Crystal Structure of the Low-pH Form of the Vesicular Stomatitis Virus Glycoprotein G.

The article discusses the crystal structure of the Vesicular Stomatitis Virus Glycoprotein G. It is found that the virus has an atypical membrane fusion G showing a hydrogen ion concentration-dependent equilibrium between two forms at the virus surface. Membrane fusion is triggered during the transition from the high-pH to low-pH form. The structure of G in its low-pH form shows the classic hairpin conformation observed in all other fusion proteins in their postfusion conformation. G with gB of herpesviruses, describes a new family of fusion proteins exhibiting a new fusion module, an elongated β structure inserted in a pH domain and carrying two fusion loops. The structural organization of G is observed to be same as that of herpesvirus. The structural transition of G is significantly affected by mutations.