Herpes viruses enter the body and hide away in cells, often re-emerging later to cause illnesses such as shingles, genital herpes and cancer. How these viruses evade the immune system remains poorly understood, but researchers at Washington University School of Medicine in St. Louis discovered that a mouse herpes virus uses molecules that mimic a cells own proteins to help thwart an immune attack.
The findings also suggest that a branch of the immune system known as the complement system may play a more important role in controlling herpes virus infections than previously thought. The study is published in the August issue of the journal Immunity.
"These findings reveal another molecular mechanism by which viruses evade the immune system," says study leader Herbert W. Virgin, M.D., Ph.D., professor of pathology and immunology and of molecular microbiology. "By targeting this viral protein or by manipulating the complement system, perhaps someday we can develop better treatments for herpes virus infections."
Darrell E. Ward | EurekAlert!
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
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