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Specific ion effects on the particle size distributions of cell culture-derived influenza A virus particles within the Hofmeister series.

ABSTRACT: Virus particle (VP) aggregation can have serious implications on clinical safety and efficacy of virus-based therapeutics. Typically, VP are suspended in buffers to establish defined product properties. Salts used to achieve these properties show specific effects in chemical and biological systems in a reoccurring trend known as Hofmeister series (HS). Hofmeister series effects are ubiquitous and can affect colloidal particle systems. In this study, influences of different ions (anions: SO4 2-, HPO4 2-, Cl-, Br-, NO3 -, I-; cations: K+, Na+, Li+, Mg2+, Ca2+) on particle size distributions of cell culture-derived influenza VP were investigated. For the experimental setup, influenza virus A/Puerto Rico/8/34 (H1N1) VP produced in adherent and suspension Madin Darby canine kidney cells were used. Inactivated and concentrated virus harvests were dialyzed against buffers containing the ions of interest, followed by differential centrifugal sedimentation to measure particle size distributions. VP from both cell lines showed no aggregation over a wide range of buffers containing different salts in concentrations ?60 mM. However, when dialyzed to low salt or Ca2+ buffers, VP produced in adherent cells showed increased aggregation compared to VP produced in suspension cells. Additionally, changes in VP diameters depending on specific ion concentrations were observed that partially reflected the HS trend.

SUBMITTER: Pieler MM

PROVIDER: S-EPMC6999566 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature

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Specific ion effects on the particle size distributions of cell culture-derived influenza A virus particles within the Hofmeister series.

Pieler Michael Martin MM Heyse Anja A Wolff Michael Werner MW Reichl Udo U

Engineering in life sciences 20161125 5

Virus particle (VP) aggregation can have serious implications on clinical safety and efficacy of virus-based therapeutics. Typically, VP are suspended in buffers to establish defined product properties. Salts used to achieve these properties show specific effects in chemical and biological systems in a reoccurring trend known as Hofmeister series (HS). Hofmeister series effects are ubiquitous and can affect colloidal particle systems. In this study, influences of different ions (anions: SO<sub>4 ...[more]

PMID: 32624792

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Project description:Quantitative interpretation and prediction of Hofmeister ion effects on protein processes, including folding and crystallization, have been elusive goals of a century of research. Here, a quantitative thermodynamic analysis, developed to treat noncoulombic interactions of solutes with biopolymer surface and recently extended to analyze the effects of Hofmeister salts on the surface tension of water, is applied to literature solubility data for small hydrocarbons and model peptides. This analysis allows us to obtain a minimum estimate of the hydration b1 (H2O A(-2)), of hydrocarbon surface and partition coefficients Kp, characterizing the distribution of salts and salt ions between this hydration water and bulk water. Assuming that Na+ and SO4(2-) ions of Na2SO4 (the salt giving the largest reduction in hydrocarbon solubility as well as the largest increase in surface tension) are fully excluded from the hydration water at hydrocarbon surface, we obtain the same b1 as for air-water surface (approximately 0.18 H2O A(-2)). Rank orders of cation and anion partition coefficients for nonpolar surface follow the Hofmeister series for protein processes, but are strongly offset for cations in the direction of exclusion (preferential hydration). By applying a coarse-grained decomposition of water accessible surface area (ASA) into nonpolar, polar amide, and other polar surface and the same hydration b1 to interpret peptide solubility increments, we determine salt partition coefficients for amide surface. These partition coefficients are separated into single-ion contributions based on the observation that both Cl- and Na+ (also K+) occupy neutral positions in the middle of the anion and cation Hofmeister series for protein folding. Independent of this assignment, we find that all cations investigated are strongly accumulated at amide surface while most anions are excluded. Cation and anion effects are independent and additive, allowing successful prediction of Hofmeister salt effects on micelle formation and other processes from structural information (ASA).

Dataset Information

Specific ion effects on the particle size distributions of cell culture-derived influenza A virus particles within the Hofmeister series.

Publications

Specific ion effects on the particle size distributions of cell culture-derived influenza A virus particles within the Hofmeister series.

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