Abstract
Marburg virus (MARV), which belongs to the virus family Filoviridae, causes hemorrhagic fever in humans and nonhuman primates that is often fatal. MARV is a lipid-enveloped virus that during the replication process extracts its lipid coat from the plasma membrane of the host cell it infects. MARV carries seven genes, one of which encodes its matrix protein VP40 (mVP40), which regulates the assembly and budding of the virions. Currently, little information is available on mVP40 lipid binding properties. Here, we have investigated the in vitro and cellular mechanisms by which mVP40 associates with lipid membranes. mVP40 associates with anionic membranes in a nonspecific manner that is dependent upon the anionic charge density of the membrane. These results are consistent with recent structural determination of mVP40, which elucidated an mVP40 dimer with a flat and extensive cationic lipid binding interface.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 3074-3085 |
| Number of pages | 12 |
| Journal | Journal of Virology |
| Volume | 90 |
| Issue number | 6 |
| DOIs | |
| State | Published - 2016 |
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ASJC Scopus subject areas
- Immunology
- Virology
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Investigation of the lipid binding properties of the Marburg virus matrix protein VP40. / Wijesinghe, Kaveesha J.; Stahelin, Robert.
In: Journal of Virology, Vol. 90, No. 6, 2016, p. 3074-3085.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Investigation of the lipid binding properties of the Marburg virus matrix protein VP40
AU - Wijesinghe, Kaveesha J.
AU - Stahelin, Robert
PY - 2016
Y1 - 2016
N2 - Marburg virus (MARV), which belongs to the virus family Filoviridae, causes hemorrhagic fever in humans and nonhuman primates that is often fatal. MARV is a lipid-enveloped virus that during the replication process extracts its lipid coat from the plasma membrane of the host cell it infects. MARV carries seven genes, one of which encodes its matrix protein VP40 (mVP40), which regulates the assembly and budding of the virions. Currently, little information is available on mVP40 lipid binding properties. Here, we have investigated the in vitro and cellular mechanisms by which mVP40 associates with lipid membranes. mVP40 associates with anionic membranes in a nonspecific manner that is dependent upon the anionic charge density of the membrane. These results are consistent with recent structural determination of mVP40, which elucidated an mVP40 dimer with a flat and extensive cationic lipid binding interface.
AB - Marburg virus (MARV), which belongs to the virus family Filoviridae, causes hemorrhagic fever in humans and nonhuman primates that is often fatal. MARV is a lipid-enveloped virus that during the replication process extracts its lipid coat from the plasma membrane of the host cell it infects. MARV carries seven genes, one of which encodes its matrix protein VP40 (mVP40), which regulates the assembly and budding of the virions. Currently, little information is available on mVP40 lipid binding properties. Here, we have investigated the in vitro and cellular mechanisms by which mVP40 associates with lipid membranes. mVP40 associates with anionic membranes in a nonspecific manner that is dependent upon the anionic charge density of the membrane. These results are consistent with recent structural determination of mVP40, which elucidated an mVP40 dimer with a flat and extensive cationic lipid binding interface.
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U2 - 10.1128/JVI.02607-15
DO - 10.1128/JVI.02607-15
M3 - Article
VL - 90
SP - 3074
EP - 3085
JO - Journal of Virology
JF - Journal of Virology
SN - 0022-538X
IS - 6
ER -