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1.
Viruses ; 14(4)2022 03 28.
Article in English | MEDLINE | ID: covidwho-1792421

ABSTRACT

Focusing on the transmembrane domains (TMDs) of viral fusion and channel-forming proteins (VCPs), experimentally available and newly generated peptides in an ideal conformation of the S and E proteins of severe acute respiratory syndrome coronavirus type 2 (SARS-CoV-2) and SARS-CoV, gp41 and Vpu, both of human immunodeficiency virus type 1 (HIV-1), haemagglutinin and M2 of influenza A, as well as gB of herpes simplex virus (HSV), are embedded in a fully hydrated lipid bilayer and used in multi-nanosecond molecular dynamics simulations. It is aimed to identify differences in the dynamics of the individual TMDs of the two types of viral membrane proteins. The assumption is made that the dynamics of the individual TMDs are decoupled from their extra-membrane domains, and that the mechanics of the TMDs are distinct from each other due to the different mechanism of function of the two types of proteins. The diffusivity coefficient (DC) of the translational and rotational diffusion is decreased in the oligomeric state of the TMDs compared to those values when calculated from simulations in their monomeric state. When comparing the calculations for two different lengths of the TMD, a longer full peptide and a shorter purely TMD stretch, (i) the difference of the calculated DCs begins to level out when the difference exceeds approximately 15 amino acids per peptide chain, and (ii) the channel protein rotational DC is the most affected diffusion parameter. The rotational dynamics of the individual amino acids within the middle section of the TMDs of the fusion peptides remain high upon oligomerization, but decrease for the channel peptides, with an increasing number of monomers forming the oligomeric state, suggesting an entropic penalty on oligomerization for the latter.


Subject(s)
COVID-19 , Ion Channels , Molecular Dynamics Simulation , Viral Fusion Proteins , Amino Acids , Humans , Ion Channels/ultrastructure , Peptides/chemistry , SARS-CoV-2 , Viral Fusion Proteins/ultrastructure
2.
Viruses ; 14(4):699, 2022.
Article in English | MDPI | ID: covidwho-1762719

ABSTRACT

Focusing on the transmembrane domains (TMDs) of viral fusion and channel-forming proteins (VCPs), experimentally available and newly generated peptides in an ideal conformation of the S and E proteins of severe acute respiratory syndrome coronavirus type 2 (SARS-CoV-2) and SARS-CoV, gp41 and Vpu, both of human immunodeficiency virus type 1 (HIV-1), haemagglutinin and M2 of influenza A, as well as gB of herpes simplex virus (HSV), are embedded in a fully hydrated lipid bilayer and used in multi-nanosecond molecular dynamics simulations. It is aimed to identify differences in the dynamics of the individual TMDs of the two types of viral membrane proteins. The assumption is made that the dynamics of the individual TMDs are decoupled from their extra-membrane domains, and that the mechanics of the TMDs are distinct from each other due to the different mechanism of function of the two types of proteins. The diffusivity coefficient (DC) of the translational and rotational diffusion is decreased in the oligomeric state of the TMDs compared to those values when calculated from simulations in their monomeric state. When comparing the calculations for two different lengths of the TMD, a longer full peptide and a shorter purely TMD stretch, (i) the difference of the calculated DCs begins to level out when the difference exceeds approximately 15 amino acids per peptide chain, and (ii) the channel protein rotational DC is the most affected diffusion parameter. The rotational dynamics of the individual amino acids within the middle section of the TMDs of the fusion peptides remain high upon oligomerization, but decrease for the channel peptides, with an increasing number of monomers forming the oligomeric state, suggesting an entropic penalty on oligomerization for the latter.

3.
Hum Vaccin Immunother ; 18(5): 2050121, 2022 Nov 30.
Article in English | MEDLINE | ID: covidwho-1764460

ABSTRACT

COVID-19 vaccination is an effective intervention preventing individuals from contracting SARS-CoV-2 or transmitting the virus to others. However, in many countries, vaccine hesitancy has impeded the progress of mass vaccination to reach herd immunity. This study aimed to understand the similarities and differences in the determinants of COVID-19 vaccine hesitancy in Taiwan, the United States, the Netherlands, and Haiti. A qualitative study was conducted by face-to-face interviews with participants in Taiwan and remote online interviews with participants in the United States, the Netherlands, and Haiti. In total, 47 interviews were conducted. A reflective thematic analysis was employed to analyze the collected data. Distrust of COVID-19 vaccines was reported by the participants in all countries. A perception of a lack of necessity or urgency to be vaccinated was reported by the Taiwanese and Haitian participants. Lack of knowledge regarding COVID-19 vaccines was reported by the Taiwanese, U.S. and Haitian participants, contributing to hesitation or refusal to vaccination. Regarding misinformation and rumors, misinformation was found among a few Taiwanese and Dutch participants. Additionally, rumors concerning COVID-19 vaccines were mentioned by the Dutch and Haitian participants. Furthermore, a lack of verified information was reported by the participants in all four countries. Overall, the current study suggests that vaccine hesitancy exists among participants in Taiwan, the United States, the Netherlands, and Haiti. Building trust in the COVID-19 vaccine, cultivating vaccine literacy, clarifying misinformation and rumors concerning COVID-19 vaccines, and providing verified information are critical for increasing public acceptance of the COVID-19 vaccine.


Subject(s)
COVID-19 , Vaccines , COVID-19/prevention & control , COVID-19 Vaccines , Haiti/epidemiology , Humans , Netherlands , Patient Acceptance of Health Care , SARS-CoV-2 , Taiwan , Trust , United States , Vaccination , Vaccination Hesitancy
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