The cunning virus structural layer EbolaBiologi: Protein that hides the viral RNA to avoid immune system detection of a deadly virus
Carmen Drahl
Ebola, RNA, VP35
X-ray structure of the two copies of the Ebola virus in Zaire protein (green, blue) to strengthen the viral RNA (pink).
A new molecular view of how the veil lifted Ebola virus not recognized by the immune system: a mechanism is used to disguise signs pemantelan penginvasiannya gossipy (Structural Nat. Mol. Biol., Doi: 10.1038/nsmb 1765). These findings may lead to the cure of Ebola hemorrhagic fever, a dangerous and often fatal disease that is accompanied by a viral infection.
Ebola is an agent of transmission of a beating where there is no cure, clear style K. Amarasinghe, a biochemist at Iowa State University The virus has left the identity card in some cells during infection: a double-stranded RNA - yours. Generally, these RNAs can activate the human immune system. However, this virus produces a protein called VP35 which makes RNA, then compared the immune response.
To learn more about how the camouflage, Amarasinghe, a virologist Christopher F. Basler of Mount Sinai School of Medicine, and colleagues to determine the X-ray crystal structure of double-stranded RNA binds to the VP35 Ebola virus in Zaire species are deadly. They found that a variety of coats assemble copies of VP35 RNA. A copy of hydrophobic amino acids using a cord bag mngenali double RNA strands of RNA and the back cover. Copies ynag column binding others through a point of basic amino acids. The changes in two basic residues is sufficient to destroy the disease causing ability of the virus in guinea pigs, the team found a new - this new (J. Virol., Doi: 10.1128/JVI.02459-09) .
In the past month, a team led by structural biologist Erica Ollman Saphire Scripps Research Institute detect VP35 RNA binding itself unusual in a few species of pathogenic Ebola (Proc. Natl. POLICY. Science. U.S. , doi: 10.1073/pnas 0.0910547107). This gives the satisfaction that strukturdari different species, obtained under different conditions showed the same unorthodox mechanism, Ollman Saphire said. "Of course, if you look at an unusual virus, you're bound to find something unusual," he said.
Besides studying how viruses work, the team hopes that the structural point of view is filled with a small molecule drug discovery efforts of the disease, which is the end - the end of this behind the development of vaccines, says Basler .
Carmen Drahl
Ebola, RNA, VP35
X-ray structure of the two copies of the Ebola virus in Zaire protein (green, blue) to strengthen the viral RNA (pink).
A new molecular view of how the veil lifted Ebola virus not recognized by the immune system: a mechanism is used to disguise signs pemantelan penginvasiannya gossipy (Structural Nat. Mol. Biol., Doi: 10.1038/nsmb 1765). These findings may lead to the cure of Ebola hemorrhagic fever, a dangerous and often fatal disease that is accompanied by a viral infection.
Ebola is an agent of transmission of a beating where there is no cure, clear style K. Amarasinghe, a biochemist at Iowa State University The virus has left the identity card in some cells during infection: a double-stranded RNA - yours. Generally, these RNAs can activate the human immune system. However, this virus produces a protein called VP35 which makes RNA, then compared the immune response.
To learn more about how the camouflage, Amarasinghe, a virologist Christopher F. Basler of Mount Sinai School of Medicine, and colleagues to determine the X-ray crystal structure of double-stranded RNA binds to the VP35 Ebola virus in Zaire species are deadly. They found that a variety of coats assemble copies of VP35 RNA. A copy of hydrophobic amino acids using a cord bag mngenali double RNA strands of RNA and the back cover. Copies ynag column binding others through a point of basic amino acids. The changes in two basic residues is sufficient to destroy the disease causing ability of the virus in guinea pigs, the team found a new - this new (J. Virol., Doi: 10.1128/JVI.02459-09) .
In the past month, a team led by structural biologist Erica Ollman Saphire Scripps Research Institute detect VP35 RNA binding itself unusual in a few species of pathogenic Ebola (Proc. Natl. POLICY. Science. U.S. , doi: 10.1073/pnas 0.0910547107). This gives the satisfaction that strukturdari different species, obtained under different conditions showed the same unorthodox mechanism, Ollman Saphire said. "Of course, if you look at an unusual virus, you're bound to find something unusual," he said.
Besides studying how viruses work, the team hopes that the structural point of view is filled with a small molecule drug discovery efforts of the disease, which is the end - the end of this behind the development of vaccines, says Basler .
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