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1.
Vet Microbiol ; 156(1-2): 96-101, 2012 Apr 23.
Article in English | MEDLINE | ID: mdl-22115968

ABSTRACT

Transboundary animal disease viruses such as foot-and-mouth disease virus (FMDV) and African swine fever virus (ASFV) are highly contagious and cause severe morbidity and mortality in livestock. Proper disinfection during an outbreak can help prevent virus spread and will shorten the time for contaminated agriculture facilities to return to food production. Wood surfaces are prevalent at these locations, but there is no standardized method for porous surface disinfection; commercial disinfectants are only certified for use on hard, nonporous surfaces. To model porous surface disinfection in the laboratory, FMDV and ASFV stocks were dried on wood coupons and exposed to citric acid or sodium hypochlorite. We found that 2% citric acid was effective at inactivating both viruses dried on a wood surface by 30 min at 22°C. While 2000 ppm sodium hypochlorite was capable of inactivating ASFV on wood under these conditions, this chemical did not meet the 4-log disinfection threshold for FMDV. Taken together, our data supports the use of chemical disinfectants containing at least 2% citric acid for porous surface disinfection of FMDV and ASFV.


Subject(s)
African Swine Fever Virus/drug effects , Citric Acid/pharmacology , Disinfectants/pharmacology , Fomites/virology , Foot-and-Mouth Disease Virus/drug effects , Sodium Hypochlorite/pharmacology , Wood/virology , African Swine Fever/transmission , African Swine Fever/virology , Animals , Betula/virology , Foot-and-Mouth Disease/transmission , Foot-and-Mouth Disease/virology , Swine
2.
Biologicals ; 39(4): 231-5, 2011 Jul.
Article in English | MEDLINE | ID: mdl-21798759

ABSTRACT

Disinfection is a critical part of the response to transboundary animal disease virus (TADV) outbreaks by inactivating viruses on fomites to help control infection. To model the inactivation of TADV on fomites, we tested selected chemicals to inactivate Foot and Mouth Disease virus (FMDV), African Swine Fever virus (ASFV), and Classical Swine Fever virus (CSFV) dried on steel and plastic surfaces. For each of these viruses, we observed a 2 to 3 log reduction of infectivity due to drying alone. We applied a modified surface disinfection method to determine the efficacy of selected disinfectants to inactivate surface-dried high-titer stocks of these three structurally different TADV. ASFV and FMDV were susceptible to sodium hypochlorite (500 and 1000 ppm, respectively) and citric acid (1%) resulting in complete disinfection. Sodium carbonate (4%), while able to reduce FMDV infectivity by greater than 4-log units, only reduced ASFV by 3 logs. Citric acid (2%) did not totally inactivate dried CSFV, suggesting it may not be completely effective for disinfection in the field. Based on these data we recommend disinfectants be formulated with a minimum of 1000 ppm sodium hypochlorite for ASFV and CSFV disinfection, and a minimum of 1% citric acid for FMDV disinfection.


Subject(s)
Disinfection , Hot Temperature , Viruses/drug effects , Sodium Hypochlorite/pharmacology , Surface Properties
3.
Chem Cent J ; 4: 15, 2010 Aug 05.
Article in English | MEDLINE | ID: mdl-20687941

ABSTRACT

BACKGROUND: Gallic acid (3,4,5-trihydroxybenzoic acid) is found in a wide variety of plants; it is extensively used in tanning, ink dyes, as well as in the manufacturing of paper. The gallate moiety is a key component of many functional phytochemicals. In this work electron paramagnetic spectroscopy (EPR) was used to detect the free radicals generated by the air-oxidation of gallic acid. RESULTS: We found that gallic acid produces two different radicals as a function of pH. In the pH range between 7-10, the spectrum of the gallate free radical is a doublet of triplets (aH = 1.00 G, aH = 0.23 G, aH = 0.28 G). This is consistent with three hydrogens providing hyperfine splitting. However, in a more alkaline environment, pH >10, the hyperfine splitting pattern transforms into a 1:2:1 pattern (aH (2) = 1.07 G). Using D2O as a solvent, we demonstrate that the third hydrogen (i.e. aH = 0.28 G) at lower pH is a slowly exchanging hydron, participating in hydrogen bonding with two oxygens in ortho position on the gallate ring. The pKa of this proton has been determined to be 10. CONCLUSIONS: This simple and novel approach permitted the understanding of the prototropic equilibrium of the semiquinone radicals generated by gallic acid, a ubiquitous compound, allowing new insights into its oxidation and subsequent reactions.

4.
Protein Sci ; 12(12): 2675-84, 2003 Dec.
Article in English | MEDLINE | ID: mdl-14627729

ABSTRACT

A combined molecular dynamics simulation and multiple ligand docking approach is applied to study the roles of the anionic subsite residues (W86, E202, Y337) in the binding of acetylcholine (ACh) to acetylcholinesterase (AChE). We find that E202 stabilizes docking of ACh via electrostatic interactions. However, we find no significant electrostatic contribution from the aromatic residues. Docking energies of ACh to mutant AChE show a more pronounced effect because of size/shape complementarity. Mutating to smaller residues results in poorer binding, both in terms of docking energy and statistical docking probability. Besides separating out electrostatics by turning off the partial charges from each residue and comparing it with the native, the mutations in this study are W86F, W86A, E202D, E202Q, E202A, Y337F, and Y337A. We also find that all perturbations result in a significant reduction in binding of extended ACh in the catalytically productive orientation. This effect is primarily caused by a small shift in preferred position of the quaternary tail.


Subject(s)
Acetylcholine/chemistry , Acetylcholine/metabolism , Acetylcholinesterase/chemistry , Acetylcholinesterase/metabolism , Amino Acid Substitution/genetics , Acetylcholinesterase/genetics , Acylation , Amino Acids/chemistry , Anions/chemistry , Binding Sites , Catalysis , Hydrogen Bonding , Hydrophobic and Hydrophilic Interactions , Ligands , Molecular Structure , Mutation/genetics , Protein Binding , Protein Structure, Tertiary , Static Electricity , Thermodynamics
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