6es8 | pdb_00006es8
HIV capsid hexamer with IP6 ligand
Structural highlights
Publication Abstract from PubMedThe HIV capsid is semipermeable and covered in electropositive pores that are essential for viral DNA synthesis and infection. Here, we show that these pores bind the abundant cellular polyanion IP6, transforming viral stability from minutes to hours and allowing newly synthesised DNA to accumulate inside the capsid. An arginine ring within the pore coordinates IP6, which strengthens capsid hexamers by almost 10 degrees C. Single molecule measurements demonstrate that this renders native HIV capsids highly stable and protected from spontaneous collapse. Moreover, encapsidated reverse transcription assays reveal that, once stabilised by IP6, the accumulation of new viral DNA inside the capsid increases >100 fold. Remarkably, isotopic labelling of inositol in virus-producing cells reveals that HIV selectively packages over 300 IP6 molecules per infectious virion. We propose that HIV recruits IP6 to regulate capsid stability and uncoating, analogous to picornavirus pocket factors. HIV-1/IP6/capsid/co-factor/reverse transcription. IP6 is an HIV pocket factor that prevents capsid collapse and promotes DNA synthesis.,Mallery DL, Marquez CL, McEwan WA, Dickson CF, Jacques DA, Anandapadamanaban M, Bichel K, Towers GJ, Saiardi A, Bocking T, James LC Elife. 2018 May 31;7. pii: 35335. doi: 10.7554/eLife.35335. PMID:29848441[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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