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PMID:1370493

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Citation

Wahlberg, JM and Garoff, H (1992) Membrane fusion process of Semliki Forest virus. I: Low pH-induced rearrangement in spike protein quaternary structure precedes virus penetration into cells. J. Cell Biol. 116:339-48

Abstract

The Semliki Forest virus (SFV) directs the synthesis of a heterodimeric membrane protein complex which is used for virus membrane assembly during budding at the surface of the infected cell, as well as for low pH-induced membrane fusion in the endosomes when particles enter new host cells. Existing evidence suggests that the E1 protein subunit carries the fusion potential of the heterodimer, whereas the E2 subunit, or its intracellular precursor p62, is required for binding to the nucleocapsid. We show here that during virus uptake into acidic endosomes the original E2E1 heterodimer is destabilized and the E1 proteins form new oligomers, presumably homooligomers, with altered E1 structure. This altered structure of E1 is specifically recognized by a monoclonal antibody which can also inhibit penetration of SFV into host cells as well as SFV-mediated cell-cell fusion, thus suggesting that the altered E1 structure is important for the membrane fusion. These results give further support for a membrane protein oligomerization-mediated control mechanism for the membrane fusion potential in alphaviruses.

Links

PubMed PMC2289294

Keywords

Animals; Antibodies, Monoclonal/immunology; Antibodies, Viral/immunology; Cell Line; Cricetinae; Endocytosis; Epitopes; Fluorescent Antibody Technique; Hydrogen-Ion Concentration; Macromolecular Substances; Membrane Fusion; Monensin/pharmacology; Protein Conformation; Semliki forest virus/immunology; Semliki forest virus/physiology; Semliki forest virus/ultrastructure; Trypsin/pharmacology; Viral Envelope Proteins/immunology; Viral Envelope Proteins/physiology; Viral Envelope Proteins/ultrastructure; Viral Fusion Proteins/physiology

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HPV16:VE2

NOT

GO:0075512: clathrin-mediated endocytosis of virus by host cell

ECO:0000315:

P

"E1 fusion protein uses first heterodimerization with p62 as a means to become incorporated into the viral envelope and then dissociation from the cleaved p62 (e2), and reorganization, possibly within itself as a way to become activated (Membrane Fusion Process, pg.9)." See Table 1 of Papaer

complete
CACAO 9564

SFV:POLS

part_of

GO:0044174: host cell endosome

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

SFV:POLS

GO:0044174: host cell endosome

ECO:0000314:

C

In figure 8b, the anti-El" antibody gave a punctal staining pattern which probably represented the endosomal structures

complete
CACAO 9648

See also

References

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