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TitleRetroviruses use different IP binding mechanisms to alter the properties of their capsids.
Journal, issue, pagesNat Commun, Vol. 17, Issue 1, Year 2026
Publish dateAug 21, 2026
AuthorsJ Ole Klarhof / Donna L Mallery / James C V Stacey / Davide Torre / Michaela Rumlova / Tomas Ruml / John A G Briggs / Leo C James /
PubMed AbstractHIV-1 uses the metabolite inositol hexakisphosphate (IP) as a host factor to assemble its capsid, but whether this strategy is unique to lentiviruses or represents a common feature of retroviral ...HIV-1 uses the metabolite inositol hexakisphosphate (IP) as a host factor to assemble its capsid, but whether this strategy is unique to lentiviruses or represents a common feature of retroviral capsids remains unclear. Here we show that IP binding is conserved across diverse retroviruses but occurs through distinct capsid sites and mechanisms, and influences viral behaviour. In contrast to HIV-1, the beta-retrovirus Mason-Pfizer Monkey Virus (MPMV) and the gamma-retrovirus Murine Leukaemia Virus (MLV) bind IP at the threefold lattice interface between capsomers rather than within capsomer pores. Cryo-EM structures of core-like particles reveal that two lysine residues from each capsomer coordinate IP between either two discrete three-lysine rings (MPMV) or a single heterogeneous six-lysine ring (MLV). MPMV and MLV are largely insensitive to IP availability in producer cells, but this binding mode renders them highly dependent on IP6 in target cells - the opposite of the dependency pattern of HIV-1. The way in which retroviruses use IP to build their capsids alters their dependence on the metabolite at different stages of the replicative cycle and in key capsid behaviours, such as assembly and stability.
External linksNat Commun / PubMed:42764334 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 4.6 Å
Structure data

56387

9tx4

EMDB-56387, PDB-9tx4:
Mature MoMLV capsid hexamer 3-fold interface from capsid-like particles
Method: EM (single particle) / Resolution: 4.2 Å

56388

9tx5

EMDB-56388, PDB-9tx5:
Mature MoMLV capsid hexamer structure from capsid-like particles
Method: EM (single particle) / Resolution: 3.5 Å

56389

9tx6

EMDB-56389, PDB-9tx6:
Mature MoMLV capsid pentamer structure from capsid-like particles
Method: EM (single particle) / Resolution: 3.9 Å

56390

9tx7

EMDB-56390, PDB-9tx7:
Mature MPMV capsid hexamer 3-fold interface from capsid-like particles
Method: EM (single particle) / Resolution: 4.1 Å

56391

9tx8

EMDB-56391, PDB-9tx8:
Mature MPMV E26A capsid pentamer structure from capsid-like particles
Method: EM (single particle) / Resolution: 4.6 Å

56392

9tx9

EMDB-56392, PDB-9tx9:
Mature MPMV E26A capsid hexamer structure from capsid-like particles
Method: EM (single particle) / Resolution: 3.8 Å

56393

9txa

EMDB-56393, PDB-9txa:
Mature MPMV capsid pentamer structure from capsid-like particles
Method: EM (single particle) / Resolution: 3.3 Å

56394

9txb

EMDB-56394, PDB-9txb:
Mature MPMV capsid hexamer structure from capsid-like particles
Method: EM (single particle) / Resolution: 3.2 Å

Source
  • Escherichia coli (E. coli)
  • moloney murine leukemia virus
  • mason-pfizer monkey virus
KeywordsVIRAL PROTEIN / MLV / capsid / mature / CA / IP6 / retrovirus / hexamer / 3-fold axis / C3 / capsomer / MoMLV / pentamer / MPMV / M-PMV / p27

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