scholarly journals Guanylate-Binding Proteins 2 and 5 Exert Broad Antiviral Activity by Inhibiting Furin-Mediated Processing of Viral Envelope Proteins

Cell Reports ◽  
2019 ◽  
Vol 27 (7) ◽  
pp. 2092-2104.e10 ◽  
Author(s):  
Elisabeth Braun ◽  
Dominik Hotter ◽  
Lennart Koepke ◽  
Fabian Zech ◽  
Rüdiger Groß ◽  
...  
Keyword(s):  
Antiviral Activity ◽  
Binding Proteins ◽  
Envelope Proteins ◽  
Viral Envelope ◽  
Viral Envelope Proteins

scholarly journals Potent in vitro antiviral activity of Cistus incanus extract against HIV and Filoviruses targets viral envelope proteins

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Stephanie Rebensburg ◽  
Markus Helfer ◽  
Martha Schneider ◽  
Herwig Koppensteiner ◽  
Josef Eberle ◽  
...  
Keyword(s):  
Antiviral Activity ◽  
Envelope Proteins ◽  
Viral Envelope ◽  
Cistus Incanus ◽  
Viral Envelope Proteins

scholarly journals Mammalian cell surface display for monoclonal antibody-based FACS selection of viral envelope proteins

mAbs ◽  
2017 ◽  
Vol 9 (7) ◽  
pp. 1052-1064 ◽  
Author(s):  
Tim-Henrik Bruun ◽  
Veronika Grassmann ◽  
Benjamin Zimmer ◽  
Benedikt Asbach ◽  
David Peterhoff ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Cell Surface ◽  
Mammalian Cell ◽  
Surface Display ◽  
Cell Surface Display ◽  
Envelope Proteins ◽  
Viral Envelope ◽  
Selection Of ◽  
Viral Envelope Proteins

scholarly journals Cellular actin-binding ezrin-radixin-moesin (ERM) family proteins are incorporated into the rabies virion and closely associated with viral envelope proteins in the cell

Virology ◽  
1995 ◽  
Vol 206 (1) ◽  
pp. 485-494 ◽  
Author(s):  
Junji Sagara ◽  
Sachiko Tsukita ◽  
Shigenobu Yonemura ◽  
Shoichiro Tsukita ◽  
Akihiko Kawai
Keyword(s):  
Envelope Proteins ◽  
Viral Envelope ◽  
Actin Binding ◽  
Viral Envelope Proteins

scholarly journals Identification of H209 as Essential for pH 8-Triggered Receptor-Independent Syncytium Formation by S Protein of Mouse Hepatitis Virus A59

2018 ◽  
Vol 92 (11) ◽  
Author(s):  
Pei Li ◽  
Yiwei Shan ◽  
Wangliang Zheng ◽  
Xiuyuan Ou ◽  
Dan Mi ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Conformational Changes ◽  
Hepatitis Virus ◽  
Mouse Hepatitis Virus ◽  
Envelope Proteins ◽  
Viral Envelope ◽  
S Protein ◽  
The Stability ◽  
Virus Fitness ◽  
Viral Envelope Proteins

ABSTRACTThe spike glycoprotein (S) of murine coronavirus mouse hepatitis virus (MHV) strain A59 uses murine carcinoembryonic antigen-related cell adhesion molecule 1a as its receptor for cell entry, but S protein can also be triggered in the absence of receptor by pH 8.0 alone at 37°C. The mechanism by which conformational changes of this S glycoprotein can be triggered by pH 8.0 has not yet been determined. Here, we show that MHV-A59 S protein is triggered by pH 8.0 at 37°C to induce receptor-independent syncytium (RIS) formation on 293T cells, and that the conformational changes in S proteins triggered by pH 8.0 are very similar to those triggered by receptor binding. We systemically mutated each of 15 histidine residues in S protein and found that H209 is essential for pH 8.0-triggered RIS formation, while H179, H441, H643, and H759 also play important roles in this process. Replacement of H209 with Ala had no effect on receptor binding, but in murine 17Cl.1 cells mutant H209A MHV-A59 showed delayed growth kinetics and was readily outcompeted by wild-type virus when mixed together, indicating that the H209A mutation caused a defect in virus fitness. Finally, the H209A mutation significantly increased the thermostability of S protein in its prefusion conformation, which may raise the energy barrier for conformational change of S protein required for membrane fusion and lead to a decrease in virus fitness in cell culture. Thus, MHV-A59 may have evolved to lower the stability of its S protein in order to increase virus fitness.IMPORTANCEEnveloped viruses enter cells through fusion of viral and cellular membranes, and the process is mediated by interactions between viral envelope proteins and their host receptors. In the prefusion conformation, viral envelope proteins are metastable, and activation to the fusion conformation is tightly regulated, since premature activation would lead to loss of viral infectivity. The stability of viral envelope proteins greatly influences their activation and virus fitness. Here, we report that, similar to the A82V mutation in Ebola glycoprotein, in the S glycoprotein of murine coronavirus MHV-A59, the histidine residue at position of 209 significantly affects the thermal stability of the S protein, determines whether S protein can be activated at 37°C by either pH 8.0 alone or by receptor binding, and affects viral fitness in cell culture. Thus, the spike glycoprotein of MHV-A59 has evolved to retain histidine at position 209 to optimize virus fitness.

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