scholarly journals Host-membrane interacting interface of the SARS coronavirus envelope protein: Immense functional potential of C-terminal domain

2020 ◽  
Vol 266 ◽  
pp. 106452 ◽  
Author(s):  
Shruti Mukherjee ◽  
Dipita Bhattacharyya ◽  
Anirban Bhunia
2021 ◽  
Vol 102 (6) ◽  
Author(s):  
Wasusit Somsoros ◽  
Takeshi Sangawa ◽  
Katsuki Takebe ◽  
Jakrada Attarataya ◽  
Kanokpan Wongprasert ◽  
...  

White spot syndrome virus (WSSV) is the most virulent pathogen causing high mortality and economic loss in shrimp aquaculture and various crustaceans. Therefore, the understanding of molecular mechanisms of WSSV infection is important to develop effective therapeutics to control the spread of this viral disease. In a previous study, we found that VP37 could bind with shrimp haemocytes through the interaction between its C-terminal domain and heparin-like molecules on the shrimp cells, and this interaction can also be inhibited by sulphated galactan. In this study, we present the crystal structure of C-terminal domain of VP37 from WSSV at a resolution of 2.51 Å. The crystal structure contains an eight-stranded β-barrel fold with an antiparallel arrangement and reveals a trimeric assembly. Moreover, there are two sulphate binding sites found in the position corresponding to R213 and K257. In order to determine whether these sulphate binding sites are involved in binding of VP37 to heparin, mutagenesis was performed to replace these residues with alanine (R213A and K257A), and the Surface Plasmon Resonance (SPR) system was used to study the interaction of each mutated VP37 with heparin. The results showed that mutants R213A and K257A exhibited a significant loss in heparin binding activity. These findings indicated that the sites of R213 and K257 on the C-terminal domain of envelope protein VP37 are essential for binding to sulphate molecules of heparin. This study provides further insight into the structure of C-terminal domain of VP37 and it is anticipated that the structure of VP37 might be used as a guideline for development of antivirus agent targeting on the VP37 protein.


2005 ◽  
Vol 280 (24) ◽  
pp. 23280-23286 ◽  
Author(s):  
I-Mei Yu ◽  
Christin L. T. Gustafson ◽  
Jianbo Diao ◽  
John W. Burgner ◽  
Zhihong Li ◽  
...  

Cell ◽  
1990 ◽  
Vol 61 (6) ◽  
pp. 979-989 ◽  
Author(s):  
Ulf Nehrbass ◽  
Hildegard Kern ◽  
Ann Mutvei ◽  
Heinz Horstmann ◽  
Brigitte Marshallsay ◽  
...  

Author(s):  
Gertjan Medema ◽  
Leo Heijnen ◽  
Goffe Elsinga ◽  
Ronald Italiaander

AbstractIn the current COVID-19 pandemic, a significant proportion of cases shed SARS-Coronavirus-2 (SARS-CoV-2) with their faeces. To determine if SARS-CoV-2 is present in sewage during the emergence of COVID-19 in the Netherlands, sewage samples of 7 cities and the airport were tested using RT-PCR against three fragments of the nucleocapsid protein gene (N1-3) and one fragment of the envelope protein gene (E). No SARS-CoV-2 was detected in samples of February 6, three weeks before the first case was reported in the Netherlands on February 27. On March 5, the N1 fragment was detected in sewage of five sites. On March 15/16, the N1 fragment was detected in sewage of six sites, and the N3 and E fragment were detected at 5 and 4 sites respectively. This is the first report of detection of SARS-CoV-2 in sewage. The detection of the virus in sewage, even when the COVID-19 prevalence is low, indicates that sewage surveillance could be a sensitive tool to monitor the circulation of the virus in the population.


2007 ◽  
Vol 16 (9) ◽  
pp. 2065-2071 ◽  
Author(s):  
Jaume Torres ◽  
Uma Maheswari ◽  
Krupakar Parthasarathy ◽  
Lifang Ng ◽  
Ding Xiang Liu ◽  
...  

2009 ◽  
Vol 5 (7) ◽  
pp. e1000511 ◽  
Author(s):  
Konstantin Pervushin ◽  
Edward Tan ◽  
Krupakar Parthasarathy ◽  
Xin Lin ◽  
Feng Li Jiang ◽  
...  

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