The COVID-19 pandemic has resulted in an unprecedented impact on global health, economy, and way of life. SARS-CoV-2, the virus responsible for the disease, utilizes the ACE2 receptor found on host cells to mediate entry, replication, and infection. Numerous studies have elucidated the presence of many components of the renin-angiotensin-aldosterone system (RAAS) in the eye, including the ACE2 receptor. Considering this, and the anatomical vulnerability that the exposed ocular surface offers with its interconnectedness to the respiratory system, there is a theoretical risk of pathogen entry from the ocular route as well as the development of COVID-19-associated eye disease. Despite this, the actual epidemiological data demonstrates low ocular symptoms, possibly due to differing ACE2 receptor expression across age, ethnicity, and sex coupled with the protective properties of tears. We summarize the current literature on ocular RAAS with specific focus on the ACE2 receptor and its interplay with the SARS-CoV-2 virus.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8831072 | PMC |
| http://dx.doi.org/10.1155/2022/9970922 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Structural and Functional Glycosylation of the Abdala COVID-19 Vaccine.
Glycobiology
January 2025
Department of Biochemistry, Dorothy Crowfoot Hodgkin Building, University of Oxford, South Parks Road, OX1 3QU, United Kingdom.
Abdala is a COVID-19 vaccine produced in Pichia pastoris and is based on the receptor-binding domain (RBD) of the SARS-CoV-2 spike. Abdala is currently approved for use in multiple countries with clinical trials confirming its safety and efficacy in preventing severe illness and death. Although P.
View Article and Find Full Text PDFResearch Progress of Food-Derived Antihypertensive Peptides in Regulating the Key Factors of the Renin-Angiotensin System.
Nutrients
December 2024
Key Laboratory of Environmental Medicine and Engineering of Ministry of Education, Department of Nutrition and Food Hygiene, School of Public Health, Southeast University, Nanjing 210009, China.
Food protein-derived antihypertensive peptides have attracted substantial attention as a safer alternative for drugs. The regulation of the renin-angiotensin system (RAS) is an essential aspect underlying the mechanisms of antihypertensive peptides. Most of the identified antihypertensive peptides exhibit the angiotensin-converting enzyme (ACE) inhibitory effect.
View Article and Find Full Text PDFDisrupting SARS-CoV-2 Spike Protein Activity: A Virtual Screening and Binding Assay Study.
Int J Mol Sci
December 2024
Abel Salazar Institute of Biomedical Sciences (ICBAS), University of Porto, 4050-313 Porto, Portugal.
Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) is a respiratory virus that emerged in late 2019 and rapidly spread worldwide, causing the COVID-19 pandemic. The spike glycoprotein (S protein) plays a crucial role in viral target recognition and entry by interacting with angiotensin, converting enzyme 2 (ACE2), the functional receptor for the virus, via its receptor binding domain (RBD). The RBD availability for this interaction can be influenced by external factors, such as fatty acids.
View Article and Find Full Text PDFDevelopment of Ni-ZnO-ACE-2 peptide hybrids as electrochemical devices for SARS-CoV-2 spike protein detection.
Bioelectrochemistry
January 2025
Centro de Ciências Naturais e Humanas, Universidade Federal do ABC, Santo André, São Paulo 09210-580, Brazil. Electronic address:
Owing to fast SARS-CoV-2 mutations, biosensors employing antibodies as biorecognition elements have presented problems with sensitivity and accuracy. To face these challenges, antibodies can be replaced with the human angiotensin converting enzyme 2 (ACE-2), where it has been shown that the affinity between ACE-2 and the receptor binding domain (RBD) increases with the emergence of new variants. Herein, we report on Ni-doped ZnO nanorod electrochemical biosensors employing an ACE-2 peptide (IEEQAKTFLDKFNHEAEDLFYQS-NH) as a biorecognition element for detecting Spike (S) Wild-Type (WT) protein.
View Article and Find Full Text PDFHost cell lectins ASGR1 and DC-SIGN jointly with TMEM106B confer ACE2 independence and imdevimab resistance to SARS-CoV-2 pseudovirus with spike mutation E484D.
J Virol
January 2025
Infection Biology Unit, German Primate Centre - Leibniz Institute for Primate Research, Göttingen, Germany.
The naturally occurring mutation E484D in the spike (S) protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) can render viral entry ACE2 independent and imdevimab resistant. Here, we investigated whether the cellular proteins ASGR1, DC-SIGN, and TMEM106B, which interact with the viral S protein, can contribute to these processes. Employing S protein-pseudotyped particles, we found that expression of ASGR1 or DC-SIGN jointly with TMEM106B allowed for robust entry of mutant E484D into otherwise non-susceptible cells, while this effect was not observed upon separate expression of the single proteins and upon infection with SARS-CoV-2 wild type (WT).
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!