Browsing
     by title


0-9 A B C D E F G H I J K L M N O P Q R S T U V W X Y Z

or enter first few letters:   
OK
Full Text
Peer Reviewed
See detailGlycoprotein Ib and integrin alphaIIbbeta3 contribute to GPVI-dependent vWF-collagen induced thrombus formation under flow
Kuijpers, Marijke; Oury, Cécile ULg; Schulte, V. et al

in Journal of Thrombosis and Haemostasis [=JTH] (2003)

Detailed reference viewed: 8 (2 ULg)
Full Text
Peer Reviewed
See detailGlycoprotein L disruption reveals two functional forms of the murine gammaherpesvirus 68 glycoprotein H.
Gillet, Laurent ULg; May, Janet S; Colaco, Susanna et al

in Journal of Virology (2007), 81(1), 280-91

The herpesvirus glycoprotein H (gH) and gL associate to form a heterodimer that plays a central role in virus-driven membrane fusion. When archetypal alpha- or betaherpesviruses lack gL, gH misfolds and ... [more ▼]

The herpesvirus glycoprotein H (gH) and gL associate to form a heterodimer that plays a central role in virus-driven membrane fusion. When archetypal alpha- or betaherpesviruses lack gL, gH misfolds and progeny virions are noninfectious. In order to define the role that gL plays in gamma-2 herpesvirus infections, we disrupted its coding sequence in murine gammaherpesvirus-68 (MHV-68). MHV-68 lacking gL folded gH into a conformation antigenically distinct from the form that normally predominates on infected cells. gL-deficient virions bound less well than the wild type to epithelial cells and fibroblasts. However, they still incorporated gH and remained infectious. The cell-to-cell spread of gL-deficient viruses was remarkably normal, as was infection, dissemination, and latency establishment in vivo. Viral membrane fusion was therefore gL independent. The major function of gL appeared to be allowing gH to participate in cell binding prior to membrane fusion. This function was most important for the entry of MHV-68 virions into fibroblasts and epithelial cells. [less ▲]

Detailed reference viewed: 19 (2 ULg)
Full Text
Peer Reviewed
See detailGlycoprotein L sets the neutralization profile of murid herpesvirus 4.
Gillet, Laurent ULg; Alenquer, Marta; Glauser, Daniel L et al

in Journal of General Virology (The) (2009), 90(Pt 5), 1202-14

Antibodies readily neutralize acute, epidemic viruses, but are less effective against more indolent pathogens such as herpesviruses. Murid herpesvirus 4 (MuHV-4) provides an accessible model for tracking ... [more ▼]

Antibodies readily neutralize acute, epidemic viruses, but are less effective against more indolent pathogens such as herpesviruses. Murid herpesvirus 4 (MuHV-4) provides an accessible model for tracking the fate of antibody-exposed gammaherpesvirus virions. Glycoprotein L (gL) plays a central role in MuHV-4 entry: it allows gH to bind heparan sulfate and regulates fusion-associated conformation changes in gH and gB. However, gL is non-essential: heparan sulfate binding can also occur via gp70, and the gB-gH complex alone seems to be sufficient for membrane fusion. Here, we investigated how gL affects the susceptibility of MuHV-4 to neutralization. Immune sera neutralized gL(-) virions more readily than gL(+) virions, chiefly because heparan sulfate binding now depended on gp70 and was therefore easier to block. However, there were also post-binding effects. First, the downstream, gL-independent conformation of gH became a neutralization target; gL normally prevents this by holding gH in an antigenically distinct heterodimer until after endocytosis. Second, gL(-) virions were more vulnerable to gB-directed neutralization. This covered multiple epitopes and thus seemed to reflect a general opening up of the gH-gB entry complex, which gL again normally restricts to late endosomes. gL therefore limits MuHV-4 neutralization by providing redundancy in cell binding and by keeping key elements of the virion fusion machinery hidden until after endocytosis. [less ▲]

Detailed reference viewed: 20 (1 ULg)
Full Text
Peer Reviewed
See detailLa glycoprotéine gE de l'herpèsvirus bovin de type 1 et les nouveaux vaccins marqués
Schynts, Frédéric; Lemaire, Mylène; Baranowski, Eric et al

in Annales de Médecine Vétérinaire (1998), 142

Detailed reference viewed: 15 (0 ULg)
Full Text
See detailLes glycoprotéines des herpèsvirus bovins 1 et 4
Thiry, Etienne ULg; Baranowski, Eric; Lomonte, Patrick et al

in El Hassane Diop, P.; Kaeckenbeeck, A. (Eds.) Biotechnologies du diagnostic et de la prévention des maldies animales (1994)

Detailed reference viewed: 54 (0 ULg)
Full Text
Peer Reviewed
See detailLes glycoproteines placentaires chez les mammiferes
Clerget, E.; Melo de Sousa, Noelita ULg; Bella, Amina ULg et al

in Annales d'Endocrinologie (2008), 69

Placental tissue exhibits a typical glycosylation pattern, which differs from that observed in the pituitary gland. Depending to the species and pregnancy period, the placenta synthesizes diverse ... [more ▼]

Placental tissue exhibits a typical glycosylation pattern, which differs from that observed in the pituitary gland. Depending to the species and pregnancy period, the placenta synthesizes diverse glycoproteins, some of which have significant hormonal activity, others being detected in maternal circulation. Thus, these molecules are of interest both from a fundamental and clinical point of view. Among the mammalian placental glycoproteins currently recognized, chorionic gonadotrophins from primates and Equidae, placental lactogen from bovines and the pregnancy-associated glycoproteins from ruminant species are particularly noteworthy. The diversity of saccharidic structures leads to multiple forms of placental glycoproteins exhibiting distinct structural and biological properties. For instance, concerning the chorionic gonadotrophins, the association of both alpha and beta subunits is essential for the binding of the hormone to specific receptors. Moreover, the N-linked oligossacharides are required for the activation of effectors systems. Bovine placental lactogen is a glycosylated hormone, exhibiting somatotropin- and prolactin-like activities. Several N-glycosylation sites confer to pregnancy-associated glycoproteins a long half-life (8-10 days) in maternal circulation. Assay of these molecules can be used for routine early pregnancy diagnosis and the follow-up of embryonic and fetal mortalities. [less ▲]

Detailed reference viewed: 170 (9 ULg)
Full Text
Peer Reviewed
See detailGlycoproteins of the aspartyl proteinase gene family secreted by the developing placenta
Roberts, R. M.; Xie, S.; Nagel, R. J. et al

in Advances in Experimental Medicine and Biology (1995)

Pregnancy in cattle and sheep can be diagnosed by the presence of placentally-derived antigens (pregnancy-associated glycoproteins or PAG-1) in maternal serum soon after implantation begins at about Day ... [more ▼]

Pregnancy in cattle and sheep can be diagnosed by the presence of placentally-derived antigens (pregnancy-associated glycoproteins or PAG-1) in maternal serum soon after implantation begins at about Day 20 following conception. Molecular cloning of their cDNA has revealed that PAG-1 belong to the aspartic proteinase gene family and have about 50% amino acid sequence identity to pepsin. However, critical amino acid substitutions at the active site regions suggest that both bovine and ovine PAG-1 are enzymatically inactive. PAG-1 expression has been shown by in situ hybridization and immunocytochemistry to be localized to the trophoblast binucleate cells, which invade maternal uterine endometrium during implantation. The glycoproteins are concentrated in dense cytoplasmic granules that are discharged after the binucleate cells have migrated to the maternal side of the placental barrier. We suggest, therefore, that the PAG-1 might have an endocrine function either as carriers of other bioactive peptides or by acting as hormones themselves. Recently screening of placental libraries with nucleic acid probes has identified additional cDNA that are very abundant and code for polypeptides (PAG-2 and PAG-3) related to, but antigenically and structurally distinct from PAG-1 described above. These molecules have sequences of amino acids at their catalytic centers that are consistent with their being potentially functional proteinases but their role during pregnancy, like that of PAG-1, is unclear. [less ▲]

Detailed reference viewed: 17 (1 ULg)
Full Text
Peer Reviewed
See detailGlycosaminoglycan interactions in murine gammaherpesvirus-68 infection.
Gillet, Laurent ULg; Adler, Heiko; Stevenson, Philip G

in PLoS ONE (2007), 2(4), 347

Glycosaminoglycans (GAGs) commonly participate in herpesvirus entry. They are thought to provide a reversible attachment to cells that promotes subsequent receptor binding. Murine gamma-herpesvirus-68 ... [more ▼]

Glycosaminoglycans (GAGs) commonly participate in herpesvirus entry. They are thought to provide a reversible attachment to cells that promotes subsequent receptor binding. Murine gamma-herpesvirus-68 (MHV-68) infection of fibroblasts and epithelial cells is highly GAG-dependent. This is a function of the viral gp150, in that gp150-deficient mutants are much less GAG-dependent than wild-type. Here we show that the major MHV-68 GAG-binding protein is not gp150 but gp70, a product of ORF4. Surprisingly, ORF4-deficient MHV-68 showed normal cell binding and was more sensitive than wild-type to inhibition by soluble heparin rather than less. Thus, the most obvious viral GAG interaction made little direct contribution to infection. Indeed, a large fraction of the virion gp70 had its GAG-binding domain removed by post-translational cleavage. ORF4 may therefore act mainly to absorb soluble GAGs and prevent them from engaging gp150 prematurely. In contrast to gp70, gp150 bound poorly to GAGs, implying that it provides little in the way of adhesion. We hypothesize that it acts instead as a GAG-sensitive switch that selectively activates MHV-68 entry at cell surfaces. [less ▲]

Detailed reference viewed: 15 (4 ULg)
Full Text
Peer Reviewed
See detailGlycosyl transferase activity of the Escherichia coli penicillin-binding protein 1b: Specificity profile for the substrate
Fraipont, Claudine ULg; Sapunaric, Frédéric ULg; Zervosen, Astrid ULg et al

in Biochemistry (2006), 45(12), 4007-4013

The glycosyl transferase of the Escherichia coli bifunctional penicillin-binding protein (PBP) 1b catalyzes the assembly of lipid-transported N-acetylglucosaminyl-beta-1,4-N-acetylmuramoyl-L-Ala-gamma-D ... [more ▼]

The glycosyl transferase of the Escherichia coli bifunctional penicillin-binding protein (PBP) 1b catalyzes the assembly of lipid-transported N-acetylglucosaminyl-beta-1,4-N-acetylmuramoyl-L-Ala-gamma-D-Glu-meso-A(2)pm-D-Ala-D-Ala units (lipid II) into linear peptidoglycan chains. These units are linked, at C1 of N-acetylmuramic acid (MurNAc), to a C-55 undecaprenyl pyrophosphate. In an in vitro assay, lipid II functions both as a glycosyl donor and as a glycosyl acceptor substrate. Using substrate analogues, it is suggested that the specificity of the enzyme for the glycosyl donor substrate differs from that for the acceptor. The donor substrate requires the presence of both N-acetylglucosamine (GlcNAc) and MurNAc and a reactive group on C1 of the MurNAc and does not absolutely require the lipid chain which can be replaced by uridine. The enzyme appears to prefer an acceptor substrate containing a polyprenyl pyrophosphate on C1 of the MurNAc sugar. The problem of glycan chain elongation that presumably proceeds by the repetitive addition of disaccharide peptide units at their reducing end is discussed. [less ▲]

Detailed reference viewed: 29 (9 ULg)
Full Text
Peer Reviewed
See detailThe Glycosylation of Bovine Pregnancy-Associated Glycoproteins Changes before Parturition
Klisch, K.; Herzog, K.; Feldmann, M. et al

in Reproduction in Domestic Animals (2006)

Detailed reference viewed: 18 (2 ULg)
Full Text
Peer Reviewed
See detailThe glycosylation of pregnancy-associated glycoproteins and prolactin-related protein-I in bovine binucleate trophoblast giant cells changes before parturition.
Klisch, Karl; Boos, A.; Friedrich, M. et al

in Reproduction (Cambridge, England) (2006), 132

Binucleate trophoblast giant cells (BNC) in the bovine placenta produce glycoproteins, which are delivered into the mother after fusion of BNC with uterine epithelial cells. During most time of pregnancy ... [more ▼]

Binucleate trophoblast giant cells (BNC) in the bovine placenta produce glycoproteins, which are delivered into the mother after fusion of BNC with uterine epithelial cells. During most time of pregnancy, BNC produce pregnancy-associated glycoproteins (PAGs) and prolactin-related protein-I (PRP-I) with asparagine-linked lactosamine-type glycans terminating with N-acetyl-galactosamine. We show by lectin histochemistry that terminal N-acetyl-galactosamine (detected by Dolichos biflorus agglutinin, DBA) in placentomal BNC is greatly reduced prior to parturition, while lactosamine-type N-glycans (detected by Phaseolus vulgaris leucoagglutinin, PHA-L) remain unaltered. The change in DBA-staining showed no statistically significant differences between placentomes of cows with and without retention of fetal membranes. Western blots revealed that, at parturition the apparent molecular mass of PAGs and PRP-I is 1-2 kDa lower than in late pregnancy. These changes are due to alterations of asparagine-linked glycans, since the molecular weight of the peptide backbones after enzymatical release of asparagine-linked glycans is identical at late pregnancy and parturition. Lectin western blots showed a reduction of terminal N-acetyl-galactosamine on PAGs at parturition. A lectin sandwich-ELISAwas used to differentiate DBA- and PHA-L-binding PAGs in sera of pregnant and non-pregnant cows. The values for DBA-binding PAGs at parturition were not significantly different from non-pregnancy, while the values for PHA-L-binding PAGs were significantly higher at parturition. The peripartal changes of PAG- and PRP-I-glycosylation could alter functional properties of these proteins and might therefore be considered for functional studies. The differentiation of PAG glycoforms in maternal serum could be valuable for a further optimization of PAG-based pregnancy diagnosis in cattle. [less ▲]

Detailed reference viewed: 16 (2 ULg)
Full Text
Peer Reviewed
See detailGlycosyltransferases encoded by viruses.
Markine-Goriaynoff, Nicolas; Gillet, Laurent ULg; Van Etten, James L et al

in Journal of General Virology (The) (2004), 85(Pt 10), 2741-54

Studies of cellular biology in recent decades have highlighted the crucial roles of glycans in numerous important biological processes, raising the concept of glycomics that is now considered as important ... [more ▼]

Studies of cellular biology in recent decades have highlighted the crucial roles of glycans in numerous important biological processes, raising the concept of glycomics that is now considered as important as genomics, transcriptomics and proteomics. For millions of years, viruses have been co-evolving with their hosts. Consequently, during this co-evolution process, viruses have acquired mechanisms to mimic, hijack or sabotage host processes that favour their replication, including mechanisms to modify the glycome. The importance of the glycome in the regulation of host-virus interactions has recently led to a new concept called 'glycovirology'. One fascinating aspect of glycovirology is the study of how viruses affect the glycome. Viruses reach that goal either by regulating expression of host glycosyltransferases or by expressing their own glycosyltransferases. This review describes all virally encoded glycosyltransferases and discusses their established or putative functions. The description of these enzymes illustrates several intriguing aspects of virology and provides further support for the importance of glycomics in biological processes. [less ▲]

Detailed reference viewed: 15 (1 ULg)
Full Text
See detailGMFS Final report Stage 1 and Stage 2
Gilliams, Sven; Bydekerke, Lieven; Delrue, Josefien et al

Report (2009)

Global Monitoring for Food Security (GMFS) is a Global Monitoring for Environment and Security (GMES) Service Element (GSE) project, part of the European Space Agency (ESA) contribution to the European ... [more ▼]

Global Monitoring for Food Security (GMFS) is a Global Monitoring for Environment and Security (GMES) Service Element (GSE) project, part of the European Space Agency (ESA) contribution to the European Union (EU) /ESA GMES Programme. GMFS aims to establish an operational service for crop monitoring in support of Food Security Monitoring to serve policy makers and operational users. The GMFS project started in March 2003 as part of Stage 1 of the ESA Earthwatch GMES services Element “Service Consolidation Actions”, and was continued in October 2005 as part of the Stage 2 of the ESA Earth watch GMES services Element – “Scaling Up Consolidated GMES Services”. In this document an overview is given of the work done throughout the previous six years. GMFS aimed at monitoring crop state /vegetation condition at continental and national scale. Low resolution Earth Observation (EO) data was used for monitoring purposes at continental scale, while at national scale products were based upon medium and high resolution data, field work and agro-meteorological models. The project was guided by a project strategy group with members from the United States Agency for International Development - Famine Early Warning System Network (USAID-FEWSNET), Directorate General for Development (DG-DEV), Consultative Group on International Agricultural Research - International Wheat Improvement Center (CGIAR-CIMMYT), European Commission Joint Research Center (EC-JRC), United Nations World Food Programme (WFP) and United Nations Food and Agricultural Organisation (FAO). The goal of the project in Stage 1 (March 2003 –November 2004) was to consolidate an early warning system for food security. This started off by an intensive literature review and setting up an initial service for the Centre de Suivi Ecologique (CSE) in Dakar Senegal. In the second Phase of Stage 1 activities focussed more on the actual service delivery and setting up activities with users. Those activities included the monitoring agricultural production for Senegal, monitoring agriculture in Malawi and giving support to the Crop and Food Supply Assessment Mission (CFSAM) of FAO /WFP. Additionally, services were set up for the centre Agro-Hydro-Météorologique (AGRHYMET) as a result of a meeting between AGHRYMET and Vlaamse Instelling voor Technologisch Onderzoek (VITO). During 2005 the early warning service was continued to support GMFS users although there was at that time no formal contract to do so. At the start of the Second Stage, in October 2005, a GMFS user executive board, consisting of one representative from: EC-JRC, FAO, WFP, Southern Africa Development Community Regional Remote Sensing Unit (SADC-RRSU), Regional Centre for Mapping of Resources for Development (RCMRD) and AGRHYMET, was set up to support the consortium in defining the correct services and to review the work. Since the focus for the Second Stage was on up scaling the consolidated services, it was decided that the early warning service and support to the CFSAM were to be continued, the agricultural mapping service was to be expanded to more countries - namely, Senegal, Sudan, Ethiopia, Malawi and Zimbabwe - and extra services on yield modeling using remote sensing and agro-meteorological models were to be provided. During the second year of this stage, the services were even more extended with, support to the Ministry of Agriculture and Meteorological Department in Mozambique, extra activities in Ethiopia and Sudan and support to the regional centers on operational use of the ESA Data Dissemination System (DDS). [less ▲]

Detailed reference viewed: 38 (0 ULg)
See detailGmsh
Geuzaine, Christophe ULg; Remacle, J.-F.

Scientific conference (2009, June 09)

Detailed reference viewed: 32 (0 ULg)
Full Text
See detailGmsh: a finite element mesh generator with built-in pre- and post-processing facilities
Geuzaine, Christophe ULg; Remacle, J.-F.

Software (1997)

Gmsh is a 3D finite element grid generator with a build-in CAD engine and post-processor. Its design goal is to provide a fast, light and user-friendly meshing tool with parametric input and advanced ... [more ▼]

Gmsh is a 3D finite element grid generator with a build-in CAD engine and post-processor. Its design goal is to provide a fast, light and user-friendly meshing tool with parametric input and advanced visualization capabilities. Gmsh is built around four modules: geometry, mesh, solver and post-processing. The specification of any input to these modules is done either interactively using the graphical user interface or in ASCII text files using Gmsh's own scripting language. See http://geuz.org/gmsh/ for more information. [less ▲]

Detailed reference viewed: 72 (5 ULg)
Peer Reviewed
See detailGmsh: a three-dimensional finite element mesh generator with built-in pre- and post-processing facilities
Geuzaine, Christophe ULg; Remacle, J.-F.

in Proceedings of the fourth international conference on advanced computational methods in engineering, ACOMEN 2008 (2008)

Detailed reference viewed: 18 (1 ULg)
Peer Reviewed
See detailGmsh: a three-dimensional finite element mesh generator with built-in pre- and post-processing facilities
Geuzaine, Christophe ULg; Remacle, J.-F.

in Proceedings of the 9th International Workshop on Finite Elements for Microwave Engineering (2008)

Detailed reference viewed: 9 (0 ULg)
Peer Reviewed
See detailGmsh: a three-dimensional finite element mesh generator with built-in pre- and post-processing facilities
Remacle, J.-F.; Geuzaine, Christophe ULg

in Proceedings of the 11th International Society of Grid Generation Conference (ISSG 2009) (2009)

Detailed reference viewed: 26 (0 ULg)
Full Text
Peer Reviewed
See detailGmsh: a three-dimensional finite element mesh generator with built-in pre- and post-processing facilities
Geuzaine, Christophe ULg; Remacle, Jean-François

in International Journal for Numerical Methods in Engineering (2009), 79(11), 1309-1331

Detailed reference viewed: 197 (14 ULg)