[7] Synthetic peptides as probes of function of viral envelope proteins

1993 ◽  
pp. 82-95 ◽  
Author(s):  
Nejat Düzgüneş
Keyword(s):  
Synthetic Peptides ◽  
Envelope Proteins ◽  
Viral Envelope ◽  
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.

Polarized distribution of viral envelope proteins in the plasma membrane of infected epithelial cells

Cell ◽  
1980 ◽  
Vol 20 (1) ◽  
pp. 45-54 ◽  
Author(s):  
Enrique Rodriguez Boulan ◽  
Maryanne Pendergast
Keyword(s):  
Plasma Membrane ◽  
Epithelial Cells ◽  
Envelope Proteins ◽  
Viral Envelope ◽  
Viral Envelope Proteins

scholarly journals Hydrophobic Inactivation of Influenza Viruses Confers Preservation of Viral Structure with Enhanced Immunogenicity

2008 ◽  
Vol 82 (9) ◽  
pp. 4612-4619 ◽  
Author(s):  
Yossef Raviv ◽  
Robert Blumenthal ◽  
S. Mark Tompkins ◽  
Jennifer Humberd ◽  
Robert J. Hogan ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Virus Infection ◽  
Cell Membrane ◽  
Target Cell ◽  
Envelope Proteins ◽  
Viral Envelope ◽  
Live Virus ◽  
Target Cell Membrane ◽  
Ph Dependent ◽  
Viral Envelope Proteins

ABSTRACT The use of inactivated influenza virus for the development of vaccines with broad heterosubtypic protection requires selective inactivation techniques that eliminate viral infectivity while preserving structural integrity. Here we tested if a hydrophobic inactivation approach reported for retroviruses could be applied to the influenza virus. By this approach, the transmembrane domains of viral envelope proteins are selectively targeted by the hydrophobic photoactivatable compound 1,5-iodonaphthyl-azide (INA). This probe partitions into the lipid bilayer of the viral envelope and upon far UV irradiation reacts selectively with membrane-embedded domains of proteins and lipids while the protein domains that localize outside the bilayer remain unaffected. INA treatment of influenza virus blocked infection in a dose-dependent manner without disrupting the virion or affecting neuraminidase activity. Moreover, the virus maintained the full activity in inducing pH-dependent lipid mixing, but pH-dependent redistribution of viral envelope proteins into the target cell membrane was completely blocked. These results indicate that INA selectively blocks fusion of the virus with the target cell membrane at the pore formation and expansion step. Using a murine model of influenza virus infection, INA-inactivated influenza virus induced potent anti-influenza virus serum antibody and T-cell responses, similar to live virus immunization, and protected against heterosubtypic challenge. INA treatment of influenza A virus produced a virus that is noninfectious, intact, and fully maintains the functional activity associated with the ectodomains of its two major envelope proteins, neuraminidase and hemagglutinin. When used as a vaccine given intranasally (i.n.), INA-inactivated influenza virus induced immune responses similar to live virus infection.

scholarly journals HIV-1 Envelope Glycoprotein at the Interface of Host Restriction and Virus Evasion

Viruses ◽  
2019 ◽  
Vol 11 (4) ◽  
pp. 311 ◽  
Author(s):  
Saina Beitari ◽  
Yimeng Wang ◽  
Shan-Lu Liu ◽  
Chen Liang
Keyword(s):  
Viral Infection ◽  
Adaptive Immunity ◽  
Viral Entry ◽  
Envelope Protein ◽  
Envelope Proteins ◽  
Viral Envelope ◽  
Innate Immune ◽  
Host Restriction ◽  
Hiv 1 ◽  
Viral Envelope Proteins

Without viral envelope proteins, viruses cannot enter cells to start infection. As the major viral proteins present on the surface of virions, viral envelope proteins are a prominent target of the host immune system in preventing and ultimately eliminating viral infection. In addition to the well-appreciated adaptive immunity that produces envelope protein-specific antibodies and T cell responses, recent studies have begun to unveil a rich layer of host innate immune mechanisms restricting viral entry. This review focuses on the exciting progress that has been made in this new direction of research, by discussing various known examples of host restriction of viral entry, and diverse viral countering strategies, in particular, the emerging role of viral envelope proteins in evading host innate immune suppression. We will also highlight the effective cooperation between innate and adaptive immunity to achieve the synergistic control of viral infection by targeting viral envelope protein and checking viral escape. Given that many of the related findings were made with HIV-1, we will use HIV-1 as the model virus to illustrate the basic principles and molecular mechanisms on host restriction targeting HIV-1 envelope protein.

Iscom of viral envelope proteins protects against Aujeszky's disease

1989 ◽  
Vol 20 (2) ◽  
pp. 143-154 ◽  
Author(s):  
B. Morein ◽  
S. Belák ◽  
T. Soós ◽  
M. Rusvai ◽  
B.S. McGwire ◽  
...  
Keyword(s):  
Envelope Proteins ◽  
Viral Envelope ◽  
Aujeszky's Disease ◽  
Aujeszky’S Disease ◽  
Viral Envelope Proteins
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