Abstract
Retroviruses are enveloped viruses that assemble on the inner leaflet of cellular membranes. Improving biophysical techniques has recently unveiled many molecular aspects of the interaction between the retroviral structural protein Gag and the cellular membrane lipids. This interaction is driven by the N-terminal matrix domain of the protein, which probably undergoes important structural modifications during this process, and could induce membrane lipid distribution changes as well. This review aims at describing the molecular events occurring during MA-membrane interaction, and pointing out their consequences in terms of viral assembly. The striking conservation of the matrix membrane binding mode among retroviruses indicates that this particular step is most probably a relevant target for antiviral research.
Highlights
Retroviruses are enveloped single-stranded RNA (+) viruses; they include some human pathogens such as human immunodeficiency virus (HIV), and oncoviruses such as the murine leukemia virus (MLV)
One element allowing the interaction with the cellular membrane is N-terminal myristylation, a post-tranlational modification found in MAs from all retroviral families, including human immunodeficiency virus (HIV) [12], human T-lymphotropic virus (HTLV) [13], Mason-Pfizer monkey virus (M-PMV) [14] and exogenous murine leukemia virus (MLV) strains [15,16]
Matrix structures from nine retroviruses have been resolved to date: HIV1 [17,18,19,20] and 2 [21], SIV [22], HTLV-2 [23], bovine leukemia virus (BLV) [24], M-PMV [25], Rous sarcoma virus (RSV) [26], equine infectious anemia virus (EIAV) [27], and MLV [28]
Summary
Retroviruses are enveloped single-stranded RNA (+) viruses; they include some human pathogens such as human immunodeficiency virus (HIV), and oncoviruses such as the murine leukemia virus (MLV). One element allowing the interaction with the cellular membrane is N-terminal myristylation, a post-tranlational modification found in MAs from all retroviral families (myrMAs), including human immunodeficiency virus (HIV) [12], human T-lymphotropic virus (HTLV) [13], Mason-Pfizer monkey virus (M-PMV) [14] and exogenous murine leukemia virus (MLV) strains [15,16]. This myristate moiety is a common signal for membrane targeting of proteins, as it can insert into membrane bilayers. Other amino acids could be involved in Gag membrane anchoring, such as the N-terminal amino acids invovled in [T] to [R] conversion in HIV-MA [33,34]
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