The Experts below are selected from a list of 3726 Experts worldwide ranked by ideXlab platform
G. Herrler - One of the best experts on this subject based on the ideXlab platform.
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Importance of cholesterol for infection of cells by Transmissible Gastroenteritis Virus
Virus research, 2008Co-Authors: Xiaofeng Ren, Christel Schwegmann-wessels, Joerg Glende, Jiechao Yin, G. HerrlerAbstract:In this study, we addressed the question whether cholesterol is important for Transmissible Gastroenteritis Virus (TGEV), a porcine coronaVirus, in the initiation of an infection. We found that cholesterol depletion from the cellular membrane by methyl-β-cyclodextrin (MβCD) significantly impaired the efficiency of TGEV infection. Infectivity was also reduced after depleting cholesterol from the viral envelope. This finding is surprising because coronaViruses bud from a pre-Golgi compartment which is expected to be low in cholesterol compared to the plasma membrane. Addition of exogenous cholesterol resulted in a restoration of the infectivity confirming our conclusion that efficient TGEV infection requires cholesterol in both the viral and the cellular membranes. Our data raise the possibility that the viral and cellular proteins involved in the entry process may be associated with cholesterol-rich membrane microdomains.
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Transmissible Gastroenteritis Virus infection: a vanishing specter.
DTW. Deutsche tierarztliche Wochenschrift, 2006Co-Authors: Christel Schwegmann-wessels, G. HerrlerAbstract:About twenty years ago, a new coronaVirus, porcine respiratory coronaVirus (PRCoV), was detected in swine herds. This Virus is related to Transmissible Gastroenteritis Virus (TGEV); however, it is not enteropathogenic but causes only minor respiratory symptoms. As PRCoV shares some epitopes for neutralizing antibodies with TGEV, it acts like a nature-made vaccine against TGEV resulting in a drastic reduction of TGE outbreaks in Europe. A major difference between the two porcine coronaViruses is a large deletion in the surface protein S gene of PRCoV. Because of this structural difference, TGEV but not PRCoV has a sialic acid binding activity that allows the attachment to mucins and mucin-type glycoproteins. The sialic acid binding activity may allow TGEV to overcome the mucus barrier in the gut and to get access to the intestinal epithelium for initiation of infection.
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Isolation of hemagglutination-defective mutants for the analysis of the sialic acid binding activity of Transmissible Gastroenteritis Virus.
Advances in experimental medicine and biology, 1998Co-Authors: C. Krempl, Luis Enjuanes, M. L. Ballesteros, G. HerrlerAbstract:The surface protein S of Transmissible Gastroenteritis Virus (TGEV) has a sialic acid binding activity that enables the Virus to agglutinate erythrocytes. A protocol is described that has been successfully applied to the isolation of hemgglutination-defective mutants. The potential of these mutants for the characterization of the sialic acid-binding site and the function of the binding activity is discussed.
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Analysis of the Sialic Acid-Binding Activity of Transmissible Gastroenteritis Virus
Advances in experimental medicine and biology, 1995Co-Authors: Beate Schultze, Luis Enjuanes, G. HerrlerAbstract:Porcine Transmissible Gastroenteritis Virus (TGEV) has been shown to agglutinate erythrocytes using a2,3-linked sialic acid on the cell surface as binding site. The hemagglutinating activity requires the pretreament of Virus with neuraminidase. We obtained evidence that TGEV recognizes not only N-acetylneuraminic acid but also N-glycoloylneuraminic acid, a sialic acid present on many porcine cells.
Luis Enjuanes - One of the best experts on this subject based on the ideXlab platform.
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immunogenic characterization and epitope mapping of Transmissible Gastroenteritis Virus rna dependent rna polymerase
Journal of Virological Methods, 2011Co-Authors: Aitor Nogales, Luis Enjuanes, Carmen Galan, Silvia Marquezjurado, Monica Garciagallo, Leonor Kremer, Fernando AlmazanAbstract:CoronaVirus RNA synthesis is a sophisticated process performed by a viral multienzymatic replicase complex, together with cellular factors. A key enzyme of this replication complex is the RNA dependent RNA polymerase (RdRp). To study the replication of coronaVirus genome, six monoclonal antibodies (mAbs) specific for Transmissible Gastroenteritis Virus (TGEV) RdRp were generated and characterized. His-tagged RdRp was expressed in baculoVirus, purified and used as immunogen to produce mAbs. The TGEV RdRp was recognized by these mAbs in the context of Virus infection by immunofluorescence analysis and Western blot. Epitope mapping by Pepscan indicated that RdRp mAbs recognized four non-overlapping linear epitopes located in a 62-amino acid region of the N-terminal domain, suggesting that this region may constitute an immunodominant domain. The availability of TGEV RdRp mAbs will be instrumental to study coronaVirus replication and to analyze the function of RdRp in pathogenesis.
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Recombinant Canine CoronaViruses Related to Transmissible Gastroenteritis Virus of Swine Are Circulating in Dogs
Journal of virology, 2008Co-Authors: Nicola Decaro, Luis Enjuanes, Viviana Mari, Marco Campolo, Alessio Lorusso, Michele Camero, Gabriella Elia, Vito Martella, Paolo Cordioli, Canio BuonavogliaAbstract:Four canine coronaVirus type II (CCoV-II) strains were identified in the guts and internal organs of pups which had died of acute Gastroenteritis. The CCoV-II strains were strictly related to porcine Transmissible Gastroenteritis Virus (TGEV) in the N-terminal domain of the spike protein, whereas in the other parts of the genome, a higher genetic relatedness to recent CCoV-II isolates was observed. Experimental infection of dogs with a TGEV-like isolate induced mild Gastroenteritis without any systemic involvement. By Virus neutralization tests, antigenic differences between reference and TGEV-like CCoVs were found. Our data support the potential recombinant origin of the TGEV-like CCoVs.
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Isolation of hemagglutination-defective mutants for the analysis of the sialic acid binding activity of Transmissible Gastroenteritis Virus.
Advances in experimental medicine and biology, 1998Co-Authors: C. Krempl, Luis Enjuanes, M. L. Ballesteros, G. HerrlerAbstract:The surface protein S of Transmissible Gastroenteritis Virus (TGEV) has a sialic acid binding activity that enables the Virus to agglutinate erythrocytes. A protocol is described that has been successfully applied to the isolation of hemgglutination-defective mutants. The potential of these mutants for the characterization of the sialic acid-binding site and the function of the binding activity is discussed.
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Analysis of the Sialic Acid-Binding Activity of Transmissible Gastroenteritis Virus
Advances in experimental medicine and biology, 1995Co-Authors: Beate Schultze, Luis Enjuanes, G. HerrlerAbstract:Porcine Transmissible Gastroenteritis Virus (TGEV) has been shown to agglutinate erythrocytes using a2,3-linked sialic acid on the cell surface as binding site. The hemagglutinating activity requires the pretreament of Virus with neuraminidase. We obtained evidence that TGEV recognizes not only N-acetylneuraminic acid but also N-glycoloylneuraminic acid, a sialic acid present on many porcine cells.
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Antigenic structure of Transmissible Gastroenteritis Virus nucleoprotein.
Virology, 1992Co-Authors: J. M. Martin Alonso, D.j. Garwes, Luis Enjuanes, Milagros Balbín, Santiago Gascón, Francisco ParraAbstract:A group of 11 monoclonal antibodies (MAbs) raised against Transmissible Gastroenteritis Virus (TGEV) was used to study the antigenic structure of the Virus nucleoprotein (N). To identify the regions recognized by MAbs, DNA fragments derived from the N-coding region of the TGEV strain FS772/70 were cloned into pUR expression plasmids and the antigenicity of the resulting fusion proteins was analyzed by immunoblotting. A major antigenic domain was identified, covering the first 241 amino acid residues of N, within which an epitope (residues 57-117) was also found. A second antigenic domain extended from residues 175 to 360 of the nucleoprotein, within which a subsite was characterized within the region covering residues 241-349. MAb DA3 recognized a linear epitope which mapped within residues 360 and 382 at the carboxy terminus of the nucleoprotein. The binding of the majority of the MAbs (8 out of 11) to large fusions, but not to smaller fragments included in them, suggests a conformational dependence of the MAb binding sites. Our data show that the use of fusions in Western blot experiments is a useful approach to map not only linear epitopes but more complex antigenic structures found in the nucleoprotein of the TGEV.
C. Krempl - One of the best experts on this subject based on the ideXlab platform.
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Isolation of hemagglutination-defective mutants for the analysis of the sialic acid binding activity of Transmissible Gastroenteritis Virus.
Advances in experimental medicine and biology, 1998Co-Authors: C. Krempl, Luis Enjuanes, M. L. Ballesteros, G. HerrlerAbstract:The surface protein S of Transmissible Gastroenteritis Virus (TGEV) has a sialic acid binding activity that enables the Virus to agglutinate erythrocytes. A protocol is described that has been successfully applied to the isolation of hemgglutination-defective mutants. The potential of these mutants for the characterization of the sialic acid-binding site and the function of the binding activity is discussed.
Beate Schultze - One of the best experts on this subject based on the ideXlab platform.
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Analysis of the Sialic Acid-Binding Activity of Transmissible Gastroenteritis Virus
Advances in experimental medicine and biology, 1995Co-Authors: Beate Schultze, Luis Enjuanes, G. HerrlerAbstract:Porcine Transmissible Gastroenteritis Virus (TGEV) has been shown to agglutinate erythrocytes using a2,3-linked sialic acid on the cell surface as binding site. The hemagglutinating activity requires the pretreament of Virus with neuraminidase. We obtained evidence that TGEV recognizes not only N-acetylneuraminic acid but also N-glycoloylneuraminic acid, a sialic acid present on many porcine cells.
M. L. Ballesteros - One of the best experts on this subject based on the ideXlab platform.
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Isolation of hemagglutination-defective mutants for the analysis of the sialic acid binding activity of Transmissible Gastroenteritis Virus.
Advances in experimental medicine and biology, 1998Co-Authors: C. Krempl, Luis Enjuanes, M. L. Ballesteros, G. HerrlerAbstract:The surface protein S of Transmissible Gastroenteritis Virus (TGEV) has a sialic acid binding activity that enables the Virus to agglutinate erythrocytes. A protocol is described that has been successfully applied to the isolation of hemgglutination-defective mutants. The potential of these mutants for the characterization of the sialic acid-binding site and the function of the binding activity is discussed.
