Influenza Virus Assembly and Lipid Raft Microdomains: a Role for the Cytoplasmic Tails of the Spike Glycoproteins

Zhang, Jie; Pekosz, Andrew; Lamb, Robert A.

doi:10.1128/jvi.74.10.4634-4644.2000

Cited by 350 publications

(403 citation statements)

References 74 publications

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“…Thus, association of HA with sulfatide may trigger MAPK activation to enhance viral RNP export. Some studies have shown the existence of sulfatide within membrane rafts [198,199], but lipid composition of purified influenza virus grown in embryonated eggs does not contain any acidic glycosphingolipids including sulfatide [154]. The raft localization of sulfatide leading to enhancement of viral RNP export has not yet been ascertained.…”

Section: Role Of Membrane Rafts In Virus Genome Replication Assemblymentioning

confidence: 99%

“…HA, NA, NP and M2 independently utilize membrane rafts together with apical targeting signal sequence for the apical sorting process, leading to efficient preferential budding and release of progeny viruses from the apical surface membrane. However, direct interactions with membrane rafts are not necessarily essential for apical sorting of these viral proteins, indicating that they can also interact with apical sorting machineries outside their membrane rafts [150,[152][153][154]156]. For example, cellular protein VIP17/MAL, a raftassociated protein, is involved in apical transport of HA in dog kidney MDCK cells [192].…”

Section: Role Of Membrane Rafts In Virus Genome Replication Assemblymentioning

confidence: 99%

“…Although these domains of NA are essential for the association with rafts, there is no evidence that NA possesses palmitoylated residues. The mechanism by which NP associates with rafts remains unknown [104,[154][155][156]191]. HA, NA, NP and M2 independently utilize membrane rafts together with apical targeting signal sequence for the apical sorting process, leading to efficient preferential budding and release of progeny viruses from the apical surface membrane.…”

Section: Role Of Membrane Rafts In Virus Genome Replication Assemblymentioning

confidence: 99%

“…For example, cellular protein VIP17/MAL, a raftassociated protein, is involved in apical transport of HA in dog kidney MDCK cells [192]. M1, which is not dependently associated with rafts, is incorporated into membrane rafts by interactions with cytoplasmic tails of both HA and M2, which promote the recruitment of internal viral proteins and viral RNP to the plasma membrane for efficient virus assembly and budding [154,193]. Although M1 has been reported to play a critical role in viral assembly and budding [194,195], a recent study has indicated that HA and NA, but not M1, are required for assembly and budding of influenza virus particles [159].…”

Section: Role Of Membrane Rafts In Virus Genome Replication Assemblymentioning

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%

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Role of Membrane Rafts in Viral Infection

Takahashi¹,

Suzuki²

2009

TODJ

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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.

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Section: Role Of Membrane Rafts In Virus Genome Replication Assemblymentioning

confidence: 99%

Section: Role Of Membrane Rafts In Virus Genome Replication Assemblymentioning

confidence: 99%

Section: Role Of Membrane Rafts In Virus Genome Replication Assemblymentioning

confidence: 99%

Section: Role Of Membrane Rafts In Virus Genome Replication Assemblymentioning

confidence: 99%

Section: Role Of Membrane Rafts In Virus Genome Replication Assemblymentioning

confidence: 99%

See 3 more Smart Citations

Role of Membrane Rafts in Viral Infection

Takahashi¹,

Suzuki²

2009

TODJ

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New structural insights into the multifunctional influenza A matrix protein 1

2021

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Influenza A virus matrix protein 1 (M1) is the most abundant protein within virions and functions at multiple steps of the virus life cycle, including nuclear RNA export, virus particle assembly, and virus disassembly. Two recent publications have presented the first structures of full‐length M1 and show that it assembles filaments in vitro via an interface between the N‐ and C‐terminal domains of adjacent monomers. These filaments were found to be similar to those that form the endoskeleton of assembled virions. The structures provide a molecular basis to understand the functions of M1 during the virus life cycle. Here, we compare and discuss the two structures, and explore their implications for the mechanisms by which the multifunctional M1 protein can mediate virus assembly, interact with viral ribonucleoproteins and act during infection of a new cell.

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