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1.
Pediatr Dermatol ; 38(4): 977-979, 2021 Jul.
Article in English | MEDLINE | ID: covidwho-1261162

ABSTRACT

A virtual pediatric dermatology student-run clinic was initiated during the COVID-19 pandemic, when in-person educational opportunities were limited. The clinic's aim is to provide high-quality dermatologic care to a diverse, underserved pediatric patient population while teaching trainees how to diagnose and manage common skin conditions. In our initial eight sessions, we served 37 patients, predominantly those with skin of color, and had a low no-show rate of 9.8%. This report describes the general structure of the clinic, goals, and the patient population to provide an overview of our educational model for those interested in similar efforts.


Subject(s)
COVID-19 , Dermatology , Education, Medical , Telemedicine , Child , Dermatology/education , Humans , Pandemics , Patient Care , SARS-CoV-2 , Students
2.
Protein Sci ; 30(6): 1131-1143, 2021 06.
Article in English | MEDLINE | ID: covidwho-1159117

ABSTRACT

SARS-CoV-2 is the coronavirus responsible for the COVID-19 pandemic. Proteases are central to the infection process of SARS-CoV-2. Cleavage of the spike protein on the virus's capsid causes the conformational change that leads to membrane fusion and viral entry into the target cell. Since inhibition of one protease, even the dominant protease like TMPRSS2, may not be sufficient to block SARS-CoV-2 entry into cells, other proteases that may play an activating role and hydrolyze the spike protein must be identified. We identified amino acid sequences in all regions of spike protein, including the S1/S2 region critical for activation and viral entry, that are susceptible to cleavage by furin and cathepsins B, K, L, S, and V using PACMANS, a computational platform that identifies and ranks preferred sites of proteolytic cleavage on substrates, and verified with molecular docking analysis and immunoblotting to determine if binding of these proteases can occur on the spike protein that were identified as possible cleavage sites. Together, this study highlights cathepsins B, K, L, S, and V for consideration in SARS-CoV-2 infection and presents methodologies by which other proteases can be screened to determine a role in viral entry. This highlights additional proteases to be considered in COVID-19 studies, particularly regarding exacerbated damage in inflammatory preconditions where these proteases are generally upregulated.


Subject(s)
COVID-19/metabolism , Cathepsins/metabolism , SARS-CoV-2/physiology , Spike Glycoprotein, Coronavirus/metabolism , Binding Sites , COVID-19/virology , Host-Pathogen Interactions , Humans , Molecular Docking Simulation , Proteolysis , Recombinant Proteins/metabolism , SARS-CoV-2/chemistry , Spike Glycoprotein, Coronavirus/chemistry , Virus Internalization
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