Tuning the binding interface between Machupo virus glycoprotein and human transferrin receptor.

ABSTRACT: Machupo virus, known to cause hemorrhagic fevers, enters human cells via binding with its envelope glycoprotein to transferrin receptor 1 (TfR). Similarly, the receptor interactions have been explored in biotechnological applications as a molecular system to ferry therapeutics across the cellular membranes and through the impenetrable blood-brain barrier that effectively blocks any such delivery into the brain. Study of the experimental structure of Machupo virus glycoprotein 1 (MGP1) in complex with TfR and glycoprotein sequence homology has identified some residues at the interface that influence binding. There are, however, no studies that have attempted to optimize the binding potential between MGP1 and TfR. In pursuits for finding therapeutic solutions for the New World arenaviruses,

SUBMITTER: Sjostrom DJ 

PROVIDER: S-EPMC7894301 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature