Lipid rafts and HIV-1: from viral entry to assembly of progeny virions

Campbell, Sally; Crowe, Suzanne; Mak, Johnson

doi:10.1016/s1386-6532(01)00193-7

Cited by 254 publications

(186 citation statements)

References 96 publications

Supporting

Mentioning

172

Contrasting

Unclassified

Order By: Relevance

“…However, although palmitoylation was shown to be crucial for CD39 localization in caveolae, 34 it seems to be unnecessary for its localization in lipid rafts. Because HIV-1 particles are known to be released from specialized glycolipid-enriched microdomains commonly called lipid rafts, 57,58 our observations support the hypothesis that CD39 is incorporated probably because of its physical presence in the membrane microdomains where virus budding is taking place.…”

Section: Discussionsupporting

confidence: 73%

“…34 Since both lipid rafts and the myristoylation of Gag precursor proteins are critical for HIV-1 membrane targeting and assembly, which result in the release of viruses from lipid rafts, 57,58 it was tempting to speculate that CD39 is incorporated simply because of its physical presence in the membrane microdomains where virus budding is occurring. To assess the putative involvement of the post-translational modification in CD39 incorporation within HIV-1, we used a truncated form of the enzyme lacking the N-terminal intracytoplasmic region, i.e.…”

Section: Cd39 Palmitoylation Is Not Required For Its Incorporation Wimentioning

confidence: 99%

See 1 more Smart Citation

The Nucleoside Triphosphate Diphosphohydrolase-1/CD39 Is Incorporated into Human Immunodeficiency Type 1 Particles, Where It Remains Biologically Active

Barat

Martin

Beaudoin

et al. 2007

Journal of Molecular Biology

View full text Add to dashboard Cite

Human immunodeficiency virus type 1 (HIV-1) carries a variety of host proteins in addition to virus-encoded structural proteins, both in its envelope and inside the viral particle. Previous studies have reported that the HIV-1 life-cycle is affected by such virus-associated host cell surface proteins. The nucleoside triphosphate diphosphohydrolase-1 (NTPDase1), also known as CD39, is a plasma membrane-bound ectoenzyme that hydrolyzes extracellular ATP and ADP to AMP. It has been shown that CD39 inhibits platelet function, and is thus a critical thromboregulatory molecule. We demonstrate here that host-derived CD39 is acquired by both laboratory-adapted and clinical variants of HIV-1 produced in cellular reservoirs of the virus. Moreover, purified CD39-bearing virions, but not isogenic viruses lacking CD39, display strong ATPase and ADPase activities. It is of particular interest that virions bearing this cellular enzyme can inhibit ADP-induced platelet aggregation, an effect blocked by an NTPDase inhibitor. On the basis of published and the present data on the functionality of human cellular proteins embedded within HIV-1, it can be proposed that these proteins might contribute to some of the immunologic deficiencies seen in infected individuals.

show abstract

Section: Discussionsupporting

confidence: 73%

Section: Cd39 Palmitoylation Is Not Required For Its Incorporation Wimentioning

confidence: 99%

The Nucleoside Triphosphate Diphosphohydrolase-1/CD39 Is Incorporated into Human Immunodeficiency Type 1 Particles, Where It Remains Biologically Active

Barat

Martin

Beaudoin

et al. 2007

Journal of Molecular Biology

View full text Add to dashboard Cite

show abstract

“…These domains have been implicated in several key cellular functions such as signaling, endocytosis, polarization (Simons and Toomre, 2000). Raft domains have also been shown to be the entry points for viruses (Campbell et al, 2001) and toxins (Lencer, 2001) and to act as pathogenic platforms for conversion of the cellular prion (PrP c ) to the scrapie version (PrP sc ) (Hooper, 2005), for bcleavage of the amyloid precursor protein (APP) (Ehehalt et al, 2003), and for activation of anthrax toxin (Abrami et al, 2003;Kurzchalia, 2003).…”

Section: Introductionmentioning

confidence: 99%

Raft association and lipid droplet targeting of flotillins are independent of caveolin

Rajendran

Lay

Illges

2007

Biological Chemistry

View full text Add to dashboard Cite

Lipid rafts are liquid ordered platforms that dynamically compartmentalize membranes. Caveolins and flotillins constitute a group of proteins that are enriched in these domains. Caveolin-1 has been shown to be an essential component of caveolae. Flotillins were also discovered as an integral component of caveolae and have since been suggested to interact with caveolins. However, flotillins are also expressed in non-caveolae-containing cells such as lymphocytes and neuronal cells. Hence, a discrepancy exists in the literature regarding the caveolin dependence of flotillin expression and their subcellular localization. To address this controversy, we used mouse embryonic fibroblasts (MEFs) from caveolin-1 knockout (Cav-1 -/-) and wild-type mice to study flotillin expression and localization. Here we show that both membrane association and lipid raft partitioning of flotillins are not perturbed in Cav-1 -/-MEFs, whereas membrane targeting and raft partitioning of caveolin-2, another caveolin family protein, is severely impaired. Moreover, we demonstrate that flotillin-1, but not flotillin-2, associates with lipid droplets upon oleic acid treatment and that this association is completely independent of caveolin. Taken together, our results show that flotillins are localized in lipid rafts independent of caveolin-1 and that translocation of flotillin-1 to lipid droplets is a caveolin-independent process.

show abstract

“…In addition to its role in entry of non enveloped the role of membrane rafts in entry of enveloped viruses has been investigated in studies using influenza virus (Orthomyxoviridae) [57][58][59][60][61], human immunodeficiency virus type 1 (HIV-1; Retroviridae) [62][63][64][65][66][67], human T lymphotropic virus 1 (HTLV-1; Retroviridae) [68,69], Ebola virus (Filoviridae) [70], Marburg virus (Filoviridae) [70,71], Epstein-Barr virus (EBV; herpesviridae) [72,73], herpes simplex virus-1 (HSV-1; herpesviridae) [74] including porcine herpesvirus-1 pseudorabies virus [75], human herpesvirus-6 (HHV-6; Herpesviridae) [76], human herpesvirus-8 (HHV-8; Herpesviridae) [77], vaccinia virus (Poxviridae) [78], coronavirus including severe acute respiratory syndrome coronavirus (SARS-CoV; Coronaviridae) [79][80][81][82][83][84][85], West Nile virus (WNV; Flaviviridae) [86], dengue virus (DEN; Flaviviridae) [87][88][89], Japanese encephalitis virus (JEV; Flaviviridae) [89], human hepatitis C virus (HCV; Flaviviridae) [90,91], Semliki Forest virus (Togaviridae) [92][93][94][95], Sindbis virus (Togaviridae) …”

Section: Role Of Membrane Rafts In Virus Entrymentioning

confidence: 99%

“…The role of membrane rafts in the assembly and budding of enveloped viruses has been investigated for influenza virus [59,63,[150][151][152][153][154][155][156][157][158][159][160], HIV-1 [63,[161][162][163][164][165][166][167][168][169][170][171][172][173], HTLV-1 [174], measles virus (Paramyxoviridae) [63,175,176], Sendai virus [Paramyxoviridae] [177,178], Newcastle disease virus (NDV; Paramyxoviridae) [179,180], RSV [147,148,[181][182][183][184], HSV [185,186], murine cytomegalovirus (MCMV; Herpesviridae) [187], Ebola virus [70,188], Marburg virus [70], and vesicular stomatitis virus (VSV; Rhabdoviridae) …”

Section: Role Of Membrane Rafts In Virus Genome Replication Assemblymentioning

confidence: 99%

Role of Membrane Rafts in Viral Infection

Takahashi¹,

Suzuki²

2009

TODJ

View full text Add to dashboard Cite

Membrane rafts are small (10-200 nm), heterogeneous, highly dynamic, sterol-and sphingolipid-enriched domains that compartmentalize cellular processes. Many studies have established that membrane rafts play an important role in the process of virus infection cycle and virus-associated diseases. It is well known that many viral components or virus receptors are concentrated in the lipid microdomains. Viruses are divided into four main classes, nonenveloped RNA virus, enveloped RNA virus, nonenveloped DNA virus, and enveloped DNA virus. General virus infection cycle is also classified into two sections, the early stage (entry) and the late stage (assembly and budding of virion). Caveola-dependent endocytosis has been investigated mostly by analysis of cell entry of the SV40 representative of polyomaviruses. Thus, the study of membrane rafts has been partially advanced by virological researches. Membrane rafts also act as a scaffold of many cellular signal transductions. Involvement of membrane rafts in many virus-associated diseases is often responsible for up-or down-regulation of cellular signal transductions. What is the role of membrane rafts in virus replications? Viruses do not necessarily require and probably utilize membrane rafts for more efficiency in virus entry, viral genome replication, high-infective virion production, and cellular signaling activation toward advantageous virus replication. In this review, we described the involvement of membrane rafts in the virus life cycle and virus-associated diseases.

show abstract

Lipid rafts and HIV-1: from viral entry to assembly of progeny virions

Cited by 254 publications

References 96 publications

The Nucleoside Triphosphate Diphosphohydrolase-1/CD39 Is Incorporated into Human Immunodeficiency Type 1 Particles, Where It Remains Biologically Active

The Nucleoside Triphosphate Diphosphohydrolase-1/CD39 Is Incorporated into Human Immunodeficiency Type 1 Particles, Where It Remains Biologically Active

Raft association and lipid droplet targeting of flotillins are independent of caveolin

Role of Membrane Rafts in Viral Infection

Contact Info

Product

Resources

About