Investigate The Critical Amino Acid Residues on ZIKA Envelope Protein for GRP78 Protein Interaction

Abstract

Zika virus is a mosquito-borne Flavivirus and is additionally transmitted by sexual contact, across the placenta and by blood transfusion. The spread of the Zika virus is also of concern in Indonesia, considering that Indonesia is a tropical country and an endemic area for dengue fever every year. There is currently no vaccine available to protect against or drug to treat Zika virus infection. The envelope (E) protein, which comprises the ZIKV virion surface, must attach to a receptor for the virus to enter into a cell. GRP78 is a host cell protein that is essential for the correct folding of new proteins, but it also plays an important role in the body's response to endoplasmic reticulum (ER) stress. The crucial residues for substrate binding to the binding domain of GRP78 protein were located at positions C308A, T309A, and A311S on ZIKV E domain III. The amount of viral infection and replication in host cells was significantly reduced as a result of knockdown by siRNA gene silencing. The residues could be crucial for interacting with other host proteins as well. Understanding the function and regulation of the Zika virus in host cells will be improved by the identification of important amino acid residues on the Zika envelope protein. It will establish the essential information and might aid in the creation of treatment strategies which include vaccine development.