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1.
EClinicalMedicine ; 2020.
Article | WHO COVID | ID: covidwho-689222

ABSTRACT

BackgroundThe outbreak of a new coronavirus (SARS-CoV-2) poses a great challenge to global public health New and effective intervention strategies are urgently needed to combat the disease

2.
EClinicalMedicine ; 2020.
Article | WHO COVID | ID: covidwho-684336

ABSTRACT

Background The outbreak of a new coronavirus (SARS-CoV-2) poses a great challenge to global public health New and effective intervention strategies are urgently needed to combat the disease Methods We conducted an open-label, non-randomized, clinical trial involving moderate COVID-19 patients according to study protocol Patients were assigned in a 1:2 ratio to receive either aerosol inhalation treatment with IFN-κ and TFF2, every 48 h for three consecutive dosages, in addition to standard treatment (experimental group), or standard treatment alone (control group) The end point was the time to discharge from the hospital This study is registered with chictr org cn, ChiCTR2000030262 Findings A total of thirty-three eligible COVID-19 patients were enrolled from February 1, 2020 to April 6, 2020, eleven were assigned to the IFN-κ plus TFF2 group, and twenty-two to the control group Safety and efficacy were evaluated for both groups No treatment-associated severe adverse effects (SAE) were observed in the group treated with aerosol inhalation of IFN-κ plus TFF2, and no significant differences in the safety evaluations were observed between experimental and control groups CT imaging was performed in all patients with the median improvement time of 5 0 days (IQR 3 0–9 0) in the experimental group versus 8 5 days (IQR 3 0–17 0) in the control group (p<0 05) In addition, the experimental group had a significant shorten median time in cough relief (4 5 days [IQR 2 0–7 0]) than the control group did (10 0 days [IQR 6 0–21 0])(p<0 005), in viral RNA reversion of 6 0 days (IQR 2 0–13 0) in the experimental group vs 9 5 days (IQR 3 0–23 0) in the control group (p < 0 05), and in the median hospitalization stays of 12 0 days (IQR 7 0–20 0) in the experimental group vs 15 0 days (IQR 10 0–25 0) in the control group (p<0 001), respectively Interpretation Aerosol inhalation of IFN-κ plus TFF2 is a safe treatment and is likely to significantly facilitate clinical improvement, including cough relief, CT imaging improvement, and viral RNA reversion, thereby achieves an early release from hospitalization These data support to explore a scale-up trial with IFN-κ plus TFF2 Funding National Major Project for Control and Prevention of Infectious Disease in China, Shanghai Science and Technology Commission, Shanghai Municipal Health Commission

4.
Science ; 2020 Jun 22.
Article in English | MEDLINE | ID: covidwho-610891

ABSTRACT

Developing therapeutics against SARS-CoV-2 could be guided by the distribution of epitopes, not only on the receptor binding domain (RBD) of the Spike (S) protein, but also across the full Spike (S) protein. We isolated and characterized monoclonal antibodies (mAbs) from ten convalescent COVID-19 patients. Three mAbs showed neutralizing activities against authentic SARS-CoV-2. An mAb, named 4A8, exhibits high neutralization potency against both authentic and pseudotyped SARS-CoV-2, but does not bind the RBD. We defined the epitope of 4A8 as the N terminal domain (NTD) of the S protein by determining its cryo-EM structure in complex with the S protein to an overall resolution of 3.1 Angstrom and local resolution of 3.3 Angstrom for the 4A8-NTD interface. This points to the NTD as a promising target for therapeutic mAbs against COVID-19.

7.
Zhejiang Da Xue Xue Bao Yi Xue Ban ; 49(2): 215-219, 2020 May 25.
Article in Chinese | MEDLINE | ID: covidwho-242643

ABSTRACT

OBJECTIVE: To evaluate the efficacy and safety of hydroxychloroquine (HCQ) in the treatment of patients with moderate coronavirus disease 2019 (COVID-19). METHODS: We prospectively enrolled 30 treatment-naïve patients with confirmed COVID-19 after informed consent at Shanghai Public Health Clinical Center. The patients were randomized 1:1 to HCQ group and the control group. Patients in HCQ group were given HCQ 400 mg per day for 5 days plus conventional treatments, while those in the control group were given conventional treatment only. The primary endpoint was negative conversion rate of SARS-CoV-2 nucleic acid in respiratory pharyngeal swab on days 7 after randomization. This study has been approved by the Ethics Committee of Shanghai Public Health Clinical Center and registered online (NCT04261517). RESULTS: One patient in HCQ group developed to severe during the treatment. On day 7, nucleic acid of throat swabs was negative in 13 (86.7%) cases in the HCQ group and 14 (93.3%) cases in the control group (P>0.05). The median duration from hospitalization to virus nucleic acid negative conservation was 4 (1,9) days in HCQ group, which is comparable to that in the control group [2 (1,4) days, Z=1.27, P>0.05]. The median time for body temperature normalization in HCQ group was 1 (0,2) day after hospitalization, which was also comparable to that in the control group [1 (0,3) day]. Radiological progression was shown on CT images in 5 cases (33.3%) of the HCQ group and 7 cases (46.7%) of the control group, and all patients showed improvement in follow-up examinations. Four cases (26.7%) of the HCQ group and 3 cases (20%) of the control group had transient diarrhea and abnormal liver function (P>0.05). CONCLUSIONS: The prognosis of COVID-19 moderate patients is good. Larger sample size study are needed to investigate the effects of HCQ in the treatment of COVID-19. Subsequent research should determine better endpoint and fully consider the feasibility of experiments such as sample size.


Subject(s)
Betacoronavirus , Hydroxychloroquine , Betacoronavirus/isolation & purification , China , Coronavirus Infections/diagnostic imaging , Coronavirus Infections/drug therapy , Humans , Hydroxychloroquine/therapeutic use , Pandemics , Pilot Projects , Pneumonia, Viral/diagnostic imaging , Pneumonia, Viral/drug therapy , RNA, Viral/isolation & purification , Treatment Outcome
8.
J Vet Sci ; 21(1): e12, 2020 Jan.
Article in English | MEDLINE | ID: covidwho-124741

ABSTRACT

Porcine deltacoronavirus (PDCoV) is an emerging swine enteric coronavirus that causes diarrhea in piglets. However, the biological characteristics of PDCoV are unclear. In this study, the hemagglutination (HA) abilities of two PDCoV strains (CH-01 and HNZK-04) were investigated. Our results showed that PDCoV has the ability to agglutinate rabbit erythrocytes after virion pretreatment with trypsin or neuraminidase. Additionally, the HA assay results showed a significant positive correlation with the infectious viral titer. Our results suggest that assessing the HA activity of PDCoV may be a useful diagnostic method for investigating and surveilling PDCoV infections.

9.
Science ; 367(6485): 1444-1448, 2020 03 27.
Article in English | MEDLINE | ID: covidwho-17388

ABSTRACT

Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for severe acute respiratory syndrome-coronavirus (SARS-CoV) and the new coronavirus (SARS-CoV-2) that is causing the serious coronavirus disease 2019 (COVID-19) epidemic. Here, we present cryo-electron microscopy structures of full-length human ACE2 in the presence of the neutral amino acid transporter B0AT1 with or without the receptor binding domain (RBD) of the surface spike glycoprotein (S protein) of SARS-CoV-2, both at an overall resolution of 2.9 angstroms, with a local resolution of 3.5 angstroms at the ACE2-RBD interface. The ACE2-B0AT1 complex is assembled as a dimer of heterodimers, with the collectrin-like domain of ACE2 mediating homodimerization. The RBD is recognized by the extracellular peptidase domain of ACE2 mainly through polar residues. These findings provide important insights into the molecular basis for coronavirus recognition and infection.


Subject(s)
Amino Acid Transport Systems, Neutral/ultrastructure , Peptidyl-Dipeptidase A/ultrastructure , Receptors, Virus/ultrastructure , Spike Glycoprotein, Coronavirus/ultrastructure , Amino Acid Sequence , Betacoronavirus , Coronavirus Infections , Cryoelectron Microscopy , Humans , Models, Molecular , Pandemics , Pneumonia, Viral , Protein Binding , Protein Domains , Protein Multimerization , SARS Virus , Sequence Alignment
10.
Chinese Journal of Organ Transplantation ; (12): E006-E006, 2020.
Article in Chinese | WPRIM (Western Pacific) | ID: covidwho-6561

ABSTRACT

Objective@#To analyze the clinical characteristics of one living-related kidney transplant recipient infected with 2019 coronavirus disease (COVID-19) .@*Method@#The clinical diagnosis and treatment of one relative renal transplant recipient after the occurrence of COVID-19 were analyzed retrospectively, including the course of onset, clinical manifestations, blood routine test, renal function, lung CT scan, nucleic acid detection, outpatient and inpatient therapies and outcomes.@*Result@#The case was diagnosed as COVID-19 (severe type) with influenza A virus infection. The clinical symptoms were gradually relieved and the lung lesions were absorbed through the treatment of reduce and stop taking immunosuppressant, antiviral therapy of abidol/oseltamivir, prevention of bacterial infection, hormone anti-inflammatory, oxygen inhalation, nutritional support and adequate rest.@*Conclusion@#This case present typical characteristics of COVID-19 in epidemiological investigation, clinical manifestation, examination, pulmonary imaging and etiology. After comprehensive treatment including reduce and stop immunosuppressive therapy, clinical cure was achieved. The long-term effect of COVID-19 on this immunosuppressive patient remains follow-up.

11.
Science ; 367(6485): 1444-1448, 2020 03 27.
Article in English | MEDLINE | ID: covidwho-5357

ABSTRACT

Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for severe acute respiratory syndrome-coronavirus (SARS-CoV) and the new coronavirus (SARS-CoV-2) that is causing the serious coronavirus disease 2019 (COVID-19) epidemic. Here, we present cryo-electron microscopy structures of full-length human ACE2 in the presence of the neutral amino acid transporter B0AT1 with or without the receptor binding domain (RBD) of the surface spike glycoprotein (S protein) of SARS-CoV-2, both at an overall resolution of 2.9 angstroms, with a local resolution of 3.5 angstroms at the ACE2-RBD interface. The ACE2-B0AT1 complex is assembled as a dimer of heterodimers, with the collectrin-like domain of ACE2 mediating homodimerization. The RBD is recognized by the extracellular peptidase domain of ACE2 mainly through polar residues. These findings provide important insights into the molecular basis for coronavirus recognition and infection.


Subject(s)
Amino Acid Transport Systems, Neutral/ultrastructure , Peptidyl-Dipeptidase A/ultrastructure , Receptors, Virus/ultrastructure , Spike Glycoprotein, Coronavirus/ultrastructure , Amino Acid Sequence , Betacoronavirus , Coronavirus Infections , Cryoelectron Microscopy , Humans , Models, Molecular , Pandemics , Pneumonia, Viral , Protein Binding , Protein Domains , Protein Multimerization , SARS Virus , Sequence Alignment
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