Document Detail


Amino acid substitutions within the leucine zipper domain of the murine coronavirus spike protein cause defects in oligomerization and the ability to induce cell-to-cell fusion.
MedLine Citation:
PMID:  10482565     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The murine coronavirus spike (S) protein contains a leucine zipper domain which is highly conserved among coronaviruses. To assess the role of this leucine zipper domain in S-induced cell-to-cell fusion, the six heptadic leucine and isoleucine residues were replaced with alanine by site-directed mutagenesis. The mutant S proteins were analyzed for cell-to-cell membrane fusion activity as well as for progress through the glycoprotein maturation process, including intracellular glycosylation, oligomerization, and cell surface expression. Single-alanine-substitution mutations had minimal, if any, effects on S-induced cell-to-cell fusion. Significant reduction in fusion activity was observed, however, when two of the four middle heptadic leucine or isoleucine residues were replaced with alanine. Double alanine substitutions that involved either of the two end heptadic leucine residues did not significantly affect fusion. All double-substitution mutant S proteins displayed levels of endoglycosidase H resistance and cell surface expression similar to those of the wild-type S. However, fusion-defective double-alanine-substitution mutants exhibited defects in S oligomerization. These results indicate that the leucine zipper domain plays a role in S-induced cell-to-cell fusion and that the ability of S to induce fusion may be dependent on the oligomeric structure of S.
Authors:
Z Luo; A M Matthews; S R Weiss
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of virology     Volume:  73     ISSN:  0022-538X     ISO Abbreviation:  J. Virol.     Publication Date:  1999 Oct 
Date Detail:
Created Date:  1999-10-12     Completed Date:  1999-10-12     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  8152-9     Citation Subset:  IM    
Affiliation:
Department of Microbiology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-6076, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Amino Acid Substitution
Animals
Cell Fusion
Cell Line
Coronavirus / physiology*
Leucine Zippers / genetics
Membrane Glycoproteins / physiology*
Mice
Molecular Sequence Data
Point Mutation*
Viral Envelope Proteins / physiology*
Virus Replication / genetics*
Grant Support
ID/Acronym/Agency:
NS-21954/NS/NINDS NIH HHS; NS-30606/NS/NINDS NIH HHS; T32 AI07324/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Membrane Glycoproteins; 0/Viral Envelope Proteins; 107476-75-5/spike glycoprotein, coronavirus
Comments/Corrections

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