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Source: SARS-CoV-2 Research  Jan 21, 2022  4 months ago
High Ionic Concentration, Presence Of Hydrophobic Fatty Acids, And Low Temperature Enhances Binding Behavior SARS-CoV-2 Virus Especially In Meat Plants
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High Ionic Concentration, Presence Of Hydrophobic Fatty Acids, And Low Temperature Enhances Binding Behavior SARS-CoV-2 Virus Especially In Meat Plants
Source: SARS-CoV-2 Research  Jan 21, 2022  4 months ago
A new study by researchers from Texas A&M University-USA has found that environmental conditions with high ionic concentration, presence of hydrophobic fatty acids, and low temperature enhances the binding behavior of both the spike protein and receptor binding domain of SARS-Cov-2 virus. Such environmental conditions are typical in most meat processing plants.


 
Though extensive research has been performed on SARS-CoV-2, the binding behavior of spike (S) protein and receptor binding domain (RBD) of SARS-CoV-2 at different environmental conditions have yet to be studied.
 
The objective of this study was to investigate the effect of temperature, fatty acids, ions, and protein concentration on the binding behavior and rates of association and dissociation between the S protein and RBD of SARS-CoV-2 and the hydrophobic aminopropylsilane (APS) biosensors using biolayer interferometry (BLI) validated with molecular dynamics simulation.
 
The study findings showed that three conditions ie high ionic concentration, presence of hydrophobic fatty acids, and low temperature favor the attachment of S protein and RBD to hydrophobic surfaces.
 
It was found that increasing the temperature within an hour from 0 to 25 °C results in S protein detachment, suggesting that freezing can cause structural changes in the S protein, affecting its binding kinetics at higher temperature. At all the conditions, RBD exhibits lower dissociation capabilities than the full-length S trimer protein, indicating that the separated RBD formed stronger attachment to hydrophobic surfaces compared to when it was included in the S protein.
 
The study findings were published in the peer reviewed journal: Scientific Reports (Nature). https://www.nature.com/articles/s41598-021-04673-y
 
Detailed structural analysis and molecular dynamics simulations have previously revealed that the hydrophobic residues at the angiotensin-converting enzyme 2 (ACE2) surfaces contribute significantly to the strength of its binding to SARS-CoV-2 S protein.
 
It has been found that food processing facilities, such as meat processing plants, typically maintain high humidity and temperatures below 12°C.
 
Along with a high concentration of fat particles in the air, such air properties could enhance the attachment of SARS-CoV-2 to surfaces in these facilities.
 
A past study conducted in Iowa described that a single SARS-CoV-2-infected individual working at a meatpacking plant led to unrestrained spread within the meat facility and consequently in 13 surrounding cities. https://www.medrxiv.org/content/10.1101/2020.06.08.20125534v1
 
A few studies have investigated the clusters of SARS-CoV-2 infections among the workers in the unique environment of meat processing facilities from different aspects, producing evidence that these facilities are far more conducive to SARS-CoV-2 replication and transmission due to their environmental conditions. https://pubmed.ncbi.nlm.nih.gov/34111143/
 
https://pubmed.ncbi.nlm.nih.gov/33012091/
 
While the low tempe rature is known to promote aerosol transmission of SARS-CoV-2, the effect of intermediate temperatures on the attachment of SARS-CoV-2 to surfaces remains largely unknown.
 
The research team from Texas A&M University studied the effect of temperature, fatty acids, ions, and protein concentration on the binding behavior of the S protein and RBD of SARS-CoV-2. The team presented the binding curves fitted to the local model using the BLItz Pro 1.3 Software (ForteBio).
 
The SARS-CoV-2 Research team also performed bio-layer interferometry (BLI) for the kinetic analysis of each of the prepared samples of S protein and RBD of SARS-CoV-2 mixed with different substances or exposed to different temperatures, using the personal assay BLItz system with aminopropylsilane (APS) biosensors.
 
The found determined rates of association and dissociation of S protein and RBD were validated using molecular dynamics simulation, and these calculations were displayed in the BLItz Pro 1.3 Software from ForteBio.
 
The study team analyzed each sample by the BLI at least twice to ensure the reproducibility of the results. Also, they used APS biosensor and phosphate-buffered saline (PBS) in the same manner before each experiment for serving as the reference correction for each assay.
 
The study findings showed that three environmental conditions were conducive to the attachment of the purified S protein and its receptor-binding domain to hydrophobic surfaces - high ionic concentration, presence of hydrophobic fatty acids, and low temperature.
 
It was also found that exposing the S protein to a wide range of temperatures from 0 °C to 25 °C within one hour resulted in S protein detachment, suggesting that freezing induced structural changes in the S protein that affected its binding kinetics, and S recovered only at a higher temperature later.
 
By experimenting under such conditions, the study team could simulate the sudden temperature drop commonly seen in meat processing plants when workers move from breakrooms to chiller or fabrication rooms. In these facilities, breakrooms have warmer temperatures of 25 °C, and the chiller or fabrication rooms usually have temperatures below 12 °C due to the presence of dry ice containers to keep the products safe during processing. As SARS-CoV-2 disseminates via aerosols, there is a possibility that it gets transported with the airflow through the openings between these locations, exposing more workers to SARS-CoV-2 infection.
 
It was found that under all the studied environmental conditions, RBD exhibited lower dissociation capabilities than the full-length S trimer protein, indicating it had a stronger attachment to hydrophobic surfaces alone than while residing within the S protein.
 
In addition, as revealed by MD simulation, the presence of fatty acid molecules significantly increased the hydrophobic surface area of RBD, altering its binding ability.
 
Environmental conditions, including low temperature, high humidity, and presence of fatty acids, of meat processing plants enhanced the binding of the SARS-CoV-2 to hydrophobic surfaces, making it impossible to remove the virus through typical sanitation procedures such as ventilation and hosing.
 
Furthermore, the enhanced attachment of the virus to equipment surfaces and workers’ clothes imposed higher risks of contact transmission.

Interestingly it was found that another condition that further contributed to higher SARS-CoV-2 transmission inside meat processing plants was the presence of fat particles in the air.
 
These fat aerosols strongly adhered to SARS-CoV-2 S protein got entrained in the ventilated airflow and traveled for a longer distance, increasing the chances of airborne SARS-CoV-2 transmission.
 
The study team based on the research findings, recommended several modifications to change the environmental conditions of food processing facilities and help protect public health and safety.
 
The study team recommended changing the sanitation and cleaning procedures in meat processing plants, such as hosing the floors and workbenches with warm water, heating all surfaces temporarily before cleaning, and lowering humidity by enhancing ventilation. All these measures could increase the chances of SARS-CoV-2 elimination from these facilities and the efficiency of sanitization procedures, thereby providing a safer environment to protect workers.
 
The study team also suggested that further detailed research is warranted to examine the binding kinetics of the SARS-CoV-2 S proteins under higher S protein concentrations and intermediate temperatures between 0 °C and 37 °C.
 
For the latest SARS-CoV-2 Research, keep on logging to Thailand Medical News.
 
 
 

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