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TitleMultivalent interactions essential for lentiviral integrase function.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 2416, Year 2022
Publish dateMay 3, 2022
AuthorsAllison Ballandras-Colas / Vidya Chivukula / Dominika T Gruszka / Zelin Shan / Parmit K Singh / Valerie E Pye / Rebecca K McLean / Gregory J Bedwell / Wen Li / Andrea Nans / Nicola J Cook / Hind J Fadel / Eric M Poeschla / David J Griffiths / Javier Vargas / Ian A Taylor / Dmitry Lyumkis / Hasan Yardimci / Alan N Engelman / Peter Cherepanov /
PubMed AbstractA multimer of retroviral integrase (IN) synapses viral DNA ends within a stable intasome nucleoprotein complex for integration into a host cell genome. Reconstitution of the intasome from the maedi- ...A multimer of retroviral integrase (IN) synapses viral DNA ends within a stable intasome nucleoprotein complex for integration into a host cell genome. Reconstitution of the intasome from the maedi-visna virus (MVV), an ovine lentivirus, revealed a large assembly containing sixteen IN subunits. Herein, we report cryo-EM structures of the lentiviral intasome prior to engagement of target DNA and following strand transfer, refined at 3.4 and 3.5 Å resolution, respectively. The structures elucidate details of the protein-protein and protein-DNA interfaces involved in lentiviral intasome formation. We show that the homomeric interfaces involved in IN hexadecamer formation and the α-helical configuration of the linker connecting the C-terminal and catalytic core domains are critical for MVV IN strand transfer activity in vitro and for virus infectivity. Single-molecule microscopy in conjunction with photobleaching reveals that the MVV intasome can bind a variable number, up to sixteen molecules, of the lentivirus-specific host factor LEDGF/p75. Concordantly, ablation of endogenous LEDGF/p75 results in gross redistribution of MVV integration sites in human and ovine cells. Our data confirm the importance of the expanded architecture observed in cryo-EM studies of lentiviral intasomes and suggest that this organization underlies multivalent interactions with chromatin for integration targeting to active genes.
External linksNat Commun / PubMed:35504909 / PubMed Central
MethodsEM (single particle)
Resolution3.46 Å
Structure data

26322

7u32

EMDB-26322, PDB-7u32:
MVV cleaved synaptic complex (CSC) intasome at 3.4 A resolution
Method: EM (single particle) / Resolution: 3.46 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-CA:
Unknown entry

Source
  • Streptomyces griseus (bacteria)
  • visna/maedi virus ev1 kv1772
  • synthetic construct (others)
KeywordsVIRAL PROTEIN/DNA / Integrase-DNA complex / hydrolase / VIRAL PROTEIN / VIRAL PROTEIN-DNA complex

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