A Spike Protein-Dependent Cellular Factor Other Than the Viral Receptor Is Required for Mouse Hepatitis Virus Entry

Virology ◽  
1993 ◽  
Vol 196 (1) ◽  
pp. 45-56 ◽  
Author(s):  
Kyoko Yokomori ◽  
Miyuki Asanaka ◽  
Stephen A. Stohlman ◽  
Michael M.C. Lai
Keyword(s):  
Hepatitis Virus ◽  
Virus Entry ◽  
Mouse Hepatitis Virus ◽  
Spike Protein ◽  
Viral Receptor ◽  
Cellular Factor

scholarly journals Functional analysis of an epitope in the S2 subunit of the murine coronavirus spike protein: involvement in fusion activity

2000 ◽  
Vol 81 (12) ◽  
pp. 2867-2871 ◽  
Author(s):  
Fumihiro Taguchi ◽  
Yohko K. Shimazaki
Keyword(s):  
Monoclonal Antibody ◽  
Hepatitis Virus ◽  
Virus Entry ◽  
Mouse Hepatitis Virus ◽  
Spike Protein ◽  
Fusion Activity ◽  
S Protein ◽  
Fusion Inhibition ◽  
Hydrophobic Amino Acids ◽  
S Proteins

The monoclonal antibody (MAb) 5B19.2, which has virus-neutralizing and fusion inhibition activities, binds to an epitope (S2A) consisting of nine hydrophobic amino acids in the S2 subunit of the mouse hepatitis virus (MHV) spike (S) protein. This suggests that the S2A epitope may be involved in binding the virus to the MHV receptor and/or in virus–cell fusion. Co-immunoprecipitation analyses demonstrated that while the binding of virus to the receptor was blocked by anti-S1 MAbs, it was not blocked by the S2A antiserum, indicating that S2A was not involved in receptor-binding. The S proteins prepared in this study with mutations in the S2A epitope were either fusogenic or non-fusogenic and their fusogenicity did not correlate with the hydrophobic feature of the S2A epitope. All of these wt and mutated S proteins were similarly transported onto the cell membrane independent of their fusogenicity capability. These results suggest that S2A may mediate the fusion activity of the MHV S protein during virus entry into cells.

scholarly journals Down-regulation of Bgp1a Viral Receptor by Interferon-γ Is Related to the Antiviral State and Resistance to Mouse Hepatitis Virus 3 Infection

Virology ◽  
2000 ◽  
Vol 274 (2) ◽  
pp. 278-283 ◽  
Author(s):  
Ruth C. Vassão ◽  
Milene T. de Franco ◽  
Dieter Hartz ◽  
Manuel Modolell ◽  
Albrecht E. Sippel ◽  
...  
Keyword(s):  
Hepatitis Virus ◽  
Mouse Hepatitis Virus ◽  
Interferon Γ ◽  
Down Regulation ◽  
Viral Receptor ◽  
Antiviral State

scholarly journals Attachment of Mouse Hepatitis Virus to O-Acetylated Sialic Acid Is Mediated by Hemagglutinin-Esterase and Not by the Spike Protein

2010 ◽  
Vol 84 (17) ◽  
pp. 8970-8974 ◽  
Author(s):  
Martijn A. Langereis ◽  
Arno L. W. van Vliet ◽  
Willemijn Boot ◽  
Raoul J. de Groot
Keyword(s):  
Sialic Acid ◽  
Hepatitis Virus ◽  
Mouse Hepatitis Virus ◽  
Protein S ◽  
Sialic Acids ◽  
The Other ◽  
Spike Protein ◽  
Apparent Contrast ◽  
Group A ◽  
New Hosts

ABSTRACT The members of Betacoronavirus phylocluster A possess two types of surface projections, one comprised of the spike protein (S) and the other of hemagglutinin-esterase (HE). Purportedly, these viruses bind to O-acetylated sialic acids (O-Ac-Sias) primarily through S, with HE serving merely as receptor-destroying enzyme. Here, we show that, in apparent contrast to human and ungulate host range variants of Betacoronavirus-1, murine coronaviruses actually bind to O-Ac-Sias via HE exclusively. Apparently, expansion of group A betacoronaviruses into new hosts and niches was accompanied by changes in HE ligand and substrate preference and in the roles of HE and S in Sia receptor usage.

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