Journal
JOURNAL OF VIROLOGY
Volume 86, Issue 8, Pages 4708-4714Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.05887-11
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Funding
- Pittsburgh Center for HIV Protein Interactions
- National Cancer Institute's intramural Center for Cancer Research
- National Center for Research Resources (NCRR), a component of the National Institutes of Health (NIH) [1 UL1 RR024153]
- NIH Roadmap for Medical Research
- NIH [GM082251, AI078839, AI052014]
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The antiviral factor CPSF6-358 interferes with the nuclear entry of human immunodeficiency virus type 1 (HIV-1). HIV-1 acquires resistance to CPSF6-358 through the N74D mutation of the capsid (CA), which alters its nuclear entry pathway. Here we show that compared to wild-type (WT) HIV-1, N74D HIV-1 is more sensitive to cyclosporine, has increased sensitivity to nevirapine, and is impaired in macrophage infection prior to reverse transcription. These phenotypes suggest a difference in the N74D reverse transcription complex that manifests early after infection and prior to interaction with the nuclear pore. Overall, our data indicate that N74D HIV-1 replication in transformed cells requires cyclophilin A but is dependent on other interactions in macrophages.
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