更新于：2024-11-01

SARS-CoV-2 E protein

更新于：2024-11-01

基本信息

别名-

简介-

关联

项与 SARS-CoV-2 E protein 相关的药物

PRAK-03202

靶点

SARS-CoV-2 E protein x SARS-CoV-2 M protein x SARS-CoV-2 S protein

作用机制

SARS-CoV-2 E protein抑制剂 [+2]

在研机构

Premas Biotech Pvt Ltd.

原研机构

Premas Biotech Pvt Ltd.

在研适应症

新型冠状病毒感染

非在研适应症-

最高研发阶段临床1期

首次获批国家/地区-

首次获批日期1800-01-20

Multiepitope vaccines(Pontifical Catholic University of Rio de Janeiro)

靶点

SARS-CoV-2 3CLpro x SARS-CoV-2 E protein x SARS-CoV-2 N protein x SARS-CoV-2 S protein

作用机制

SARS-CoV 3CLpro抑制剂 [+3]

在研机构

Pontifícia Universidade Católica do Rio de Janeiro

原研机构

Pontifícia Universidade Católica do Rio de Janeiro

在研适应症

冠状病毒感染

非在研适应症-

最高研发阶段临床前

首次获批国家/地区-

首次获批日期1800-01-20

rVSV-msp-SF-Gtc

靶点

SARS-CoV-2 E protein x SARS-CoV-2 S protein

作用机制

SARS-CoV-2 E protein抑制剂 [+1]

在研机构-

原研机构

Sumagen Co., Ltd.

在研适应症-

非在研适应症

冠状病毒感染

最高研发阶段无进展

首次获批国家/地区-

首次获批日期1800-01-20

100 项与 SARS-CoV-2 E protein 相关的临床结果

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100 项与 SARS-CoV-2 E protein 相关的转化医学

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0 项与 SARS-CoV-2 E protein 相关的专利（医药）

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项与 SARS-CoV-2 E protein 相关的文献（医药）

2022-09-05·ChemBioChem

Synthetic α‐Helical Peptides as Potential Inhibitors of the ACE2 SARS‐CoV‐2 Interaction

Article

作者: Hackenberger, Christian P. R. ; Neudörfl, Jörg‐Martin ; Schmalz, Hans‐Günther ; Florez‐Rueda, Sebastián ; Neundorf, Ines ; Kühne, Ronald ; Engelhardt, Pascal M. ; Drexelius, Marco ; Lauster, Daniel

AbstractDuring viral cell entry, the spike protein of SARS‐CoV‐2 binds to the α1‐helix motif of human angiotensin‐converting enzyme 2 (ACE2). Thus, alpha‐helical peptides mimicking this motif may serve as inhibitors of viral cell entry. For this purpose, we employed the rigidified diproline‐derived module ProM‐5 to induce α‐helicity in short peptide sequences inspired by the ACE2 α1‐helix. Starting with Ac‐QAKTFLDKFNHEAEDLFYQ‐NH2 as a relevant section of α1, a series of peptides, N‐capped with either Ac‐βHAsp‐[ProM‐5] or Ac‐βHAsp‐PP, were prepared and their α‐helicities were investigated. While ProM‐5 clearly showed a pronounced effect, an even increased degree of helicity (up to 63 %) was observed in sequences in which non‐binding amino acids were replaced by alanine. The binding affinities of the peptides towards the spike protein, as determined by means of microscale thermophoresis (MST), revealed only a subtle influence of the α‐helical content and, noteworthy, led to the identification of an Ac‐βHAsp‐PP‐capped peptide displaying a very strong binding affinity (KD=62 nM).

2021-12-01·Cardiovascular Diabetology

Correction to: Expression of the SARS‑CoV‑2 receptorACE2 in human heart is associated with uncontrolled diabetes, obesity, and activation of the renin angiotensin system

作者: Herman-Edelstein, Michal ; Hochhauser, Edith ; Guetta, Tali ; Ben-Dor, Naomi ; Barnea, Amir ; Aravot, Dan ; Waldman, Maayan ; Barac, Yaron D ; Arad, Michael ; Kornowski, Ran

Diabetic and obese patients are at higher risk of severe disease and cardiac injury in corona virus 2 (SARS-CoV-2) infections. Cellular entry of SARS-CoV-2 is mainly via the angiotensin-converting enzyme 2 (ACE2) receptor, which is highly expressed in normal hearts. There is a disagreement regarding the effect of factors such as obesity and diabetes on ACE2 expression in the human heart and whether treatment with renin–angiotensin system inhibitors or anti-diabetic medications increases ACE2 expression and subsequently the susceptibility to infection. We designed this study to elucidate factors that control ACE2 expression in human serum, human heart biopsies, and mice. Right atrial appendage biopsies were collected from 79 patients that underwent coronary artery bypass graft (CABG) surgery. We investigated the alteration in ACE2 mRNA and protein expression in heart tissue and serum. ACE2 expression was compared with clinical risk factors: diabetes, obesity and different anti-hypertensive or anti-diabetic therapies. WT or db/db mice were infused with Angiotensin II (ATII), treated with different anti-diabetic drugs (Metformin, GLP1A and SGLT2i) were also tested. ACE2 gene expression was increased in diabetic hearts compared to non-diabetic hearts and was positively correlated with glycosylated hemoglobin (HbA1c), body mass index (BMI), and activation of the renin angiotensin system (RAS), and negatively correlated with ejection fraction. ACE2 was not differentially expressed in patients who were on angiotensin converting enzyme inhibitors (ACEi) or angiotensin receptor blockers (ARBs) prior to the operation. We found no correlation between plasma free ACE2 and cardiac tissue ACE2 expression. Transmembrane serine protease 2 (TMPRSS2), metalloprotease ADAM10 and ADAM17 that facilitate viral-ACE2 complex entry and degradation were increased in diabetic hearts. ACE2 expression in mice was increased with ATII infusion and attenuated following anti-diabetic drugs treatment. Patients with uncontrolled diabetes or obesity with RAS activation have higher ACE2 expressions therefore are at higher risk for severe infection. Since ACEi or ARBs show no effect on ACE2 expression in the heart further support their safety.

2021-01-01·Journal of Clinical and Translational Science

Detecting SARS-CoV-2 Orf3a and E ion channel activity in COVID-19 blood samples

Article

作者: Yu, Han-Gang ; Smoot, Katy ; Perrotta, Peter ; Sizemore, Gina

AbstractBackground:SARS-CoV-2 has been found in the heart of COVID-19 patients. It is unclear how the virus passes from the upper respiratory tract to the myocardium. We hypothesized that SARS-CoV-2 is present in the blood of COVID-19 infected patients, spreading to other organs such as heart.Methods:We targeted two viroporins, Orf3a and E, in SARS-CoV-2. Orf3a and E form non-voltage-gated ion channels. A combined fluorescence potassium ion assay with three channel modulators (4-aminopyridine, emodin-Orf3a channel blocker, and gliclazide-E channel blocker) was developed to detect SARS-CoV-2 Orf3a/E channel activity. In blood samples, we subtracted the fluorescence signals in the absence and presence of emodin/gliclazide to detect Orf3a and E channel activity.Results:In lentivirus-spiked samples, we detected significant channel activity of Orf3a/E based on increase in fluorescence induced by 4-aminopyridine, and this increase in fluorescence was inhibited by emodin and gliclazide. In 18 antigen/PCR-positive samples, our test results found 15 are positive, demonstrating 83.3% concordance. In 24 antigen/PCR-negative samples, our test results found 21 are negative, showing 87.5% concordance.Conclusions:We developed a cell-free test that can detect Orf3a/E channel activity of SARS-CoV-2 in blood samples from COVID-19-infected individuals, confirming a hypothesis that the virus spreads to the heart via blood circulation.