-
Something wrong with this record ?
Membrane Interactions of the Mason-Pfizer Monkey Virus Matrix Protein and Its Budding Deficient Mutants
T. Kroupa, H. Langerová, M. Doležal, J. Prchal, V. Spiwok, E. Hunter, M. Rumlová, R. Hrabal, T. Ruml,
Language English Country England, Great Britain
Document type Journal Article
Links
PubMed
27725181
DOI
10.1016/j.jmb.2016.10.010
Knihovny.cz E-resources
- MeSH
- Cell Membrane metabolism MeSH
- Phospholipids metabolism MeSH
- Liposomes metabolism MeSH
- Magnetic Resonance Spectroscopy MeSH
- Mason-Pfizer monkey virus physiology MeSH
- Fatty Acids metabolism MeSH
- Mutation, Missense MeSH
- Mutant Proteins chemistry metabolism MeSH
- Viral Matrix Proteins chemistry metabolism MeSH
- Virus Release * MeSH
- Protein Binding MeSH
- Publication type
- Journal Article MeSH
Matrix proteins (MAs) play a key role in the transport of retroviral proteins inside infected cells and in the interaction with cellular membranes. In most retroviruses, retroviral MAs are N-terminally myristoylated. This modification serves as a membrane targeting signal and also as an anchor for membrane interaction. The aim of this work was to characterize the interactions anchoring retroviral MA at the plasma membrane of infected cell. To address this issue, we compared the structures and membrane affinity of the Mason-Pfizer monkey virus (M-PMV) wild-type MA with its two budding deficient double mutants, that is, T41I/T78I and Y28F/Y67F. The structures of the mutants were determined using solution NMR spectroscopy, and their interactions with water-soluble phospholipids were studied. Water-soluble phospholipids are widely used models for studying membrane interactions by solution NMR spectroscopy. However, this approach might lead to artificial results due to unnatural hydrophobic interactions. Therefore, we used a new approach based on the measurement of the loss of the (1)H NMR signal intensity of the protein sample induced by the addition of the liposomes containing phospholipids with naturally long fatty acids. HIV-1 MA was used as a positive control because its ability to interact with liposomes has already been described. We found that in contrast to HIV-1, the M-PMV MA interacted with the liposomes differently and much weaker. In our invivo experiments, the M-PMV MA did not co-localize with lipid rafts. Therefore, we concluded that M-PMV might adopt a different membrane binding mechanism than HIV-1.
- 000
- 00000naa a2200000 a 4500
- 001
- bmc17023603
- 003
- CZ-PrNML
- 005
- 20240522141356.0
- 007
- ta
- 008
- 170720s2016 enk f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.1016/j.jmb.2016.10.010 $2 doi
- 035 __
- $a (PubMed)27725181
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a enk
- 100 1_
- $a Kroupa, Tomáš $u Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Technická 5, 166 28 Prague 6, Czech Republic; Laboratory of NMR Spectroscopy, University of Chemistry and Technology, Prague, Technická 5, 166 28 Prague 6, Czech Republic. Electronic address: kroupat@vscht.cz.
- 245 10
- $a Membrane Interactions of the Mason-Pfizer Monkey Virus Matrix Protein and Its Budding Deficient Mutants / $c T. Kroupa, H. Langerová, M. Doležal, J. Prchal, V. Spiwok, E. Hunter, M. Rumlová, R. Hrabal, T. Ruml,
- 520 9_
- $a Matrix proteins (MAs) play a key role in the transport of retroviral proteins inside infected cells and in the interaction with cellular membranes. In most retroviruses, retroviral MAs are N-terminally myristoylated. This modification serves as a membrane targeting signal and also as an anchor for membrane interaction. The aim of this work was to characterize the interactions anchoring retroviral MA at the plasma membrane of infected cell. To address this issue, we compared the structures and membrane affinity of the Mason-Pfizer monkey virus (M-PMV) wild-type MA with its two budding deficient double mutants, that is, T41I/T78I and Y28F/Y67F. The structures of the mutants were determined using solution NMR spectroscopy, and their interactions with water-soluble phospholipids were studied. Water-soluble phospholipids are widely used models for studying membrane interactions by solution NMR spectroscopy. However, this approach might lead to artificial results due to unnatural hydrophobic interactions. Therefore, we used a new approach based on the measurement of the loss of the (1)H NMR signal intensity of the protein sample induced by the addition of the liposomes containing phospholipids with naturally long fatty acids. HIV-1 MA was used as a positive control because its ability to interact with liposomes has already been described. We found that in contrast to HIV-1, the M-PMV MA interacted with the liposomes differently and much weaker. In our invivo experiments, the M-PMV MA did not co-localize with lipid rafts. Therefore, we concluded that M-PMV might adopt a different membrane binding mechanism than HIV-1.
- 650 _2
- $a buněčná membrána $x metabolismus $7 D002462
- 650 _2
- $a mastné kyseliny $x metabolismus $7 D005227
- 650 _2
- $a liposomy $x metabolismus $7 D008081
- 650 _2
- $a magnetická rezonanční spektroskopie $7 D009682
- 650 _2
- $a Masonův-Pfizerův opičí virus $x fyziologie $7 D016093
- 650 _2
- $a mutantní proteiny $x chemie $x metabolismus $7 D050505
- 650 _2
- $a missense mutace $7 D020125
- 650 _2
- $a fosfolipidy $x metabolismus $7 D010743
- 650 _2
- $a vazba proteinů $7 D011485
- 650 _2
- $a proteiny virové matrix $x chemie $x metabolismus $7 D014763
- 650 12
- $a uvolnění viru z buňky $7 D057074
- 655 _2
- $a časopisecké články $7 D016428
- 700 1_
- $a Langerová, Hana $u Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Technická 5, 166 28 Prague 6, Czech Republic. Electronic address: langeroh@vscht.cz.
- 700 1_
- $a Doležal, Michal $u Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Technická 5, 166 28 Prague 6, Czech Republic; Laboratory of NMR Spectroscopy, University of Chemistry and Technology, Prague, Technická 5, 166 28 Prague 6, Czech Republic. Electronic address: dolezal@uochb.cas.cz. $7 xx0317427
- 700 1_
- $a Prchal, Jan $u Laboratory of NMR Spectroscopy, University of Chemistry and Technology, Prague, Technická 5, 166 28 Prague 6, Czech Republic. Electronic address: prchalj@vscht.cz.
- 700 1_
- $a Spiwok, Vojtěch $u Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Technická 5, 166 28 Prague 6, Czech Republic. Electronic address: spiwokv@vscht.cz.
- 700 1_
- $a Hunter, Eric $u Emory Vaccine Center, Yerkes National Primate Research Center, 954 Gatewood Road, Atlanta, GA 30329, USA. Electronic address: ehunte4@emory.edu.
- 700 1_
- $a Rumlová, Michaela $u Department of Biotechnology, University of Chemistry and Technology, Prague, Technická 5, 166 28 Prague 6, Czech Republic. Electronic address: rumlovai@vscht.cz.
- 700 1_
- $a Hrabal, Richard $u Laboratory of NMR Spectroscopy, University of Chemistry and Technology, Prague, Technická 5, 166 28 Prague 6, Czech Republic. Electronic address: hrabalr@vscht.cz.
- 700 1_
- $a Ruml, Tomáš $u Department of Biochemistry and Microbiology, University of Chemistry and Technology, Prague, Technická 5, 166 28 Prague 6, Czech Republic. Electronic address: rumlt@vscht.cz.
- 773 0_
- $w MED00002808 $t Journal of molecular biology $x 1089-8638 $g Roč. 428, č. 23 (2016), s. 4708-4722
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/27725181 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y a $z 0
- 990 __
- $a 20170720 $b ABA008
- 991 __
- $a 20240522141352 $b ABA008
- 999 __
- $a ok $b bmc $g 1239284 $s 984516
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2016 $b 428 $c 23 $d 4708-4722 $e 20161008 $i 1089-8638 $m Journal of Molecular Biology $n J Mol Biol $x MED00002808
- LZP __
- $a Pubmed-20170720