Maturation of the matrix and viral membrane of HIV-1

Kun Qu, Zunlong Ke, Vojtech Zila, Maria Anders-Össwein, Bärbel Glass, Frauke Mücksch, Rainer Müller, Carsten Schultz, Barbara Müller, Hans Georg Kräusslich, John A.G. Briggs

Research output: Contribution to journalArticlepeer-review

41 Scopus citations


Gag, the primary structural protein of HIV-1, is recruited to the plasma membrane for virus assembly by its matrix (MA) domain. Gag is subsequently cleaved into its component domains, causing structural maturation to repurpose the virion for cell entry. We determined the structure and arrangement of MA within immature and mature HIV-1 through cryo-electron tomography. We found that MA rearranges between two different hexameric lattices upon maturation. In mature HIV-1, a lipid extends out of the membrane to bind with a pocket in MA. Our data suggest that proteolytic maturation of HIV-1 not only assembles the viral capsid surrounding the genome but also repurposes the membrane-bound MA lattice for an entry or postentry function and results in the partial removal of up to 2500 lipids from the viral membrane.

Original languageEnglish (US)
Pages (from-to)700-704
Number of pages5
Issue number6555
StatePublished - Aug 6 2021
Externally publishedYes

ASJC Scopus subject areas

  • General


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