Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0017160 (gastroenteritis)
 11,398 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Transgenic plants represent an inexpensive alternative to classical fermentation systems for production of recombinant subunit vaccines. Transgenic potato plants were created that express the N-terminal domain of the glycoprotein S (N-gS) from Transmissible gastroenteritis coronavirus (TGEV), containing the major antigenic sites of the protein. Extracts from potato tubers expressing N-gS were inoculated intraperitoneally to mice, and the vaccinated mice developed serum IgG specific for TGEV. Furthermore, when potato tubers expressing N-gS were fed directly to mice, they developed serum antibodies specific for gS protein, demonstrating the oral immunogenicity of the plant derived spike protein from TGEV.
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PMID:Oral immunogenicity of the plant derived spike protein from swine-transmissible gastroenteritis coronavirus. 1100 80

The sedimentation behavior of transmissible gastroenteritis coronavirus (TGEV) was analyzed. Upon sucrose gradient centrifugation, the major virus band was found at a density of 1.20 to 1.22 g/cm(3). This high density was observed only when TGEV with a functional sialic acid binding activity was analyzed. Mutants of TGEV that lacked sialic acid binding activity due to a point mutation in the sialic acid binding site of the S protein were mainly recovered at a lower-density position on the sucrose gradient (1.18 to 1.19 g/cm(3)). Neuraminidase treatment of purified virions resulted in a shift of the sedimentation value from the higher to the lower density. These results suggest that binding of sialoglycoproteins to the virion surface is responsible for the sedimentation behavior of TGEV. When purified virions were treated with octylglucoside to solubilize viral glycoproteins, ultracentrifugation resulted in sedimentation of the S protein of TGEV. However, when neuraminidase-treated virions or mutants with a defective sialic acid binding activity were analyzed, the S protein remained in the supernatant rather than in the pellet fraction. These results indicate that the interaction of the surface protein S with sialoglycoconjugates is maintained after solubilization of this viral glycoprotein by detergent treatment.
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PMID:Sialic acid binding activity of transmissible gastroenteritis coronavirus affects sedimentation behavior of virions and solubilized glycoproteins. 1113 97

Passive protection experiments were conducted to determine the frequency and amounts of hyperimmune antiserum needed to block a transmissible gastroenteritis virus (TGEV) challenge infection and to identify monoclonal antibodies that are partially protective against TGEV. Hyperimmune antiserum or monoclonal antibodies were added to milk at each feeding or at selected feedings when the amount of antiserum was reduced. Three-day-old piglets were challenged with virulent virus that had been preincubated with antiserum or monoclonal antibodies. The results indicated that supplementing antiserum every other day was not efficacious for protection. Supplementing even small quantities of hyperimmune antiserum (0.5 ml) at least once a day in most cases was sufficient for piglet survival but did not prevent morbidity. Increasing the amount (>2 ml) and providing antiserum 3 times/day completely blocked the TGEV challenge infection. Two monoclonal antibodies were discovered that also provided passive protection for baby pigs. One monoclonal antibody, 5G1, had a high neutralizing titer, and the other, 6C4, was more effective in neutralizing and binding to virulent TGEV than to attenuated TGEVs. Both of these monoclonal antibodies were partially effective as supplements in milk for passive protection. Furthermore, these monoclonal antibodies were useful for boosting the efficacy of TGEV-neutralizing colostrum, which by itself was ineffective. These results show that other antigenic sites, different from the 4-well characterized epitopes on the S glycoprotein of TGEV, also are important for passive protection.
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PMID:Partial passive protection with two monoclonal antibodies and frequency of feeding of hyperimmune anti-transmissible gastroenteritis virus (TGEV) serum for protection of three-day-old piglets from a TGEV challenge infection. 1147 99

In earlier studies in our laboratory, we found that bovine coronavirus (BCV) was pathogenic for 1-day-old turkey poults. This finding prompted us to study the antigenic and genomic relatedness of turkey origin coronaviruses (TOCVs) to BCV. A one-step reverse transcription (RT)-polymerase chain reaction (PCR) targeting a 730-base pair fragment of the nucleocapsid (N) gene of BCV and a nested PCR targeting a 407-base pair fragment of the N gene were used in an attempt to detect TOCV from North Carolina, Indiana, and a prototype turkey coronavirus (TCV) obtained from the American Type Culture Collection. Both the one-step RT-PCR and the nested PCR amplified cell culture-passaged isolates of calf diarrhea strains of BCV but none of the 15 tested TOCVs or transmissible gastroenteritis coronavirus of swine. TOCVs also did not cross-react in a BCV antigen-capture (AC) enzyme-linked immunosorbent assay (ELISA) system with monoclonal antibodies (MAbs) against N, spike glycoprotein, and hemagglutinin esterase glycoprotein proteins of BCV as coating antibodies. The same TOCVs could be detected with primers designed from the genome of infectious bronchitis virus (IBV) of chickens. These primers amplified a 1082-base pair region spanning portions of the membrane glycoprotein (M) and N protein genes of IBV and TCV. The TOCVs also cross-reacted in an AC-ELISA with MAbs against the M and subunit 2 of spike glycoprotein of IBV.
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PMID:Antigenic and genomic relatedness of turkey-origin coronaviruses, bovine coronaviruses, and infectious bronchitis virus of chickens. 1178 2

The bovine rotavirus (BRV) WC3 serves as the background strain in the development of a multivalent reassortant vaccine against rotavirus gastroenteritis in infants. The genes encoding the outer capsid spike protein VP4, the inner capsid protein VP6, the outer capsid glycoprotein VP7, and the viral enterotoxin NSP4 of BRV WC3 were sequenced. Comparative analysis of the deduced amino acids of the sequenced genes indicated that the BRV WC3 strain shares a high degree of amino acid identity with serotype P7 VP4 (93-96%), serotype G6 VP7 (91-97%), subgroup (SG) I VP6 (96-99%), and NSP4 genogroup A (96-98%) BRV strains. Our results confirm and extend previous studies which suggested that the VP4 of BRV WC3 was closely related to that of the P7 prototype, BRV UK. In addition, the VP6 and VP7 of BRV WC3 were very similar to the VP6 and VP7 of both SG I and G6 BRV NCDV and UK strains. However, the NSP4 of BRV WC3 was more closely related to that BRV NCDV, the P6 prototype, than to that of BRV UK.
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PMID:Sequence analysis of the VP4, VP6, VP7, and NSP4 gene products of the bovine rotavirus WC3. 1201 1

The surface glycoprotein S of transmissible gastroenteritis virus (TGEV) has two binding activities. (i) Binding to porcine aminopeptidase N (pAPN) is essential for the initiation of infection. (ii) Binding to sialic acid residues on glycoproteins is dispensable for the infection of cultured cells but is required for enteropathogenicity. By comparing parental TGEV with mutant viruses deficient in the sialic acid binding activity, we determined the contributions of both binding activities to the attachment of TGEV to cultured cells. In the presence of a functional sialic acid binding activity, the amount of virus bound to two different porcine cell lines was increased sixfold compared to the binding of the mutant viruses. The attachment of parental virus was reduced to levels observed with the mutants when sialic acid containing inhibitors was present or when the cells were pretreated with neuraminidase. In virus overlay binding assays with immobilized cell surface proteins, the mutant virus only recognized pAPN. In addition, the parental virus bound to a high-molecular-mass sialoglycoprotein. The recognition of pAPN was sensitive to reducing conditions and was not dependent on sialic acid residues. On the other hand, binding to the sialic acid residues of the high-molecular-mass glycoprotein was observed regardless of whether the cellular proteins had been separated under reducing or nonreducing conditions. We propose that binding to a surface sialoglycoprotein is required for TGEV as a primary attachment site to initiate infection of intestinal cells. This concept is discussed in the context of other viruses that use two different receptors to infect cells.
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PMID:Binding of transmissible gastroenteritis coronavirus to cell surface sialoglycoproteins. 1202 36

The spike (S) glycoprotein of transmissible gastroenteritis virus (TGEV) is the predominant inducer of neutralizing antibodies and has been implicated in virulence and host cell tropism. In this study, the nucleotide and deduced amino acid sequences of the amino terminal half of the S glycoprotein gene of one Korean field TGEV strain (133) isolated in 1997 and three Korean field TGEV strains (KT2, KT3 and KT4) isolated in 2000 and HKT2 strain, KT2 passaged 104 times in ST cells, were determined. The amino terminal half of the S glycoprotein gene including antigenic sites A, B, C and D, were amplified by reverse transcriptase-polymerase chain reaction (RT-PCR). Amplified PCR products were cloned, sequenced, and compared with published sequences for non-Korean TGEV strains. Korea TGEV field strains had 98.5-99.5% nucleotide sequence and 97.2-99.0% amino acid sequence similarity with each other. They had 96.5-99.0% nucleotide sequence similarity and 94.9-97.6% amino acid sequence similarity compared to non-Korean TGEV strains. Korean TGEV strains had several specific nucleotide and amino acid sequences which were not found in foreign TGEV or PRCV strains. HKT2 strain differed by 0.89% in nucleotide and 2.03% amino acid sequences compared to original KT2 strain although the regions forming four antigenic sites were not changed. By phylogenetic tree analysis, Korean field TGEV strains were branched into different groups from non-Korean TGEV or PRCV strains. Korean TGEV field strains KT2 and 133 were branched in separate groups that were differentiated from the other Korean TGEV strains. The Korean TGEV strains seemed to be evolved from a separate lineage of TGEV strain.
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PMID:Partial sequence of the spike glycoprotein gene of transmissible gastroenteritis viruses isolated in Korea. 1281 87

Transmissible gastroenteritis coronavirus (TGEV) is a porcine pathogen causing enteric infections that are lethal for suckling piglets. The enterotropism of TGEV is connected with the sialic acid binding activity of the viral surface protein S. Here we show that, among porcine intestinal brush border membrane proteins, TGEV recognizes a mucin-type glycoprotein designated MGP in a sialic acid-dependent fashion. Virus binding assays with cryosections of the small intestine from a suckling piglet revealed the binding of TGEV to mucin-producing goblet cells. A nonenteropathogenic mutant virus that lacked a sialic acid binding activity was unable to bind to MGP and to attach to goblet cells. Our results suggest a role of MGP in the enteropathogenicity of TGEV.
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PMID:Binding of transmissible gastroenteritis coronavirus to brush border membrane sialoglycoproteins. 1455 69

Rotavirus is the major cause of dehydrating gastroenteritis in children and young animals. NSP4 (non-structural protein 4), a rotaviral non-structural glycoprotein and a peptide NSP4(114-135) (DKLTTREIEQVELLKRIYDKLT), corresponding to NSP4 amino acids 114-135, induce diarrhoeal disease in a neonatal mouse model and interact with model membranes that mimic caveolae. Correlation of the mechanisms of diarrhoea induction and membrane interactions by NSP4 protein and peptide remain unclear. Several additional NSP4 peptides were synthesized and their interactions with membranes studied by (i) CD, (ii) a filtration-binding assay and (iii) a fluorescent molecule leakage assay. Model membranes that varied in lipid compositions and radius of curvature were utilized to determine the compositional and structural requirements for optimal interaction with the peptides of NSP4. Similar to the intact protein and NSP4(114-135), peptides overlapping residues 114-135 had significantly higher affinities to membranes rich in negatively charged lipids, rich in cholesterol and with a high radius of curvature. In the leakage assay, small and large unilamellar vesicles loaded with the fluorophore/quencher pair 8-aminonaphthalene-1,3,6-trisulphonic acid disodium salt/p -xylene-bis-pyridinium bromide were incubated with the NSP4 peptides and monitored for membrane disruption by lipid reorganization or by pore formation. At a peptide concentration of 15 microM, none of the NSP4 peptides caused leakage. These results confirm that NSP4 interacts with caveolae-like membranes and the alpha-helical region of NSP4(114-135) comprises a membrane interaction domain that does not induce membrane disruption at physiological concentrations.
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PMID:Interaction(s) of rotavirus non-structural protein 4 (NSP4) C-terminal peptides with model membranes. 1501 30

Lactobacillus casei strain Shirota was selected as a bacterial carrier for the development of live mucosal vaccines against coronavirus. A 75 kDa fragment of transmissible gastroenteritis coronavirus (TGEV) spike glycoprotein S was used as the model coronavirus antigen. The S glycoprotein was cloned into a Lactobacillus/E. coli shuttle vector (pLP500) where expression and secretion of the glycoprotein S from the recombinant lactobacilli was detected via immunoblotting. Oral immunization of BALB/c mice with recombinant LcS that constitutively expresses the 75 kDa fragment of the glycoprotein S, induced both local mucosal and systemic immune responses against TGEV. Maximum titers of IgG (8.38+/-0.19 ng/ml of serum) and IgA (64.82+/-2.9 ng/ml of intestinal water) were attained 32 days post oral inturbation. The induced antibodies demonstrated neutralizing effects on TGEV infection.
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PMID:Intragastric administration of Lactobacillus casei expressing transmissible gastroentritis coronavirus spike glycoprotein induced specific antibody production. 1566 81


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