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An impedimetric immunosensor for determination of porcine epidemic diarrhea virus based on the nanocomposite consisting of molybdenum disulfide/reduced graphene oxide decorated with gold nanoparticles.

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An electrochemical immunosensor for the determination of porcine epidemic diarrhea virus (PEDV) is described. It was manufactured by using gold nanoparticles/molybdenum disulfide/reduced graphene oxide nanocomposites modified on the surface of a glassy carbon electrode (GCE). The independently

Antiviral effect of N-butyldeoxynojirimycin against bovine viral diarrhea virus correlates with misfolding of E2 envelope proteins and impairment of their association into E1-E2 heterodimers.

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The iminosugar N-butyldeoxynojirimycin (NB-DNJ), an endoplasmic reticulum alpha-glucosidase inhibitor, has an antiviral effect against bovine viral diarrhea virus (BVDV). In this report, we investigate the molecular mechanism of this inhibition by studying the folding pathway of BVDV envelope

Crystal structure of heat-labile enterotoxin from Escherichia coli with increased thermostability introduced by an engineered disulfide bond in the A subunit.

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Cholera toxin (CT) produced by Vibrio cholerae and heat-labile enterotoxin (LT-I), produced by enterotoxigenic Escherichia coli, are AB5 heterohexamers with an ADP-ribosylating A subunit and a GM1 receptor binding B pentamer. These toxins are among the most potent mucosal adjuvants known and, hence,

Reduction of the secretory response to Escherichia coli heat-stable enterotoxin by thiol and disulfide compounds.

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We examined the effects of disulfide and thiol compounds on Escherichia coli heat-stable enterotoxin (ST) and cyclic GMP-induced secretion. Both cystamine and cystine (disulfide compounds) reduced the secretory responses to submaximal doses of ST in suckling mice (at 0.5 mumol per mouse) and reduced

Importance of disulfide bridges in the structure and activity of Escherichia coli enterotoxin ST1b.

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A 13-amino acid sequence of the Escherichia coli heat-stable enterotoxin ST1b encodes its receptor-binding and diarrheal functions. This sequence includes six cysteines involved in three intramolecular disulfide bridges. To determine the importance of disulfide bridges to the biological activity of

Presence of bovine viral diarrhea virus (BVDV) E2 glycoprotein in VSV recombinant particles and induction of neutralizing BVDV antibodies in mice.

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We generated a recombinant vesicular stomatitis virus (VSV-E2) encoding the bovine viral diarrhea virus (BVDV) E2 glycoprotein with the VSV-G protein signal peptide. Infection of BHK21 cells with VSV-E2 induced the synthesis of a recombinant E2 (rE2) that comigrated with authentic BVDV-E2 in

Pestivirus glycoprotein which induces neutralizing antibodies forms part of a disulfide-linked heterodimer.

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Neutralizing monoclonal antibodies directed against hog cholera virus (HCV) precipitated two HCV-encoded glycoproteins, HCV gp55 and HCV gp33. Immunoassay with bacterial fusion proteins and Western immunoblotting with extracts from infected cells revealed that the antibodies recognized only HCV

Role of disulfide bond formation in the folding and assembly of the envelope glycoproteins of a pestivirus.

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Bovine viral diarrhea virus (BVDV) is a pestivirus member of the Flaviviridae family, closely related to, and used as a surrogate model for the hepatitis C virus. Its envelope contains the E1 and E2 glycoproteins, disulfide linked into homo- and heterodimers. In this study, we investigate the role

Crystal structure of glycoprotein E2 from bovine viral diarrhea virus.

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Pestiviruses, including bovine viral diarrhea virus, are important animal pathogens and are closely related to hepatitis C virus, which remains a major global health threat. They have an outer lipid envelope bearing two glycoproteins, E1 and E2, required for cell entry. They deliver their genome

The Salmonella SPI1 type three secretion system responds to periplasmic disulfide bond status via the flagellar apparatus and the RcsCDB system.

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Upon contact with intestinal epithelial cells, Salmonella enterica serovar Typhimurium injects a set of effector proteins into the host cell cytoplasm via the Salmonella pathogenicity island 1 (SPI1) type III secretion system (T3SS) to induce inflammatory diarrhea and bacterial uptake. The master

The structural basis of receptor-binding by Escherichia coli associated with diarrhea and septicemia.

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GafD in Escherichia coli G (F17) fimbriae is associated with diarrheal disease, and the structure of the ligand-binding domain, GafD1-178, has been determined at 1.7A resolution in the presence of the receptor sugar N-acetyl-D-glucosamine. The overall fold is a beta-barrel jelly-roll fold. The

Prosequence switching: an effective strategy to produce biologically active E. coli heat-stable enterotoxin STh.

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Enterotoxigenic Escherichia coli (ETEC) infections account for the majority of cases of acute secretory diarrhea. The causative agents are enterotoxins secreted by ETEC, among them is the heat-stable enterotoxin, STh. STh is a 19-amino acid peptide containing three disulfide bonds that stimulates

Molecular weight analysis of Entamoeba histolytica antigens recognized by IgG and IgM antibodies in the sera of patients with amoebiasis.

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The sera of four patients with amoebic liver abscess and two patients with diarrhea caused by Entamoeba histolytica were tested on "Western blots" prepared from E. histolytica strains A3, SFL-3 and HK-9 separated by SDS-PAGE. IgG antibodies in the sera from patients with liver abscess were found to

Derlin-1 facilitates the retro-translocation of cholera toxin.

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Cholera toxin (CT) intoxicates cells by using its receptor-binding B subunit (CTB) to traffic from the plasma membrane to the endoplasmic reticulum (ER). In this compartment, the catalytic A1 subunit (CTA1) is unfolded by protein disulfide isomerase (PDI) and retro-translocated to the cytosol where

Structure, glycosylation, and localization of rat intestinal guanylyl cyclase C: modulation by fasting.

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Guanylyl cyclase C (GC-C), an intestinal receptor guanylyl cyclase, binds diarrhea-producing bacterial ligands such as the Escherichia coli heat stable enterotoxin. We examined the regulatory influence of feeding and fasting on the expression, structure, and biochemical properties of GC-C. When

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