scholarly journals Delineating the Specific Influence of Virus Isoelectric Point and Size on Virus Adsorption and Transport through Sandy Soils

1998 ◽  
Vol 64 (2) ◽  
pp. 405-410 ◽  
Author(s):  
Scot E. Dowd ◽  
Suresh D. Pillai ◽  
Sookyun Wang ◽  
M. Yavuz Corapcioglu

ABSTRACT Many of the factors controlling viral transport and survival within the subsurface are still poorly understood. In order to identify the precise influence of viral isoelectric point on viral adsorption onto aquifer sediment material, we employed five different spherical bacteriophages (MS2, PRD1, Qβ, φX174, and PM2) having differing isoelectric points (pI 3.9, 4.2, 5.3, 6.6, and 7.3 respectively) in laboratory viral transport studies. We employed conventional batch flowthrough columns, as well as a novel continuously recirculating column, in these studies. In a 0.78-m batch flowthrough column, the smaller phages (MS2, φX174, and Qβ), which had similar diameters, exhibited maximum effluent concentration/initial concentration values that correlated exactly with their isoelectric points. In the continuously recirculating column, viral adsorption was negatively correlated with the isoelectric points of the viruses. A model of virus migration in the soil columns was created by using a one-dimensional transport model in which kinetic sorption was used. The data suggest that the isoelectric point of a virus is the predetermining factor controlling viral adsorption within aquifers. The data also suggest that when virus particles are more than 60 nm in diameter, viral dimensions become the overriding factor.

Author(s):  
Kanad Mallik

A novel approach has been suggested to use isoelectric points of viral and human proteins to quickly identify proteins that are effective in not allowing virus particles to attach to human receptor cells by virtue of their electrical charge. The method has been applied to SARS CoV-2 to suggest potentially important human proteins that can be suitable for making anti-viral drugs.


1995 ◽  
Vol 412 ◽  
Author(s):  
A. V. Wolfsberg ◽  
B. A. Robinson ◽  
J. T. Fabryka-Martin

AbstractCharacterization and performance assessment (PA) studies for the potential high-level nuclear waste repository at Yucca Mountain require an understanding of migration mechanisms and pathways of radioactive solutes. Measurements of 36C1 in samples extracted from boreholes at the site are being used in conjunction with recent infiltration estimates to calibrate a site-scale flow and solute transport model. This exercise using the flow and solute transport model, FEHM, involves testing different model formulations and two different hypotheses to explain the occurrence of elevated 36Cl in the Calico Hills unit (CHn) which indicates younger water than in the overlying Topopah Spring unit (TSw). One hypothesis suggests fast vertical transport from the surface via fractures in the TSw to the CHn. An alternative hypothesis is that the elevated 36C1 concentrations reflect rapid horizontal flow in the CHn or at the interface between the CHn and the TSw with the source being vertical percolation under spatially isolated regions of high infiltration or at outcrops of those units. Arguments in favor of and against the hypotheses are described in conjunction with the site-scale transport studies.


1995 ◽  
Vol 89 (5) ◽  
pp. 487-495 ◽  
Author(s):  
M. Susan Monteith ◽  
Tao Wang ◽  
Morris J. Brown

1. We have previously reported the relative mRNA and protein level of the long and short splice variants of Gsα (GsαL and GsαS) in human atrium. We have now measured the relative proportions of the serine+ and serine− variants of GsαL and GsαS in human atrium, and assessed, indirectly, whether their differential expression may (i) regulate Gsα phosphorylation, and (ii) be regulated by atrial cyclic AMP levels. 2. The serine+ and serine− variants of GsαL and GsαS were estimated by single nucleotide primer extension in 36 right atrial strips of which half were from β-adrenoceptor-blocked patients. The ratio of serine+ to serine− variants was 0.06 ± 0.12 for GsαL, compared with 8.04 ± 12.16 for GsαS (P < 0.001). 3. Isoelectric points of GsαL and GsαS in the atria of four β-adrenoceptor-blocked and four non-β-adrenoceptor-blocked patients were estimated by two-dimensional gel electrophoresis. Two-dimensional gel analysis gave a consistent pattern with several spots for both GsαL and GsαS; however, the isoelectric points of GsαS were more acid (5.18 ± 0.24) than those of GsαL (5.87 ± 0.17, P < 0.001). 4. No significant difference in either the serine variants or isoelectric point value was observed between β-adrenoceptor-blocked and non-β-adrenoceptor-blocked patients. 5. In conclusion, all four Gsα variants were expressed in human atrium, but GsαL is almost entirely of the serine− form. GsαS has a more acidic isoelectric point than GsαL, indicating a possible post-translational modification. The lack of difference in our results between β-adrenoceptor-blocked and non-β-adrenoceptor-blocked patients suggests indirectly that cyclic AMP is an unlikely candidate for regulating splicing or post-translational modification of Gsα in vivo.


1982 ◽  
Vol 203 (2) ◽  
pp. 427-433 ◽  
Author(s):  
N UI ◽  
C Takasaki ◽  
N Tamiya

The isoelectric points of erabutoxins a, b and c, neurotoxic proteins of a sea snake, Laticauda semifasciata, were determined by density-gradient isoelectric focusing. The same measurement was also made with monoacyl derivatives of erabutoxin b, in which each one of all amino groups had been either acetylated or propionylated. Erabutoxins a and b showed the same isoelectric point at pH 9.68. The values for [1-N alpha-acetyl-arginine]-, [15-N6-acetyl-lysine]-, [27-N6-acetyl-lysine]-, [47-N6-propionyl-lysine]- and [51-N6-acetyl-lysine]-erabutoxin b were at pH 9.52, 9.31, 9.45, 9.22 and 9.09 respectively, being definitely different from each other and lower than the value for the unmodified molecule. The isoelectric point of erabutoxin c, which is [51-asparagine]-erabutoxin b, was the same as that of [51-N6-acetyl-lysine]erabutoxin b. Assuming that no change in pK occurs on monoacylation, the pK values of amino groups in erabutoxin b were calculated from the isoelectric-point data. It is indicated that the pK values of zeta-amino groups differ markedly from each other and that the value of alpha-amino group is anomalously high.


1924 ◽  
Vol 6 (3) ◽  
pp. 259-271 ◽  
Author(s):  
William J. Robbins

1. Mycelium of Rhizopus nigricans when stained with certain acid and basic dyes and washed with buffer mixtures of 0.1 M phosphoric acid and sodium hydroxide responded much like an amphoteric colloid with an isoelectric point near pH 5.0. 2. When grown on potato dextrose agar the reaction of which was varied with phosphoric acid the extent of colony growth of Rhizopus nigricans plotted against the initial Sörensen value of the agar produced a double maximum curve with the minimum between the two maxima at initial pH 5.2. 3. When grown in potato dextrose broth the reaction of which was varied with phosphoric acid the dry matter produced by Rhizopus nigricans plotted against the Sörensen value of the broth produced a double maximum curve with the minimum between the two maxima at initial pH 5.2 or average pH 4.9. 4. Mycelium of Rhizopus nigricans placed in buffer mixtures of 0.01 M phosphoric acid and sodium hydroxide of pH 4.1 to 6.3, changed the reaction in most cases toward greater alkalinity. 5. Mycelium of Fusarium lycopersici stained with certain acid and basic dyes and washed with buffer mixtures of 0.1 M phosphoric acid and sodium hydroxide responded much like an amphoteric colloid with an isoelectric point near pH 5.5.


1968 ◽  
Vol 14 (3) ◽  
pp. 197-204 ◽  
Author(s):  
Tam S. David-West ◽  
Patricia M. Cooke ◽  
J. W. Stevenson

An antiviral substance elaborated in Czapek-Dox broth by a strain of Penicillium cyaneo-fulvum isolated in this laboratory, and active against influenza A virus (PR8), influenza B virus (Lee), and Newcastle disease virus (B1) in modified Maitland tissue cultures has been shown to act at an intracellular site in the viral replicative cycle. The substance neither blocks virus adsorption nor impedes the release of newly formed virus particles. It is not viricidal, does not interfere with the action of ths viral neuraminidase on red blood cells, and does not possess any haemagglutination or haemagglutination–inhibition activity. A comparison with other reported antiviral agents shows that the antiviral substance is different from those previously studied.


1986 ◽  
Vol 6 (7) ◽  
pp. 685-689 ◽  
Author(s):  
F. A. Hashim ◽  
E. Davies Jones ◽  
R. D. Howells ◽  
B. Rees Smith

The water soluble A subunit of the human TSH receptor has been shown to have an isoelectric point of 5. As both TSH and TSH receptor antibodies have isoelectric points in the region of 8–10, charge-charge interactions must be of major importance in the binding of hormone or antibody to the TSH receptor A subunit.


1919 ◽  
Vol 2 (2) ◽  
pp. 145-160 ◽  
Author(s):  
Edwin J. Cohn ◽  
Joseph Gross ◽  
Omer C. Johnson

The state in which a protein substance exists depends upon the nature of its combination with acids or bases and is changed by change in the protein compound. The nature of the compound of a protein that exists at any hydrogen ion concentration can be ascertained if the isoelectric point of the protein is known. Accordingly information regarding the isoelectric points of vegetable proteins is of importance for operations in which it may be desirable to change the state of protein substances, as in the dehydration of vegetables. The Protein in Potato Juice.—The hydrogen ion concentration of the filtered juice of the potato is in the neighborhood of 10–7N. Such juice contains the globulin tuberin to the extent of from 1 to 2 per cent. The character of the compound of tuberin that exists in nature was suggested by its anodic migration in an electric field. The addition of acid to potato juice dissociated this compound and liberated tuberin at its isoelectric point. The isoelectric point of tuberin coincided with a slightly lower hydrogen ion concentration than 10–4N. At that reaction it existed most nearly uncombined. The flow of current during cataphoresis was greatest in the neighborhood of the isoelectric point. This evidence supplements that of the direction of the migration of tuberin, since it also suggests the existence of the greatest number of uncombined ions near this point. At acidities greater than the isoelectric point tuberin combined with acid. The compound that was formed contained nearly three times as much acid as was needed to dissociate the tuberin compound that existed in nature. At such acidities tuberin migrated to the cathode. Though never completely precipitated tuberin was least soluble in the juice of the potato in the neighborhood of its isoelectric point. Both the compounds of tuberin with acids and with bases were more soluble in the juice than was uncombined tuberin. The nature of the slight precipitate that separated when potato juice was made slightly alkaline was not determined. The Protein in Carrot Juice.—The isoelectric point of the protein in carrot juice coincided with that of tuberin. Remarkably similar also were the properties of carrot juice and the juice of the potato. Existing in nature at nearly the same reaction they combined with acids and bases to nearly the same extent and showed minima in solubility at the same hydrogen ion concentrations. The greatest difference in behavior concerned the alkaline precipitate which, in the carrot, was nearly as great as the acid precipitate. The Protein in Tomato Juice.—The protein of the tomato existed in a precipitated form near its isoelectric point. Accordingly it was not present to any extent in filtered tomato juice. If, however, the considerable acidity at which the tomato exists was neutralized the protein dissolved and was filterable. It then migrated to the anode in an electric field. The addition of sufficient acid to make the hydrogen ion concentration slightly greater than 10–5N again precipitated the protein at its isoelectric point. At greater acidities migration was cathodic.


1951 ◽  
Vol 4 (3) ◽  
pp. 372
Author(s):  
CWN Cumper ◽  
AE Alexander

The electrophoretic mobility of bovine γ-globulin, haemoglobin, and insulin adsorbed upon particles of different chemical types (mostly hydrocarbon derivatives) has been studied as a function of protein concentration and of pH. On the majority of the surfaces used the isoelectric points of the bovine γ-globulin and insulin were 6.0 and 5.0 respectively. However, with certain particles, especially cetyl alcohol, a marked shift in the isoelectric point was observed and on either side of the isoelectric point the mobility depended to a certain extent upon the nature of the particle. These effects have been ascribed to two causes : (a) a specific reaction between the protein and the particle and (b) an incomplete coverage of the particle by the protein. Insulin adsorbed upon particles became more negatively charged on standing. probably due to the insulin dissociating into smaller units.


1985 ◽  
Vol 17 (10) ◽  
pp. 201-210 ◽  
Author(s):  
M. Butler ◽  
A. R. Medien ◽  
G. R. Taylor

Viruses have individual and characteristic isoelectric points and for poliovirus there was good evidence for a correlation between one of these and sensitivity to chlorine. However, in the presence of chlorine dioxide, bromine chloride and iodine the behaviour of poliovirus and f2 coliphage was similar and not apparently influenced by the isoelectric point.


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