Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1991 Apr;65(4):1916-28.
doi: 10.1128/JVI.65.4.1916-1928.1991.

Alteration of the pH dependence of coronavirus-induced cell fusion: effect of mutations in the spike glycoprotein

Affiliations

Alteration of the pH dependence of coronavirus-induced cell fusion: effect of mutations in the spike glycoprotein

T M Gallagher et al. J Virol. 1991 Apr.

Abstract

Infection of susceptible murine cells with the coronavirus mouse hepatitis virus type 4 (MHV4) results in extensive cell-cell fusion at pHs from 5.5 to 8.5. The endosomotropic weak bases chloroquine and ammonium chloride do not prevent MHV4 infection. In marked contrast, we have selected variants from a neural cell line persistently infected with MHV4 which are entirely dependent on acid pH to fuse host cells and are strongly inhibited by endosomotropic weak bases. Wild-type and variant viruses were compared at the level of the fusion-active surface (S) glycoprotein gene. Cloning and sequencing of each 4,131-base open reading frame predicted a total of eight amino acid differences which fell into three distinct clusters. Each S glycoprotein, when expressed from cDNA, was synthesized in equivalent amounts, and similar proportions were transported to the cell surface. Wild-type S induced cell-cell fusion at neutral pH, whereas variant S required prolonged exposure to acidic pH to induce fusion. Expression of hybrid S genes prepared by exchange of restriction fragments between wild-type and variant cDNAs revealed that elimination of neutral pH fusion was solely dependent on amino acid alterations at positions 1067 (Q to H), 1094 (Q to H), and 1114 (L to R). These changes lie within a predicted heptad repeat region of the transmembrane cleavage fragment of S (S2). These findings demonstrate that the pH dependence of coronavirus fusion is highly variable and that this variability can be determined by as few as three amino acid residues.

PubMed Disclaimer

References

    1. J Virol. 1980 Jan;33(1):449-62 - PubMed
    1. Annu Rev Biophys Biophys Chem. 1989;18:187-211 - PubMed
    1. J Immunol. 1976 Nov;117(5 Pt 1):1482-90 - PubMed
    1. J Exp Med. 1978 Aug 1;148(2):408-23 - PubMed
    1. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463-7 - PubMed

Publication types

MeSH terms

LinkOut - more resources