they self-assembled and were detectable by enzyme immunoassays with high sensitivity and specificity.


Asunto(s)
Sistema del Grupo Sanguíneo ABO/química , Carbohidratos/química , Nanofibras/química , Humanos
5.
Transfusion ; 56(2): 325-33, 2016 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-26589374

RESUMEN

BACKGROUND: Lewis serologic reagents frequently give inaccurate phenotyping results. Furthermore these serologic reagents are often used in nonserologic assays such as inhibition and immunohistochemistry. In both scenarios knowledge of the fine specificity and cross-reactivity of these reagents will improve the quality of results obtained. STUDY DESIGN AND METHODS: A range of contemporary and historical workshop and developmental Lewis reagents including mouse monoclonal (MoAb) and human and goat polyclonal (PoAb) reagents were evaluated. All were evaluated both against Lewis kodecytes expressing only single Le(a) , Le(b) , ALe(b) , BLe(b) , Le(x) , Le(y) , ALe(y) , or BLe(y) antigens and against the same antigens inkjet printed on a paper-based microplate and analyzed by enzyme immunoassay. Nine clinical samples were also evaluated. A kodecyte antigen dilution sensitivity assay was used to establish the ratio of Le(b) antigen between group A1 /A2 and O RBCs. RESULTS: A continuum of cross-reactivity from Le(x) through to H was observed with MoAbs. All PoAb and few MoAb anti-Le(a) samples and reagents cross-reacted to some degree with Le(b) antigen. Some PoAb and MoAb anti-Le(b) did not cross-react with Le(a) . All polyclonal goat anti-Le(b) reagents showed substantial activity against ALe(b) and BLe(b) , while no MoAb reagent had this activity. A1 RBCs had less than half the Le(b) antigen of A2 /O RBCs. CONCLUSIONS: Substantial cross-reactivity of both MoAbs and PoAbs with related antigens highlights the risks of using serologic reagents in nonserologic assays or against synthetic antigens. The lack of ALe(b) activity in anti-Le(b) MoAbs explains their poor performance against blood group A1 Le(a-b+) phenotypes.


Asunto(s)
Anticuerpos Monoclonales de Origen Murino/química , Especificidad de Anticuerpos , Tipificación y Pruebas Cruzadas Sanguíneas/métodos , Antígenos del Grupo Sanguíneo de Lewis/sangre , Animales , Anticuerpos Monoclonales de Origen Murino/inmunología , Línea Celular , Reacciones Cruzadas , Humanos , Antígenos del Grupo Sanguíneo de Lewis/inmunología , Ratones
6.
Int J Mol Sci ; 17(1)2016 Jan 16.
Artículo en Inglés | MEDLINE | ID: mdl-26784187

RESUMEN

The ability to glycosylate surfaces has medical and diagnostic applications, but there is no technology currently recognized as being able to coat any surface without the need for prior chemical modification of the surface. Recently, a family of constructs called function-spacer-lipids (FSL) has been used to glycosylate cells. Because it is known that lipid-based material can adsorb onto surfaces, we explored the potential and performance of cell-labelling FSL constructs to "glycosylate" non-biological surfaces. Using blood group A antigen as an indicator, the performance of a several variations of FSL constructs to modify a large variety of non-biological surfaces was evaluated. It was found the FSL constructs when optimised could in a few seconds glycosylate almost any non-biological surface including metals, glass, plastics, rubbers and other polymers. Although the FSL glycan coating was non-covalent, and therefore temporary, it was sufficiently robust with appropriate selection of spacer and surface that it could capture anti-glycan antibodies, immobilize cells (via antibody), and withstand incubation in serum and extensive buffer washing, making it suitable for diagnostic and research applications.


Asunto(s)
Materiales Biocompatibles Revestidos/química , Polisacáridos/química , Adhesión Celular , Materiales Biocompatibles Revestidos/farmacología , Eritrocitos/efectos de los fármacos , Eritrocitos/fisiología , Glicosilación , Humanos , Nanofibras/química
7.
Glycobiology ; 25(7): 726-34, 2015 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-25681326

RESUMEN

A major aspect of carbohydrate-dependent galectin functionality is their cross-linking capacity. Using a cell surface as biorelevant platform for galectin binding and a panel of 40 glycans as sensor part of a fluorescent polyacrylamide neoglycopolymer for profiling galectin reactivity, properties of related proteins can be comparatively analyzed. The group of the chicken galectins (CGs) is an especially suited system toward this end due to its relatively small size, compared with mammalian galectins. The experiments reveal particularly strong reactivity toward N-acetyllactosamine repeats for all tested CGs and shared reactivity of CG-1A and CG-2 to histo-blood group ABH determinants. In cross-species comparison, CG-1B's properties closely resembled those of human galectin-1, as was the case for the galectin-2 (but not galectin-3) ortholog pair. Although binding-site architectures are rather similar, reactivity patterns can well differ.


Asunto(s)
Glicoconjugados/metabolismo , Lectinas/metabolismo , Polisacáridos/metabolismo , Secuencia de Aminoácidos , Animales , Secuencia de Carbohidratos , Línea Celular , Pollos , Glicoconjugados/química , Humanos , Lectinas/química , Datos de Secuencia Molecular , Polisacáridos/química , Homología de Secuencia de Aminoácido
8.
Transfusion ; 55(1): 129-36, 2015 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-25039359

RESUMEN

BACKGROUND: The FORS blood group system (originally recognized as the Apae phenotype) was discovered by sporadic activity against polyclonal anti-A reagents and activity against the lectin Helix pomatia. The extent of monoclonal anti-A reagent activity against the FORS1 antigen is serologically and immunochemically incomplete. STUDY DESIGN AND METHODS: In the absence of natural FORS1-positive red blood cells (RBCs), kodecytes were created with synthetic disaccharide and pentasaccharide Forssman function-spacer-lipid (FSL) constructs, Fsdi -kodecytes, and FORS1-kodecytes, respectively. FSL constructs were also applied to solid surfaces and used in solid-phase enzyme immunoassays. A range of characterized monoclonal anti-A and anti-B reagents were then serologically and immunochemically characterized against these Forssman antigens. Polyclonal human anti-A, anti-B, the lectin H. pomatia serologic reagents; and canine RBCs were used as serologic controls. RESULTS: None of 19 different monoclonal anti-A reagents were able to detect the pentasaccharide Forssman on FORS1-kodecytes, while three reagents were able to detect disaccharide Forssman on Fsdi -kodecytes. Most anti-A reagents were immunochemically reactive with both the di- and the pentasaccharide Forssman antigens in the solid-phase assays. Historic polyclonal human anti-A and the lectin H. pomatia reacted strongly with the FORS1-kodecytes, correlating with the discovery of the Apae phenotype and supporting the use of FORS1-kodecytes as FORS1 surrogates. CONCLUSIONS: Monoclonal anti-A reagents, despite showing reactivity against the FORS1 antigen in solid-phase assays are unlikely to cause the agglutination of FORS1 antigen-positive RBCs.


Asunto(s)
Anticuerpos Heterófilos/inmunología , Anticuerpos Monoclonales/inmunología , Antígeno de Forssman/análisis , Oligosacáridos/análisis , Animales , Reacciones Antígeno-Anticuerpo , Secuencia de Carbohidratos , Disacáridos/inmunología , Perros , Membrana Eritrocítica/química , Membrana Eritrocítica/inmunología , Antígeno de Forssman/inmunología , Globósidos/inmunología , Humanos , Técnicas para Inmunoenzimas , Lectinas/inmunología , Membrana Dobles de Lípidos/química , Membranas Artificiales , Datos de Secuencia Molecular , Estructura Molecular , Oligosacáridos/inmunología , Fosfatidiletanolaminas , Polisacáridos/inmunología
9.
Transfusion ; 54(10): 2477-84, 2014 Oct.
Artículo en Inglés | MEDLINE | ID: mdl-24749871

RESUMEN

BACKGROUND: Monoclonal (MoAb) reagents are routinely used and are usually very reliable for the serologic determination of ABO blood types. However, the fine specificity and cross-reactivity of these reagents are often unknown, particularly against synthetic antigens used in some diagnostic assays. If nonserologic assays or very sensitive techniques other than those specifically prescribed by the manufacturer are used, then there is a risk of incorrect interpretation of results. STUDY DESIGN AND METHODS: Forty-seven MoAbs and two polyclonal ABO reagents were tested against red blood cell (RBC) kodecytes prepared with A trisaccharide, A Type 1, A Type 2, A Type 3, A Type 4, B trisaccharide, B Type 1, B Type 2, acquired B trisaccharide, and Le(a) trisaccharide function-spacer-lipid (FSL) constructs. Natural RBCs were tested in parallel. In addition these FSL constructs were printed onto paper with a desktop inkjet printer and used in a novel immunoassay that identifies reactivity through the appearance of alphanumeric characters. RESULTS: Mapping of MoAbs with kodecytes and printed FSL constructs revealed a series of broad recognition patterns. All ABO MoAbs tested were reactive with the RBC dominant Type 2 ABO antigens. Unexpectedly some anti-A reagents were reactive against the B Type 1 antigen, while others were poorly reactive with trisaccharide antigens. CONCLUSIONS: All ABO MoAbs detect the RBC dominant Type 2 ABO antigens; however, some reagents may show minor reactivity with inappropriate blood group antigens, which needs to be considered when using these reagents in alternative or highly sensitive analytic systems.


Asunto(s)
Sistema del Grupo Sanguíneo ABO/inmunología , Anticuerpos Monoclonales/inmunología , Especificidad de Anticuerpos , Tipificación y Pruebas Cruzadas Sanguíneas/instrumentación , Tipificación y Pruebas Cruzadas Sanguíneas/métodos , Eritrocitos/inmunología , Reacciones Cruzadas , Mapeo Epitopo/instrumentación , Mapeo Epitopo/métodos , Eritrocitos/citología , Humanos , Inmunoensayo/instrumentación , Inmunoensayo/métodos , Indicadores y Reactivos , Lípidos/farmacología , Papel , Tiras Reactivas , Pruebas Serológicas/instrumentación , Pruebas Serológicas/métodos
10.
Biomolecules ; 13(8)2023 07 26.
Artículo en Inglés | MEDLINE | ID: mdl-37627231

RESUMEN

The recruitment of leukocytes from blood is one of the most important cellular processes in response to tissue damage and inflammation. This multi-step process includes rolling leukocytes and their adhesion to endothelial cells (EC), culminating in crossing the EC barrier to reach the inflamed tissue. Galectin-8 and galectin-9 expressed on the immune system cells are part of this process and can induce cell adhesion via binding to oligolactosamine glycans. Similarly, these galectins have an order of magnitude higher affinity towards glycans of the ABH blood group system, widely represented on ECs. However, the roles of gal-8 and gal-9 as mediators of adhesion to endothelial ABH antigens are practically unknown. In this work, we investigated whether H antigen-gal-9-mediated adhesion occurred between Jurkat cells (of lymphocytic origin and known to have gal-9) and EA.hy 926 cells (immortalized endothelial cells and known to have blood group H antigen). Baseline experiments showed that Jurkat cells adhered to EA.hy 926 cells; however when these EA.hy 926 cells were defucosylated (despite the unmasking of lactosamine chains), adherence was abolished. Restoration of fucosylation by insertion of synthetic glycolipids in the form of H (type 2) trisaccharide Fucα1-2Galß1-4GlcNAc restored adhesion. The degree of lymphocyte adhesion to native and the "H-restored" (glycolipid-loaded) EA.hy 926 cells was comparable. If this gal-9/H (type 2) interaction is similar to processes that occur in vivo, this suggests that only the short (trisaccharide) H glycan on ECs is required.


Asunto(s)
Sistema del Grupo Sanguíneo ABO , Células Endoteliales , Humanos , Galectinas , Glucolípidos , Células Jurkat , Endotelio
11.
Glycobiology ; 22(9): 1207-17, 2012 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-22547138

RESUMEN

Adhesion/growth-regulatory galectins (gals) exert their functionality by the cis/trans-cross-linking of distinct glycans after initial one-point binding. In order to define the specificity of ensuing association events leading to cross-linking, we recently established a cell-based assay using fluorescent glycoconjugates as flow cytometry probes and tested it on two human gals (gal-1 and -3). Here we present a systematic study of tandem-repeat-type gal-4, -8 and -9 loaded on Raji cells resulting in the following key insights: (i) all three gals bound to oligolactosamines; (ii) binding to ligands with Galß1-3GlcNAc or Galß1-3GalNAc as basic motifs was commonly better than that to canonical Galß1-4GlcNAc; (iii) all three gals bound to 3'-O-sulfated and 3'-sialylated disaccharides mentioned above better than that to parental neutral forms and (iv) histo-blood group ABH antigens were the highest affinity ligands in both the cell and the solid-phase assay. Fine specificity differences were revealed as follows: (i) gal-8 and -9, but not gal-4, bound to disaccharide Galß1-3GlcNAc; (ii) increase in binding due to negatively charged substituents was marked only in the case of gal-4 and (iii) gal-4 and -8 bound preferably to histo-blood group A glycans, whereas gal-9 targeted B-type glycans. Experiments with single carbohydrate recognition domains (CRDs) of gal-4 showed that the C-CRD preferably bound to ABH glycans, whereas the N-CRD associated with oligolactosamines. In summary, the comparative analysis disclosed the characteristic profiles of glycan reactivity for the accessible CRD of cell-bound gals. These results indicate the distinct sets of functionality for these three members of the same subgroup of human gals.


Asunto(s)
Amino Azúcares/química , Linfocitos B/química , Galectina 4/química , Galectinas/química , Polisacáridos/química , Sistema del Grupo Sanguíneo ABO/química , Sistema del Grupo Sanguíneo ABO/metabolismo , Amino Azúcares/metabolismo , Linfocitos B/citología , Linfocitos B/metabolismo , Sitios de Unión , Bioensayo , Secuencia de Carbohidratos , Línea Celular , Colorantes Fluorescentes , Galectina 4/metabolismo , Galectinas/metabolismo , Glicoconjugados/química , Glicoconjugados/metabolismo , Humanos , Datos de Secuencia Molecular , Polisacáridos/metabolismo , Unión Proteica , Proteínas Recombinantes/química , Proteínas Recombinantes/metabolismo , Electricidad Estática
12.
Transfusion ; 52(4): 860-9, 2012 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-21981750

RESUMEN

BACKGROUND: According to Landsteiner's law, alloantibodies are prevalent and autoantibodies are absent in the ABO blood group system. However, one study (Spalter et al., Blood 1999;93:4418-24) has suggested that low-affinity ABO autoantibodies, mitigated by anti-idiotypic immunoglobulins are also prevalent, while another publication (Rieben et al., Eur J Immunol 1992;22:2713-7) shows that humans do not have B-lymphocytes capable of producing immunoglobulin G ABO autoantibodies. STUDY DESIGN AND METHODS: We used hapten-specific chromatography to isolate allo- and autoantibodies from pools of A or B serum and then characterized the resultant antibodies against a wide range of ABO and related glycoconjugates. RESULTS: We found that the apparent autoantibodies are directed against blood group A or B disaccharides, without consideration for the presence of fucose, but requiring the absence of elongating sugar X in composition of Gal(NAc)α1-3(Fucα1-2)Galß1-X-terminated carbohydrate chain. In contrast, ABO alloantibodies required a minimum trisaccharide Gal(NAc)α1-3(Fucα1-2)Gal epitope and recognize the elongated type-specific tetrasaccharides. Furthermore, alloantibodies appear to be a small set of specific yet crossreactive antibodies that detect all backbone types of A or B antigens, rather than being a collection of specific antibodies, each of which detects a different type of A or B antigen. CONCLUSION: Apparent ABO autoantibodies appear to have no natural human target.


Asunto(s)
Sistema del Grupo Sanguíneo ABO/inmunología , Autoanticuerpos/inmunología , Epítopos , Isoanticuerpos/inmunología , Adulto , Autoanticuerpos/aislamiento & purificación , Humanos , Isoanticuerpos/aislamiento & purificación , Polisacáridos/metabolismo
13.
Cardiology ; 121(1): 59-70, 2012.
Artículo en Inglés | MEDLINE | ID: mdl-22398380

RESUMEN

OBJECTIVES: Intracoronary administration of glycosaminoglycan analogs, including the complement inhibitor dextran sulfate, attenuates myocardial ischemia/reperfusion injury (I/R injury). However, dextran sulfate has a distinct anticoagulatory effect, possibly limiting its use in specific situations in vivo. We therefore developed multimeric tyrosine sulfate (sTyr-PAA), a novel, minimally anticoagulatory, fully synthetic non-carbohydrate-containing polyacrylamide conjugate, for in vivo testing in an acute closed-chest porcine model of acute myocardial infarction. METHODS: Following balloon occlusion of the left anterior descending artery just after the first diagonal branch (60-minute ischemia), sTyr-PAA (approx. 10 mg/kg bodyweight, fraction with strongest complement-inhibitory and minimal anticoagulatory properties, n = 11) or phosphate-buffered saline (controls, n = 9) was administered intracoronarily into ischemic myocardium prior to 120 min of reperfusion. RESULTS: sTyr-PAA significantly reduced infarct size (from 61.0 ± 12.0% of the ischemic area at risk to 39.4 ± 17.0%), plasma creatine kinase, local complement deposition and tissue factor upregulation, without affecting systemic coagulation. Protection was associated with significantly reduced myocardial neutrophil extravasation and translated into a significant improvement of ejection fraction and left ventricular enddiastolic pressure. CONCLUSIONS: sTyr-PAA protected significantly against myocardial I/R injury without substantially affecting systemic coagulation. Local intravascular sTyr-PAA administration may prove advantageous in situations where bleeding complications are likely or are to be avoided at all costs.


Asunto(s)
Anticoagulantes/farmacología , Inactivadores del Complemento/farmacología , Infarto del Miocardio/complicaciones , Daño por Reperfusión Miocárdica/prevención & control , Tirosina/análogos & derivados , Animales , Vía Clásica del Complemento/efectos de los fármacos , Citoprotección/efectos de los fármacos , Relación Dosis-Respuesta a Droga , Granulocitos/patología , Hemodinámica/efectos de los fármacos , Infarto del Miocardio/inmunología , Reperfusión Miocárdica , Daño por Reperfusión Miocárdica/inmunología , Daño por Reperfusión Miocárdica/patología , Neutrófilos/patología , Sus scrofa , Tromboplastina/metabolismo , Tirosina/farmacología , Fibrilación Ventricular/inducido químicamente
14.
Analyst ; 136(3): 560-9, 2011 Feb 07.
Artículo en Inglés | MEDLINE | ID: mdl-21107457

RESUMEN

Glycan-binding antibodies form a significant subpopulation of both natural and acquired antibodies and play an important role in various immune processes. They are for example involved in innate immune responses, cancer, autoimmune diseases, and neurological disorders. In the present study, a microsphere-based flow-cytometric immunoassay (suspension array) was applied for multiplexed detection of glycan-binding antibodies in human serum. Several approaches for immobilization of glycoconjugates onto commercially available fluorescent microspheres were compared, and as the result, the design based on coupling of end-biotinylated glycopolymers has been selected. This method requires only minute amounts of glycans, similar to a printed glycan microarray. The resulting glyco-microspheres were used for detection of IgM and IgG antibodies directed against ABO blood group antigens. The possibility of multiplexing this assay was demonstrated with mixtures of microspheres modified with six different ABO related glycans. Multiplexed detection of anti-glycan IgM and IgG correlated well with singleplex assays (Pearson's correlation coefficient r = 0.95-0.99 for sera of different blood groups). The suspension array in singleplex format for A/B trisaccharide, H(di) and Le(x) microspheres corresponded well to the standard ELISA (r > 0.94). Therefore, the described method is promising for rapid, sensitive, and reproducible detection of anti-glycan antibodies in a multiplexed format.


Asunto(s)
Citometría de Flujo/métodos , Inmunoensayo/métodos , Inmunoglobulina G/sangre , Inmunoglobulina M/sangre , Polisacáridos/inmunología , Sistema del Grupo Sanguíneo ABO/inmunología , Ensayo de Inmunoadsorción Enzimática , Glicoconjugados/química , Humanos , Microesferas , Reproducibilidad de los Resultados
15.
J Clin Med ; 10(23)2021 Nov 26.
Artículo en Inglés | MEDLINE | ID: mdl-34884266

RESUMEN

This study aimed to reveal differences in exposure to coronavirus disease (COVID-19) during the first (W1) and the second (W2) waves of the pandemic in six countries among university students and to show the prevalence and associations between exposure to COVID-19 and coronavirus-related post-traumatic stress syndrome (PTSD) risk during W2. The repeated cross-sectional study was conducted among university students from Germany, Poland, Russia, Slovenia, Turkey, and Ukraine (W1: n = 1684; W2: n = 1741). Eight items measured exposure to COVID-19 (regarding COVID-19 symptoms, testing, hospitalizing quarantine, infected relatives, death of relatives, job loss, and worsening economic status due to the COVID-19 pandemic). Coronavirus-related PTSD risk was evaluated by PCL-S. The exposure to COVID-19 symptoms was higher during W2 than W1 among students from all countries, except Germany, where, in contrast, the increase in testing was the strongest. Students from Poland, Turkey, and the total sample were more frequently hospitalized for COVID-19 in W2. In these countries, and Ukraine, students were more often in quarantine. In all countries, participants were more exposed to infected friends/relatives and the loss of a family member due to COVID-19 in W2 than W1. The increase in job loss due to COVID-19 was only noted in Ukraine. Economic status during W2 only worsened in Poland and improved in Russia. This was due to the significant wave of restrictions in Russia and more stringent restrictions in Poland. The prevalence of coronavirus-related PTSD risk at three cutoff scores (25, 44, and 50) was 78.20%, 32.70%, and 23.10%, respectively. The prediction models for different severity of PTSD risk differed. Female gender, a prior diagnosis of depression, a loss of friends/relatives, job loss, and worsening economic status due to the COVID-19 were positively associated with high and very high coronavirus-related PTSD risk, while female gender, a prior PTSD diagnosis, experiencing COVID-19 symptoms, testing for COVID-19, having infected friends/relatives and worsening economic status were associated with moderate risk.

16.
Biochim Biophys Acta Biomembr ; 1863(9): 183645, 2021 09 01.
Artículo en Inglés | MEDLINE | ID: mdl-34019901

RESUMEN

Modification of the cell surface with synthetic glycolipids opens up a wide range of possibilities for studying the function of glycolipids. Synthetic glycolipids called Function-Spacer-Lipids (FSL; where F is a glycan or label, S is a spacer, and L is dioleoylphosphatidyl ethanolamine) easily and controllably modify the membrane of a living cells. This current study investigates the dynamics and mechanism of the FSL insertion and release/loss. FSL insert into the cell membrane (~1 million molecules per cell) within tens of minutes, almost regardless of the nature of the cells (including the thickness of their glycocalyx) and the size of the FSL glycan. FSLs do not accumulate uniformly, but instead form patches >300 nm in size either entrapped in the glycocalyx, or integrated in the plane of the plasma membrane, but always outside the cell rafts. The natural release (loss) of FSL from the modified cell was two orders of magnitude slower than attachment/insertion and occurred mainly in the form of released microvesicles with a size of 140 ± 5 nm. The accumulation of FSL as patches in the cell membrane is similar to the coalescence of natural glycosphingolipids and supports (along with their long residence time in the membrane) the use of FSL as probes for the study of glycosphingolipid-protein interactions.


Asunto(s)
Membrana Celular/química , Glucolípidos/química , Células Cultivadas , Glucolípidos/síntesis química , Humanos , Estructura Molecular
17.
J Clin Med ; 10(13)2021 Jun 29.
Artículo en Inglés | MEDLINE | ID: mdl-34209619

RESUMEN

The mental health of young adults, particularly students, is at high risk during the COVID-19 pandemic. The purpose of this study was to examine differences in mental health between university students in nine countries during the pandemic. The study encompassed 2349 university students (69% female) from Colombia, the Czech Republic (Czechia), Germany, Israel, Poland, Russia, Slovenia, Turkey, and Ukraine. Participants underwent the following tests: Patient Health Questionnaire (PHQ-8), Generalized Anxiety Disorder (GAD-7), Exposure to COVID-19 (EC-19), Perceived Impact of Coronavirus (PIC) on students' well-being, Physical Activity (PA), and General Self-Reported Health (GSRH). The one-way ANOVA showed significant differences between countries. The highest depression and anxiety risk occurred in Turkey, the lowest depression in the Czech Republic and the lowest anxiety in Germany. The χ2 independence test showed that EC-19, PIC, and GSRH were associated with anxiety and depression in most of the countries, whereas PA was associated in less than half of the countries. Logistic regression showed distinct risk factors for each country. Gender and EC-19 were the most frequent predictors of depression and anxiety across the countries. The role of gender and PA for depression and anxiety is not universal and depends on cross-cultural differences. Students' mental health should be addressed from a cross-cultural perspective.

18.
Sci Rep ; 11(1): 18644, 2021 09 20.
Artículo en Inglés | MEDLINE | ID: mdl-34545120

RESUMEN

The student population has been highly vulnerable to the risk of mental health deterioration during the coronavirus disease (COVID-19) pandemic. This study aimed to reveal the prevalence and predictors of mental health among students in Poland, Slovenia, Czechia, Ukraine, Russia, Germany, Turkey, Israel, and Colombia in a socioeconomic context during the COVID-19 pandemic. The study was conducted among 2349 students (69% women) from May-July 2020. Data were collected by means of the Generalized Anxiety Disorder (GAD-7), Patient Health Questionnaire (PHQ-8), Perceived Stress Scale (PSS-10), Gender Inequality Index (GII), Standard & Poor's Global Ratings, the Oxford COVID-19 Government Response Tracker (OxCGRT), and a sociodemographic survey. Descriptive statistics and Bayesian multilevel skew-normal regression analyses were conducted. The prevalence of high stress, depression, and generalized anxiety symptoms in the total sample was 61.30%, 40.3%, and 30%, respectively. The multilevel Bayesian model showed that female sex was a credible predictor of PSS-10, GAD-7, and PHQ-8 scores. In addition, place of residence (town) and educational level (first-cycle studies) were risk factors for the PHQ-8. This study showed that mental health issues are alarming in the student population. Regular psychological support should be provided to students by universities.


Asunto(s)
COVID-19/epidemiología , COVID-19/psicología , Salud Mental , Pandemias , Estudiantes/psicología , Universidades , Trastornos de Ansiedad/epidemiología , Trastornos de Ansiedad/psicología , Teorema de Bayes , Depresión/epidemiología , Depresión/psicología , Femenino , Geografía , Humanos , Masculino , Análisis Multinivel , Prevalencia , Análisis de Regresión , Estrés Psicológico/epidemiología , Estrés Psicológico/psicología
19.
Glycoconj J ; 27(3): 321-7, 2010 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-20195900

RESUMEN

Influenza virus neuraminidase inhibitors (NAIs), currently used as anti-influenza drugs, can lead to the appearance of drug-resistant variants. Resistance to NAIs appears due to mutations in the active site of the neuraminidase (NA) molecule that decrease the NA enzymatic activity and sometimes in the hemagglutinin (HA) that decrease its affinity for cell receptors and, therefore, reduce the requirement for NA activity in releasing mature virions from infected cells. Using a set of sialo-oligosaccharides, we evaluated changes in the receptor-binding specificity of the HA and substrate specificity of the NA of influenza B viruses that had acquired resistance to NAIs. The oligosaccharide specificity of two pairs of field influenza B viruses, namely: i) B/Memphis/20/96 and its NAI-resistant variant, B/Memphis/20-152K/96, containing mutation R152K in the NA and 5 amino acid substitutions in the HA1, and ii) B/Hong Kong/45/2005 and its NAI-resistant variant B/Hong Kong/36/2005, containing a single R371K mutation in the NA, was evaluated. Wild type viruses bound strictly to a "human type" receptor, alpha2-6-sialo-oligosaccharide 6;SLN, but desialylated it is approximately 8 times less efficiently than the alpha2-3 sialosaccharides. Both drug-resistant viruses demonstrated the ability to bind to "avian type" receptors, alpha2-3 sialo-oligosaccharides (such as 3;SLN), whereas their affinity for 6;SLN was noticeably reduced in comparison with corresponding wild type viruses. Thus, the development of the NAI resistance in the studied influenza B viruses was accompanied by a readjustment of HA-NA oligosaccharide specificities.


Asunto(s)
Hemaglutininas/metabolismo , Virus de la Influenza B/efectos de los fármacos , Virus de la Influenza B/enzimología , Neuraminidasa/antagonistas & inhibidores , Neuraminidasa/metabolismo , Animales , Antivirales/farmacología , Línea Celular , Perros , Farmacorresistencia Viral/genética , Hemaglutininas/química , Hemaglutininas/genética , Virus de la Influenza B/genética , Neuraminidasa/química , Neuraminidasa/genética , Estructura Secundaria de Proteína , Reacción en Cadena de la Polimerasa de Transcriptasa Inversa , Especificidad por Sustrato
20.
ChemistryOpen ; 9(6): 640, 2020 06.
Artículo en Inglés | MEDLINE | ID: mdl-32499989

RESUMEN

Invited for this month's cover is the group of Prof. Nicolai Bovin from the Russian Academy of Sciences. The cover picture shows how a biotin residue initially hidden in a monolayer formed on the surface of a material by biot-CMG-DOPE (see top left) is pulled out of the layer by the streptavidin molecule (Str) that has come close to it (see below). This can be considered as a model of certain events (in particular, cis protein-ligand interactions) occurring on the surface of a living cell when it is necessary to hide the ligand from undesirable interactions, but leave the possibility of its recognition by a high-affinity protein. The picture is inspired by the legendary Yellow Submarine cartoon. Read the full text of their Full Paper at https://doi.org/10.1002/open.201900276.

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