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9EK1

HIV-1 mature WT matrix protein p17 lattice

Summary for 9EK1
Entry DOI10.2210/pdb9ek1/pdb
EMDB information47842
DescriptorMatrix protein p17, MYRISTIC ACID (2 entities in total)
Functional Keywordsmatrix, hiv-1, p17, hiv-1 p17, virus, structural protein, viral protein
Biological sourceHuman immunodeficiency virus type 1 (HIV-1)
Total number of polymer chains39
Total formula weight519220.81
Authors
Rey, J.S.,Perilla, J.R.,Chen, L.,Zhang, P. (deposition date: 2024-11-30, release date: 2025-01-08, Last modification date: 2025-05-21)
Primary citationChen, L.,Hikichi, Y.,Rey, J.S.,Akil, C.,Zhu, Y.,Veler, H.,Shen, Y.,Perilla, J.R.,Freed, E.O.,Zhang, P.
Structural maturation of the matrix lattice is not required for HIV-1 particle infectivity.
Sci Adv, 11:eadv4356-eadv4356, 2025
Cited by
PubMed Abstract: During HIV-1 maturation, the matrix (MA) lattice underlying the viral membrane undergoes a structural rearrangement, and the newly released capsid (CA) protein forms a mature CA. While it is well established that CA formation is essential for particle infectivity, the functional role of MA structural maturation remains unclear. Here, we examine maturation of an MA triple mutant, L20K/E73K/A82T, which, despite replicating similarly to wild-type (WT) in some cell lines, exhibits distinct biochemical behaviors that suggest altered MA-MA interactions. Cryo-electron tomography with subtomogram averaging reveals that, although the MA lattice in immature L20K/E73K/A82T virions closely resembles that of the WT, mature L20K/E73K/A82T virions lack a detectable MA lattice. All-atom molecular dynamics simulations suggest that this absence results from destabilized inter-trimer MA interactions in mature L20K/E73K/A82T mutant virions. These findings suggest that an ordered, membrane-associated mature MA lattice is not essential for HIV-1 infectivity, providing insights into the structural requirements for HIV-1 particle maturation and generation of infectious particles.
PubMed: 40344051
DOI: 10.1126/sciadv.adv4356
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (7.3 Å)
Structure validation

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