The transmembrane nucleoporin Pom121 ensures efficient HIV-1 pre-integration complex nuclear import

Virology. 2018 Aug:521:169-174. doi: 10.1016/j.virol.2018.06.008. Epub 2018 Jun 25.

Abstract

HIV-1 hijacks host classical cargo nuclear transportation, or nonclassical pathways by directly interacting with importin-β family proteins or nucleoporins for efficient pre-integration complex (PIC) nuclear import. Recently, an N-terminal truncated form of nucleoporin Pom121c (601-987 aa) was reported to inhibit HIV-1 replication. In contrast, we found that HIV-1 replication was significantly decreased in 293T and TZM-b1 cells with siRNA-mediated Pom121 knockdown. Quantitative PCR indicated that viral replication was impaired at the step of cDNA nuclear import. Furthermore, we found that karyopherin-β1 (KPNB1), which belongs to the importin-β family, interacts with Pom121 and is involved in Pom121-mediated PIC nuclear import. Rescue experiment indicated that the FG-repeats and the following α-helix in Pom121 are required for its role in HIV-1 PIC nuclear import. Taken together, our results showed that full-length Pom121 enables efficient PIC nuclear import, and suggested that this process may rely on KPNB1 dependent classical cargo nuclear transportation way.

Keywords: HIV-1; Nuclear import; Nucleoporins; Pom121; Pre-integration complex.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Active Transport, Cell Nucleus*
  • Cell Line
  • HIV-1 / physiology*
  • Host-Pathogen Interactions*
  • Humans
  • Membrane Glycoproteins / metabolism*
  • Protein Interaction Maps
  • Real-Time Polymerase Chain Reaction
  • Virus Replication*
  • beta Karyopherins / metabolism*

Substances

  • KPNB1 protein, human
  • Membrane Glycoproteins
  • POM121 protein, human
  • beta Karyopherins