Isoelectric point is an inadequate descriptor of MS2, Phi X 174 and PRD1 phages adhesion on abiotic surfaces

Dika, C.; Duval, Jérôme F. L.; Francius, Grégory; Perrin, Aline; Gantzer, Christophe

doi:10.1016/j.jcis.2014.08.055

Cited by 87 publications

(90 citation statements)

References 38 publications

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“…These results indicate that the viruses have different surface hydrophobicities, with MS2 being the most hydrophobic, followed by PV, AdV, and φX174 in that order. Dika et al (2015) reported that MS2 is more hydrophobic than φX174, which agrees with our results. Because mechanisms that destabilize viruses and NOM during the coagulation process, that is, coordination reactions between coagulant species and carboxyl groups of the virus surface proteins or NOM, are similar for the two species (Bratby, 2006), and because the hydrophobic fractions of NOM are removed from water more efficiently than are the hydrophilic fractions (Matilainen et al, 2010), virus particles having a more hydrophobic surface can be expected to be removed during coagulation to a greater extent than viruses having a less hydrophobic surface.…”

Section: Relationships Between Enteric Virus Removal and Bacteriophagsupporting

confidence: 93%

“…Therefore, the difference in the AdV, PV, MS2, and φX174 removal ratios during coagulation did not depend solely on the difference in electrophoretic mobility between the viruses in the source water samples used in the present study. Dika et al (2015) reported that in prepared de-ionized water at pH 7, MS2 is more negatively charged than φX174, in agreement with our observation in prepared Milli-Q water at the same pH ( Figure S3). In contrast, φX174 tended to be more negatively charged than MS2 in the filtered source water samples, as described above, probably owing to the difference in the solvent water quality.…”

Section: Relationships Between Enteric Virus Removal and Bacteriophagsupporting

confidence: 91%

See 1 more Smart Citation

Investigation of enteric adenovirus and poliovirus removal by coagulation processes and suitability of bacteriophages MS2 and φX174 as surrogates for those viruses

Shirasaki

Matsushita

Matsui

et al. 2016

Science of The Total Environment

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We evaluated the removal of enteric adenovirus (AdV) type 40 and poliovirus (PV) type 1 by coagulation, using water samples from 13 water sources for drinking water treatment plants in Japan. The behaviors of two widely accepted enteric virus surrogates, bacteriophages MS2 and φX174, were compared with the behaviors of AdV and PV. Coagulation with polyaluminum chloride (PACl, basicity 1.5) removed AdV and PV from virus-spiked source waters: the infectious AdV and PV removal ratios evaluated by means of a plaque-forming-unit method were 0.1-1.4-log10 and 0.5-2.4-log10, respectively. A nonsulfated high-basicity PACl (basicity 2.1) removed infectious AdV and PV more efficiently than did other commercially available PACls (basicity 1.5-2.1), alum, and ferric chloride. The MS2 removal ratios tended to be larger than those of AdV and PV, partly because of differences in the hydrophobicities of the virus particles and the sensitivity of the virus to the virucidal activity of PACl; the differences in removal ratios were not due to differences in the surface charges of the virus particles. MS2, which was more hydrophobic than the other viruses, was inactivated during coagulation with PACl. Therefore, MS2 does not appear to be an appropriate surrogate for AdV and PV during coagulation. In contrast, because φX174, like AdV and PV, was not inactivated during coagulation, and because the hydrophobicity of φX174 was similar to or somewhat lower than the hydrophobicities of AdV and PV, the φX174 removal ratios tended to be similar to or somewhat smaller than those of the enteric viruses. Therefore, φX174 is a potential conservative surrogate for AdV and PV during coagulation. In summary, the surface hydrophobicity of virus particles and the sensitivity of the virus to the virucidal activity of the coagulant are probably important determinants of the efficiency of virus removal during coagulation.

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Section: Relationships Between Enteric Virus Removal and Bacteriophagsupporting

confidence: 93%

Section: Relationships Between Enteric Virus Removal and Bacteriophagsupporting

confidence: 91%

Investigation of enteric adenovirus and poliovirus removal by coagulation processes and suitability of bacteriophages MS2 and φX174 as surrogates for those viruses

Shirasaki

Matsushita

Matsui

et al. 2016

Science of The Total Environment

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“…The pI values we obtain for other proteins are listed in Table I and also correspond well with the experimental values: pI ∼ 4.7-5.6 for HSA [71,72] and pI ∼ 5.1 for β-lactoglobulin [73,74]. The pI value obtained for the phage MS2 capsid protein at a first glance disagrees with the very low reported value of the phage MS2, pI ∼ 2.2-3.9 [75,76]. The notable discrepancy stems most probably from the presence of the genome in the interior of the virion and the permeability of the capsid to external flow [77] -in studies where the capsid protein alone was considered, the obtained isoelectric point was at a pI > 8 [78][79][80].…”

Section: Resultssupporting

confidence: 80%

pH Dependence of Charge Multipole Moments in Proteins

Božič

Podgornik

2017

Biophysical Journal

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Electrostatic interactions play a fundamental role in the structure and function of proteins. Due to ionizable amino acid residues present on the solvent-exposed surfaces of proteins, the protein charge is not constant but varies with the changes in the environment-most notably, the pH of the surrounding solution. We study the effects of pH on the charge of four globular proteins by expanding their surface charge distributions in terms of multipoles. The detailed representation of the charges on the proteins is in this way replaced by the magnitudes and orientations of the multipole moments of varying order. Focusing on the three lowest-order multipoles-the total charge, dipole, and quadrupole moment-we show that the value of pH influences not only their magnitudes, but more notably and importantly also the spatial orientation of their principal axes. Our findings imply important consequences for the study of protein-protein interactions and the assembly of both proteinaceous shells and patchy colloids with dissociable charge groups.

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“…3 are relatively large and thus the accuracy of the theoretical prediction is quantitatively reduced, it can be exploited to qualitatively explain experimental observations. In many previous studies [4][5][6][7], MS2-virus like particles begin to aggregate at at pH ≤ 4. The finding suggest the electrostatic forces experience a replusive-toattractive transition at pH = 4.…”

Section: Interactions Of the Metal Sphere With The Ms2 Virusmentioning

confidence: 99%

The pH-dependent electrostatic interaction of a metal nanoparticle with the MS2 virus-like particles

Phan

Hoang

2019

Chemical Physics Letters

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The electrostatic interaction of metal nanoparticles with viruses is attracting great interest due to their antiviral activity and their role in enhancing the detection of viruses at ultra-low concentrations. We model the MS2 virus devoid of its single strand RNA core using a core-shell model. The dependence of the inner and outer surface charge density on the pH is taken into account in our model of the interaction. Varying the pH causes a change in the sign of the outer surface charge leading to the attractive-repulsive transition in the electrostatic interaction between the MS2 virus and metal nanoparticle at pH = 4.PACS numbers:

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Isoelectric point is an inadequate descriptor of MS2, Phi X 174 and PRD1 phages adhesion on abiotic surfaces

Cited by 87 publications

References 38 publications

Investigation of enteric adenovirus and poliovirus removal by coagulation processes and suitability of bacteriophages MS2 and φX174 as surrogates for those viruses

Investigation of enteric adenovirus and poliovirus removal by coagulation processes and suitability of bacteriophages MS2 and φX174 as surrogates for those viruses

pH Dependence of Charge Multipole Moments in Proteins

The pH-dependent electrostatic interaction of a metal nanoparticle with the MS2 virus-like particles

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