Differences and commonalities in plasma membrane recruitment of the two morphogenetically distinct retroviruses HIV-1 and MMTV.

Gag polyprotein HIV-1 coarse-grained molecular dynamics covalent labeling–mass spectrometry human immunodeficiency virus (HIV) lipid–protein interaction mass spectrometry (MS) matrix protein membrane binding molecular dynamics mouse mammary tumor virus (MMTV) particle assembly retrovirus viral replication

Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
26 06 2020
Historique:
received: 21 11 2019
revised: 05 05 2020
pubmed: 10 5 2020
medline: 14 1 2021
entrez: 10 5 2020
Statut: ppublish

Résumé

Retroviral Gag polyproteins are targeted to the inner leaflet of the plasma membrane through their N-terminal matrix (MA) domain. Because retroviruses of different morphogenetic types assemble their immature particles in distinct regions of the host cell, the mechanism of MA-mediated plasma membrane targeting differs among distinct retroviral morphogenetic types. Here, we focused on possible mechanistic differences of the MA-mediated plasma membrane targeting of the B-type mouse mammary tumor virus (MMTV) and C-type HIV-1, which assemble in the cytoplasm and at the plasma membrane, respectively. Molecular dynamics simulations, together with surface mapping, indicated that, similarly to HIV-1, MMTV uses a myristic switch to anchor the MA to the membrane and electrostatically interacts with phosphatidylinositol 4,5-bisphosphate to stabilize MA orientation. We observed that the affinity of MMTV MA to the membrane is lower than that of HIV-1 MA, possibly related to their different topologies and the number of basic residues in the highly basic MA region. The latter probably reflects the requirement of C-type retroviruses for tighter membrane binding, essential for assembly, unlike for D/B-type retroviruses, which assemble in the cytoplasm. A comparison of the membrane topology of the HIV-1 MA, using the surface-mapping method and molecular dynamics simulations, revealed that the residues at the HIV-1 MA C terminus help stabilize protein-protein interactions within the HIV-1 MA lattice at the plasma membrane. In summary, HIV-1 and MMTV share common features such as membrane binding of the MA via hydrophobic interactions and exhibit several differences, including lower membrane affinity of MMTV MA.

Identifiants

pubmed: 32385109
pii: S0021-9258(17)49376-8
doi: 10.1074/jbc.RA119.011991
pmc: PMC7324529
pii:
doi:

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

8819-8833

Commentaires et corrections

Type : ErratumIn

Informations de copyright

© 2020 Junková et al.

Déclaration de conflit d'intérêts

Conflict of interest—The authors declare that they have no conflicts of interest with the contents of this article.

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Auteurs

Petra Junková (P)

Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic; Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Prague, Czech Republic.

Roman Pleskot (R)

Department of Plant Biotechnology and Bioinformatics, Ghent University, Ghent, Belgium; VIB Center for Plant Systems Biology, Ghent, Belgium.

Jan Prchal (J)

Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic.

Jakub Sýs (J)

Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic.

Tomáš Ruml (T)

Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Czech Republic. Electronic address: tomas.ruml@vscht.cz.

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