E. O. Freed

Structural Basis of HIV-1 Maturation Inhibitor Binding and Activity

This study determines the structural basis of HIV-1 maturation inhibitor binding and resistance using NMR, revealing an allosteric mechanism and conformational changes in SP1 variants.

Rab11-FIP1C is dispensable for HIV-1 replication in primary CD4+ T cells but its role is cell-type-dependent in immortalized human T-cell lines

This study shows FIP1C is not essential for HIV-1 replication in primary CD4+ T cells but has cell-type-dependent effects in T-cell lines.

Mechanism of Viral Glycoprotein Targeting by Membrane-associated-RING-CH Proteins

This paper investigates how MARCH8 targets viral glycoproteins to impair their function, showing CT-dependent and -independent mechanisms for different viruses.

Elucidating the basis for permissivity of the MT-4 T-cell line to replication of an HIV-1 mutant lacking the gp41 cytoplasmic tail

This study investigates why MT-4 T-cells allow HIV-1 replication despite lacking the gp41 cytoplasmic tail, finding faster viral production, higher surface Env, and increased cell-to-cell transmission contribute to this permissivity.

CryoET structures of immature HIV Gag reveal a complete six-helix bundle and stabilizing small molecules distinct from IP6

The paper determines the structure of the HIV Gag six-helix bundle using cryoET and identifies small molecules stabilizing the immature lattice.

Mechanistic Analysis of the Broad Antiretroviral Resistance Conferred by HIV-1 Envelope Glycoprotein Mutations

This study shows that HIV-1 envelope glycoprotein mutations can confer broad antiretroviral resistance through cell-cell transmission and structural changes, independent of target-gene mutations.

PSGL-1 inhibits the virion incorporation of SARS-CoV and SARS-CoV-2 spike glycoproteins and impairs virus attachment and infectivity

The paper shows PSGL-1 inhibits SARS-CoV and SARS-CoV-2 spike glycoprotein incorporation into pseudovirions, blocking virus attachment and infectivity.

The Vpu-interacting protein ATP6V0C regulates expression of tetherin and HIV-1 release

This study identifies ATP6V0C as a Vpu-interacting protein that regulates tetherin expression and HIV-1 release by stabilizing tetherin and affecting its subcellular localization.