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

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. Copyright © 2018 Elsevier Inc. All rights reserved.

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Jing Guo, Xianxian Liu, Chuanjian Wu, Jingping Hu, Ke Peng, Li Wu, Sidong Xiong, Chunsheng Dong. The transmembrane nucleoporin Pom121 ensures efficient HIV-1 pre-integration complex nuclear import. Virology. 2018 Aug;521:169-174

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PMID: 29957337

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