Interactions between cellular actin and human respiratory syncytial virus (HRSV)

Ulloa, Luis; Serra, Roberto; Asenjo, Ana B.; Villanueva, Nieves

doi:10.1016/s0168-1702(97)00121-4

Cited by 68 publications

(88 citation statements)

References 34 publications

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“…Several cytoskeletal proteins, including actin isoforms, cofilin, and filamin-1, were detected by mass spectrometry analyses of purified viral filaments (although purity was difficult to assess due to the cell-associated nature of filaments). There is ample evidence of a role for polymerized actin and actinregulatory proteins in assembly (4,6,11,22,30,32,49,53,59). However, the role of polymerized actin seems to be limited to the actual budding/release event (11,30,32), which was shown previously to occur at sites of lipid rafts (8,9,22,27,31,36,42,49,50).…”

Section: Discussionmentioning

confidence: 99%

“…However, the composition and functions of IBs, including a potential role in viral filament formation, are poorly understood. Several reports have implicated cytoskeletal elements in the processes that lead to virus egress, in particular microtubules, myosin V, actin, and actin-regulatory proteins such as profilin and RhoA (30,32,59). In addition, a role for an actin/myosinbased motility system in HRSV exit has been proposed (6,53,59), and there is strong evidence for the involvement of lipid rafts (8,9,22,27,31,36,49,50,53).…”

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confidence: 99%

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The Human Respiratory Syncytial Virus Matrix Protein Is Required for Maturation of Viral Filaments

Mitra

Baviskar

Duncan-Decocq

et al. 2012

J Virol

110

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An experimental system was developed to generate infectious human respiratory syncytial virus (HRSV) lacking matrix (M) protein expression (M-null virus) from cDNA. The role of the M protein in virus assembly was then examined by infecting HEp-2 and Vero cells with the M-null virus and assessing the impact on infectious virus production and viral protein trafficking. In the absence of M, the production of infectious progeny was strongly impaired. Immunofluorescence (IF) microscopy analysis using antibodies against the nucleoprotein (N), attachment protein (G), and fusion protein (F) failed to detect the characteristic virusinduced cell surface filaments, which are believed to represent infectious virions. In addition, a large proportion of the N protein was detected in viral replication factories termed inclusion bodies (IBs). High-resolution analysis of the surface of M-null virusinfected cells by field emission scanning electron microscopy (SEM) revealed the presence of large areas with densely packed, uniformly short filaments. Although unusually short, these filaments were otherwise similar to those induced by an M-containing control virus, including the presence of the viral G and F proteins. The abundance of the short, stunted filaments in the absence of M indicates that M is not required for the initial stages of filament formation but plays an important role in the maturation or elongation of these structures. In addition, the absence of mature viral filaments and the simultaneous increase in the level of the N protein within IBs suggest that the M protein is involved in the transport of viral ribonucleoprotein (RNP) complexes from cytoplasmic IBs to sites of budding.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

The Human Respiratory Syncytial Virus Matrix Protein Is Required for Maturation of Viral Filaments

Mitra

Baviskar

Duncan-Decocq

et al. 2012

J Virol

110

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“…1). In addition, the viral particle contains cellular proteins, such as actin, which has been demonstrated on the surface of HRSV [148], caveolin-1 [18] and MHC class I molecules 1 . Thus, BRSV propagated in bovine cells can be neutralised by monoclonal antibodies specific for bovine MHC class I.…”

Section: The Virionmentioning

confidence: 99%

Bovine respiratory syncytial virus infection

Valarcher¹,

2007

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-Bovine respiratory syncytial virus (BRSV) belongs to the pneumovirus genus within the family Paramyxoviridae and is a major cause of respiratory disease in young calves. BRSV is enveloped and contains a negative sense, single-stranded RNA genome encoding 11 proteins. The virus replicates predominantly in ciliated respiratory epithelial cells but also in type II pneumocytes. It appears to cause little or no cytopathology in ciliated epithelial cell cultures in vitro, suggesting that much of the pathology is due to the host's response to virus infection. RSV infection induces an array of pro-inflammatory chemokines and cytokines that recruit neutrophils, macrophages and lymphocytes to the respiratory tract resulting in respiratory disease. Although the mechanisms responsible for induction of these chemokines and cytokines are unclear, studies on the closely related human (H)RSV suggest that activation of NF-κB via TLR4 and TLR3 signalling pathways is involved. An understanding of the mechanisms by which BRSV is able to establish infection and induce an inflammatory response has been facilitated by advances in reverse genetics, which have enabled manipulation of the virus genome. These studies have demonstrated an important role for the non-structural proteins in anti-interferon activity, a role for a virokinin, released during proteolytic cleavage of the fusion protein, in the inflammatory response and a role for the SH and the secreted form of the G protein in establishing pulmonary infection. Knowledge gained from these studies has also provided the opportunity to develop safe, stable, live attenuated virus vaccine candidates.

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“…Assembly and budding of RSV takes place at the apical cell surface from lipid raft- [30]. In the same study, N and M were both shown to interact with soluble, monomeric actin.…”

Section: Movement To Site Of Virus Buddingmentioning

confidence: 78%

“…By analogy to other related viruses in Mononegavirales, M association may also result in a tightly coiled nucleocapsid in preparation for packaging with the envelope glycoprotein complex [28]. This inference is based on studies showing that removal of M from virions results in collapse of internal structure and a very loose, extended nucleocapsid [29]; and by a study showing that N protein, which is accessible to antibodies in nucleocapsids without M, becomes inaccessible when M is present [30]. Using cells cotransfected to express various combinations of N, P, L, M2-1 and M, it was shown that M only colocalised to cytoplasmic inclusions that also contained M2-1; M association was almost certainly via its interaction with M2-1 dependent on M's N terminus [9].…”

Section: A Formation Of Cytoplasmic Inclusionsmentioning

confidence: 99%

Protein-Protein Interactions in RSV Assembly: Potential Targets for Attenuating RSV Strains

Ghildyal

Jans²,

Bardin

et al. 2012

IDDT

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Respiratory syncytial virus (RSV) is the major respiratory pathogen of infants and children worldwide, with no effective treatment or vaccine available. Steady progress has been made in understanding the respiratory syncytial virus lifecycle and the consequences of infection, but some areas of RSV still remain poorly understood. Although many of the interactions between virus proteins that are required for efficient RSV assembly have been elucidated, many questions still remain regarding viral assembly, as well as the mechanisms of RSV budding. This review will summarise the current understanding of RSV assembly, including the various interactions between virus proteins and the involvement of cellular factors with a view to identifying possible attenuation and/or drug targets within the assembly pathway.

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Interactions between cellular actin and human respiratory syncytial virus (HRSV)

Cited by 68 publications

References 34 publications

The Human Respiratory Syncytial Virus Matrix Protein Is Required for Maturation of Viral Filaments

The Human Respiratory Syncytial Virus Matrix Protein Is Required for Maturation of Viral Filaments

Bovine respiratory syncytial virus infection

Protein-Protein Interactions in RSV Assembly: Potential Targets for Attenuating RSV Strains

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