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TIM-1 acts a dual-attachment receptor for Ebolavirus by interacting directly with viral GP and the PS on the viral envelope
Protein & Cell ; (12): 814-824, 2015.
Article in English | WPRIM | ID: wpr-757174
ABSTRACT
Ebolavirus can cause hemorrhagic fever in humans with a mortality rate of 50%-90%. Currently, no approved vaccines and antiviral therapies are available. Human TIM1 is considered as an attachment factor for EBOV, enhancing viral infection through interaction with PS located on the viral envelope. However, reasons underlying the preferable usage of hTIM-1, but not other PS binding receptors by filovirus, remain unknown. We firstly demonstrated a direct interaction between hTIM-1 and EBOV GP in vitro and determined the crystal structures of the Ig V domains of hTIM-1 and hTIM-4. The binding region in hTIM-1 to EBOV GP was mapped by chimeras and mutation assays, which were designed based on structural analysis. Pseudovirion infection assays performed using hTIM-1 and its homologs as well as point mutants verified the location of the GP binding site and the importance of EBOV GP-hTIM-1 interaction in EBOV cellular entry.
Subject(s)
Full text: Available Index: WPRIM (Western Pacific) Main subject: Protein Binding / Receptors, Virus / Viral Proteins / Membrane Glycoproteins / Glycoproteins / Viral Envelope Proteins / Surface Plasmon Resonance / Ebolavirus / Flow Cytometry / Hepatitis A Virus Cellular Receptor 1 Limits: Humans Language: English Journal: Protein & Cell Year: 2015 Type: Article

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Full text: Available Index: WPRIM (Western Pacific) Main subject: Protein Binding / Receptors, Virus / Viral Proteins / Membrane Glycoproteins / Glycoproteins / Viral Envelope Proteins / Surface Plasmon Resonance / Ebolavirus / Flow Cytometry / Hepatitis A Virus Cellular Receptor 1 Limits: Humans Language: English Journal: Protein & Cell Year: 2015 Type: Article