Oral cavity infection by the SARS-CoV-2: emphasizing the essence of masking and peptide therapeutics

The SARS-CoV-2 has infected many people globally with the ravaging COVID-19; a disease, which has become challenging for every aspect of modern healthcare. The saliva and oral mucosa are sites of high risk for increased viral loads, and aside from the usual epithelial functions like lining and prote...

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Bibliographic Details
Published in:Egyptian Journal of Medical Human Genetics 2022-01, Vol.23 (1), p.1-7
Main Authors: Ibiang, Glory Omini, Malachi, Joseph, Ibiang, Mercy Omini, Chukwudi, Daniel Kenechi, Durojaye, Olanrewaju Ayodeji
Format: Article
Language:English
Subjects:
ACE2
Angiotensin-converting enzyme 2
Aprotinin
Blood pressure
Cathepsin L
Correspondence
COVID-19
Cytoplasm
Health aspects
Homeopathy
Homeostasis
Mastication
Materia medica and therapeutics
Mucosa
Nucleocapsids
Oral cavity
Peptides
Protease inhibitors
Proteases
Proteinase inhibitors
Proteolysis
Saliva
SARS-CoV-2
Severe acute respiratory syndrome coronavirus 2
Spike glycoprotein
Taste perception
Therapeutics
TMPRSS2
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Summary:The SARS-CoV-2 has infected many people globally with the ravaging COVID-19; a disease, which has become challenging for every aspect of modern healthcare. The saliva and oral mucosa are sites of high risk for increased viral loads, and aside from the usual epithelial functions like lining and protection, the oral mucosa is also specialized for crucial functions, such as secretion, mastication, sensory perception, and taste perception. The human ACE2 receptor has been extensively studied for its essential role in the regulation of blood pressure homeostasis. However, scRNA-Seq studies have revealed high expression levels of the protein in keratinized epithelial surfaces of the oral cavity. The SARS-CoV-2 have access to the host's body by binding to the ACE2 receptor, leading to the cleavage and major conformational changes in the viral spike glycoprotein for the release of its nucleocapsid into the cellular cytoplasm. This proteolytic cleavage is carried out by the TMPRSS2 and cathepsin L. In this study, we harnessed the information from the binding interface of TMPRSS2 and PAI-1 (a protease inhibitor known to inhibit the TMPRSS2 and several other proteases) to design a potential therapeutic peptide for the inhibition of the TMPRSS2, while also emphasizing the need for preventive masking.
ISSN:1110-8630
2090-2441
DOI:10.1186/s43042-022-00213-z