Mamuka Kvaratskhelia

The paper shows that HIV-1 integrase C-terminal domain mutations affect sensitivity to ALLINIs by altering gRNA binding, despite being distant from the drug binding site.

This study identifies the minimal MX2 region required for HIV-1 restriction and shows that MX2 binding disrupts the capsid lattice, leading to premature fragmentation and preventing viral nuclear import.

This study determines cryo-EM structures of HIV-1 integrase tetramers and intasome hexadecamers, revealing structural plasticity and functional roles in viral integration and RNA binding.

This paper investigates how the M66I mutation in HIV-1 capsid protein confers resistance to lenacapavir by altering inhibitor binding and viral replication.

This study identifies the mechanism by which lenacapavir inhibits HIV-1 maturation by altering capsid protein assembly.

This study shows that the RANBP2-Cyp domain influences HIV-1 infection and MX2 activity by modulating CA interactions with nucleoporins and integration targeting.

The paper shows that disrupting HIV-1 integrase interactions with LEDGF/p75 increases antisense RNA (asRNA) production in HIV-1 infected cells.

This paper identifies the mechanism of resistance to the HIV-1 integrase inhibitor pirmitegravir and develops a more potent analog to overcome this resistance.

This study shows that MX2 antiviral activity depends on CypA-CA interactions and GTPase function, with loss of GTPase activity altering Nup requirements for viral restriction.