scholarly journals Stability of Secondary and Tertiary Structures of Virus-Like Particles Representing Noroviruses: Effects of pH, Ionic Strength, and Temperature and Implications for Adhesion to Surfaces

2015 ◽  
Vol 81 (22) ◽  
pp. 7680-7686 ◽  
Author(s):  
Idrissa Samandoulgou ◽  
Riadh Hammami ◽  
Rocio Morales Rayas ◽  
Ismail Fliss ◽  
Julie Jean
Keyword(s):  
Ionic Strength ◽  
Structural Rearrangement ◽  
Tertiary Structures ◽  
Hydrophobic Residues ◽  
Virus Like Particles ◽  
Nacl Concentration ◽  
Effects Of Ph ◽  
The Stability ◽  
Α Helix ◽  
Fresh Foods

ABSTRACTLoss of ordered molecular structure in proteins is known to increase their adhesion to surfaces. The aim of this work was to study the stability of norovirus secondary and tertiary structures and its implications for viral adhesion to fresh foods and agrifood surfaces. The pH, ionic strength, and temperature conditions studied correspond to those prevalent in the principal vehicles of viral transmission (vomit and feces) and in the food processing and handling environment (pasteurization and refrigeration). The structures of virus-like particles representing GI.1, GII.4, and feline calicivirus (FCV) were studied using circular dichroism and intrinsic UV fluorescence. The particles were remarkably stable under most of the conditions. However, heating to 65°C caused losses of β-strand structure, notably in GI.1 and FCV, while at 75°C the α-helix content of GII.4 and FCV decreased and tertiary structures unfolded in all three cases. Combining temperature with pH or ionic strength caused variable losses of structure depending on the particle type. Regardless of pH, heating to pasteurization temperatures or higher would be required to increase GII.4 and FCV adhesion, while either low or high temperatures would favor GI.1 adhesion. Regardless of temperature, increased ionic strength would increase GII.4 adhesion but would decrease GI.1 adhesion. FCV adsorption would be greater at refrigeration, pasteurization, or high temperature combined with a low salt concentration or at a higher NaCl concentration regardless of temperature. Norovirus adhesion mediated by hydrophobic interaction may depend on hydrophobic residues normally exposed on the capsid surface at pH 3, pH 8, physiological ionic strength, and low temperature, while at pasteurization temperatures it may rely more on buried hydrophobic residues exposed upon structural rearrangement.

scholarly journals Effects of pH and Ionic Strength on the Stability of Nanobubbles in Aqueous Solutions of α-Cyclodextrin

2007 ◽  
Vol 111 (40) ◽  
pp. 11745-11749 ◽  
Author(s):  
Fan Jin ◽  
Junfang Li ◽  
Xiaodong Ye ◽  
Chi Wu
Keyword(s):  
Ionic Strength ◽  
Aqueous Solutions ◽  
Effects Of Ph ◽  
The Stability

scholarly journals Mechanisms of Heat-induced Antigen Retrieval: Does pH or Ionic Strength of the Solution Play a Role for Refolding Antigens?

2005 ◽  
Vol 53 (11) ◽  
pp. 1311-1321 ◽  
Author(s):  
Katsura Emoto ◽  
Shuji Yamashita ◽  
Yasunori Okada
Keyword(s):  
Ionic Strength ◽  
The Other ◽  
Antigen Retrieval ◽  
Antigenic Determinants ◽  
Acidic Ph ◽  
Cooling Process ◽  
Ph Values ◽  
Ph Dependency ◽  
Nacl Concentration ◽  
Effects Of Ph

We investigated the effects of pH and ionic strength of solutions used for antigen retrieval to elucidate the mechanism of heat-induced antigen retrieval (HIAR) in immunohistochemistry. The immunostaining intensity of nuclear, cytoplasmic, cell membrane, and extracellular matrix antigens with 17 different antibodies was evaluated in formaldehyde-fixed and paraffin-embedded mouse and human tissues. Deparaffinized sections were autoclaved for 10 min in buffers with different pH values ranging from 3.0 to 10.5. To test the influence of ionic strength on immunoreactions, the sections were autoclaved for 10 min in 20 mM Tris-HCl buffers (TB) at pH 9.0 and 10.5 with or without 25, 50, and 100 mM NaCl. There were two immunostaining patterns for pH dependency of HIAR. First, the majority of antibodies recovered their antigenicity when heated in the buffers with both acidic pH (pH 3.0) and basic pH (pH 9.0 and 10.5). Second, some antibodies showed strong immunostaining only at basic pH values (pH 9.0 and 10.5). When the sections were autoclaved in TB at pH 9.0, immunostaining of all eight antibodies examined decreased as the NaCl concentration increased. On the other hand, when the sections were treated with TB at pH 10.5, all antibodies yielded stronger reactions in the buffer containing NaCl than in the buffer without NaCl; five antibodies exhibited the strongest immunoreaction at concentrations from 25 to 50 mM. These results suggest that the extended polypeptides by heating are charged negatively or positively at basic or acidic pH, and that an electrostatic repulsion force acts to prevent random entangling of polypeptides caused by hydrophobic attractive force and to expose antigenic determinants, during cooling process of HIAR solution.

scholarly journals Effect of sodium chloride concentration on fluid-phase assembly and stability of the C3 convertase of the classical pathway of the complement system

1990 ◽  
Vol 271 (3) ◽  
pp. 749-754 ◽  
Author(s):  
S Maeda ◽  
S Nagasawa
Keyword(s):  
Ionic Strength ◽  
Chloride Concentration ◽  
Fluid Phase ◽  
Classical Pathway ◽  
Factor I ◽  
Nacl Concentration ◽  
The Stability ◽  
Low Ionic Strength ◽  
The Complement System ◽  
Strength Medium

The assembly of the classical-pathway C3 convertase from C4 and I2-treated C2 by the action of C1s is an Mg2(+)-dependent reaction. The Mg2+ concentration necessary for the assembly of C3 convertase in the fluid phase was found to be dependent on NaCl concentration. In the absence of NaCl more than 5 mM-MgCl2 was found to be required, whereas 0.5 mM-MgCl2 was adequate for the assembly of C3 convertase in the presence of 150 mM-NaCl. The C3 convertase assembled in a low-ionic-strength buffer was extremely labile compared with that assembled in buffer of physiological ionic strength, and the stability of C3 convertase was improved with the increase in NaCl concentration. It was found that the stabilizing effect of NaCl on C3 convertase was due to inhibition of the dissociating activity of C2b, which was formed during the assembly of C3 convertase. In addition to the dissociation-accelerating effect, C2b inhibited the assembly of C3 convertase in low-ionic-strength buffer, and this effect also was diminished with increase in NaCl concentration. An increase in NaCl concentration to more than 200 mM resulted in a decrease in the assembly of C3 convertase. This effect was not due to the lability of the assembled C3 convertase but due rather to the inhibition of C2 cleavage by C1s. Purified C3 convertase itself is stable in dilute medium or high-ionic-strength medium such as 500 mM-NaCl, suggesting that the interactions between C4b and C2a are hydrophobic. In these respects C2b seemed to be functionally similar to C4bp, but C2b failed to act as a cofactor for the Factor I-catalysed C4b cleavage.

scholarly journals Optimizing the synthesis and purification of MS2 virus like particles

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Khadijeh Hashemi ◽  
Mohammad Mahdi Ghahramani Seno ◽  
Mohammad Reza Ahmadian ◽  
Bizhan Malaekeh-Nikouei ◽  
Mohammad Reza Bassami ◽  
...  
Keyword(s):  
Size Range ◽  
Therapeutic Agents ◽  
Precipitation Method ◽  
Rna Sequences ◽  
Virus Like Particles ◽  
Bacteriophage Ms2 ◽  
Effects Of Ph ◽  
Peg Precipitation Method ◽  
The Stability

AbstractIntroducing bacteriophage MS2 virus-like particles (VLPs) as gene and drug delivery tools increases the demand for optimizing their production and purification procedure. PEG precipitation method is used efficiently to purify VLPs, while the effects of pH and different electrolytes on the stability, size, and homogeneity of purified MS2 VLPs, and the encapsulated RNA sequences remained to be elucidated. In this regard, a vector, capable of producing VLP with an shRNA packed inside was prepared. The resulting VLPs in different buffers/solutions were assessed for their size, polydispersity index, and ability to protect the enclosed shRNA. We report that among Tris, HEPES, and PBS, with or without NaNO3, and also NaNO3 alone in different pH and ionic concentrations, the 100 mM NaNO3-Tris buffer with pH:8 can be used as a new and optimal MS2 VLP production buffer, capable of inhibiting the VLPs aggregation. These VLPs show a size range of 27-30 nm and suitable homogeneity with minimum 12-month stability at 4 °C. Moreover, the resulting MS2 VLPs were highly efficient and stable for at least 48 h in conditions similar to in vivo. These features of MS2 VLPs produced in the newly introduced buffer make them an appropriate candidate for therapeutic agents’ delivery.

scholarly journals Virus-Like Particles Produced Using the Brome Mosaic Virus Recombinant Capsid Protein Expressed in a Bacterial System

2021 ◽  
Vol 22 (6) ◽  
pp. 3098
Author(s):  
Aleksander Strugała ◽  
Jakub Jagielski ◽  
Karol Kamel ◽  
Grzegorz Nowaczyk ◽  
Marcin Radom ◽  
...  
Keyword(s):  
Ionic Strength ◽  
Mosaic Virus ◽  
Capsid Protein ◽  
Self Assembly ◽  
Environmental Changes ◽  
Expression System ◽  
Brome Mosaic Virus ◽  
Virus Like Particles ◽  
Assembly Principles ◽  
The Impact

Virus-like particles (VLPs), due to their nanoscale dimensions, presence of interior cavities, self-organization abilities and responsiveness to environmental changes, are of interest in the field of nanotechnology. Nevertheless, comprehensive knowledge of VLP self-assembly principles is incomplete. VLP formation is governed by two types of interactions: protein–cargo and protein–protein. These interactions can be modulated by the physicochemical properties of the surroundings. Here, we used brome mosaic virus (BMV) capsid protein produced in an E. coli expression system to study the impact of ionic strength, pH and encapsulated cargo on the assembly of VLPs and their features. We showed that empty VLP assembly strongly depends on pH whereas ionic strength of the buffer plays secondary but significant role. Comparison of VLPs containing tRNA and polystyrene sulfonic acid (PSS) revealed that the structured tRNA profoundly increases VLPs stability. We also designed and produced mutated BMV capsid proteins that formed VLPs showing altered diameters and stability compared to VLPs composed of unmodified proteins. We also observed that VLPs containing unstructured polyelectrolyte (PSS) adopt compact but not necessarily more stable structures. Thus, our methodology of VLP production allows for obtaining different VLP variants and their adjustment to the incorporated cargo.

Effects of pH and ionic strength on the cation exchange capacity of soils with variable charge

Soil Research ◽  
1981 ◽  
Vol 19 (1) ◽  
pp. 93 ◽  
Author(s):  
GP Gillman
Keyword(s):  
Ionic Strength ◽  
Cation Exchange ◽  
Cation Exchange Capacity ◽  
Exchange Capacity ◽  
Surface Soils ◽  
Ph Values ◽  
Variable Charge ◽  
Effects Of Ph ◽  
Variable Charge Soils

The cation exchange capacity of six surface soils from north Queensland and Hawaii has been measured over a range of pH values (4-6) and ionic strength values (0.003-0.05). The results show that for variable charge soils, modest changes in electrolyte ionic strength are as important in their effect on caton exchange capacity as are changes in pH values.

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