Study sheds light on how neutralizing antibodies prevent EBV from entering host cells


Researchers report that they have found a new clue to how EBV enters and infect the host cell. The finding would guide the development of therapies and vaccines for the common virus.

Researchers participating in the study include Karthik Sathiyamoorthy and Theodore Jardetzky from Stanford University School of Medicine, Jiansen Jiang and Z. Hong Zhou from the University of California, and Britta Möhl, Jia Chen, and Richard Longnecker from Northwestern University.

The study is built on previous research by Jardetzky and Longnecker which solved the structure of EBV proteins that modulate the fusion of the virus with host cell membranes.

EBV, short for Epstein–Barr virus, belongs to the herpesvirus family and is extremely ubiquitous in all human populations. In the vast majority of EBV-infected individuals, there are limited clinical symptoms associated with EBV infection. But in some cases, EBV infection triggers varied diseases, particularly cancer and autoimmune disorders.

EBV is an enveloped virus and the envelope protects the entire viral structure. Envelop proteins also help the virus to attach to the host cell surface. EBV produces a set of glycoproteins, gH, gL, and gB, which work in coordination to allow the virus to enter cells.

For this work, Jardetzky and collaborators investigated how two anti-EBV monoclonal antibodies interact with the EBV glycoproteins and prevent the virus from entering the cell. The two antibodies, termed CL40 and CL59, block the fusion of EBV with host cells. The researchers identified the binding sites on EBV glycoproteins for the antibodies.

In conclusion, the study, which is published online before print in PNAS, sheds light on how neutralizing antibodies recognize EBV glycoproteins and prevent the virus from getting into a cell.
 
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