|
Mutation Information
|
Mutation Site
|
R85A |
|
Mutation Type
|
Amino acid level |
|
Gene/Protein/Region Type
|
Vpr |
|
Genotype/Subtype
|
G |
Literature Information
|
PubMed PMID
|
32753492
|
|
Published Year
|
2020 |
|
Journal
|
mBio |
|
Title
|
HIV Vpr Modulates the Host DNA Damage Response at Two Independent Steps to Damage DNA and Repress Double-Strand DNA Break Repair. |
|
Author
|
Li D,Lopez A,Sandoval C,Nichols Doyle R,Fregoso OI |
|
Evidence
|
These include HIV-1 W54R/HIV-2 L59A Vpr mutants, which block the ability of HIV-1 Vpr to recruit and degrade the DNA glycosylase UNG2;HIV-1 Q65R/HIV-2 Q70R Vpr, which renders Vpr unable to properly localize, multimerize, or recruit known host proteins, such as the Cul4ADCAF1 complex or UNG2 and, therefore, is largely functionally dead;HIV-1 S79A/HIV-2 S84A mutants, which render Vpr unable to cause cell cycle arrest or interact with TAK1 to activate canonical NF-kappaB;and HIV-1 R80A/HIV-2 R85A Vpr mutants, which can still interact with Cul4ADCAF1 and degrade TET2 but do not cause cell cycle arrest, presumably due to the requirement of an additional unknown host protein(s).
|
|
|
HIV Mutation Detail Information