In the Journals

New findings suggest Ebola virus morphs from one shape to another

The same molecule that assembles and releases new Ebola viruses also rearranges itself into different shapes, with each shape controlling a different step of the virus’s life cycle, according to new research published online.

Erica Ollmann Saphire, PhD, professor in the department of immunology and microbial science at Scripps Research Institute, La Jolla, Calif., and colleagues combined cellular microscopy and critical replication experiments with X-ray crystallography and protein biochemistry to arrive at the results.

Erica Ollmann Saphire, PhD 

Erica Ollmann Saphire

The findings revealed that the Ebola virus VP40 protein exists as a dimer, not as a monomer as previously thought. The data also show that it rearranges its structure to assemble filaments to build the virus shell to release countless new viruses from infected cells.

The researchers said the protein also rearranges itself into rings to bind RNA and control the internal components of the virus copied inside infected cells.

This “shape-shifting” or “transformer” behavior explains how the Ebola virus can control a multi-step viral life cycle using only a very limited number of genes, the researchers said.

“[The study] revises a central dogma of molecular biology — that a protein molecule has one shape that predestines one biological function,” Saphire said in a press release.

Ebola hemorrhagic fever is one of the most virulent diseases known to humankind. Very few pathogens prove more dangerous than Ebola virus once a person is infected, according to the researchers. There is no cure, and the case-fatality rate can be up to 90%, depending on which strain is involved.

Disclosure: The researchers report no relevant financial disclosures.

The same molecule that assembles and releases new Ebola viruses also rearranges itself into different shapes, with each shape controlling a different step of the virus’s life cycle, according to new research published online.

Erica Ollmann Saphire, PhD, professor in the department of immunology and microbial science at Scripps Research Institute, La Jolla, Calif., and colleagues combined cellular microscopy and critical replication experiments with X-ray crystallography and protein biochemistry to arrive at the results.

Erica Ollmann Saphire, PhD 

Erica Ollmann Saphire

The findings revealed that the Ebola virus VP40 protein exists as a dimer, not as a monomer as previously thought. The data also show that it rearranges its structure to assemble filaments to build the virus shell to release countless new viruses from infected cells.

The researchers said the protein also rearranges itself into rings to bind RNA and control the internal components of the virus copied inside infected cells.

This “shape-shifting” or “transformer” behavior explains how the Ebola virus can control a multi-step viral life cycle using only a very limited number of genes, the researchers said.

“[The study] revises a central dogma of molecular biology — that a protein molecule has one shape that predestines one biological function,” Saphire said in a press release.

Ebola hemorrhagic fever is one of the most virulent diseases known to humankind. Very few pathogens prove more dangerous than Ebola virus once a person is infected, according to the researchers. There is no cure, and the case-fatality rate can be up to 90%, depending on which strain is involved.

Disclosure: The researchers report no relevant financial disclosures.