Heat Shock Cognate Protein 70 Is a Cell Fusion-Enhancing Factor but Not an Entry Factor for Human T-Cell Lymphotropic Virus Type I

Fang, Deyu; Haraguchi, Yuji; Jinno, Atsushi; Soda, Yasushi; Shimizu, Nobuaki; Hoshino, Hiroo

doi:10.1006/bbrc.1999.1028

Cited by 24 publications

(19 citation statements)

References 38 publications

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“…When interacting with RNA viruses, other functions were found for Hsc70. It was involved in syncytium formation by human T-cell lymphotropic virus type I (Fang et al, 1999;Sagara et al, 1998Sagara et al, , 2001. It was also shown to be part of a complex receptor for rotavirus entry into the cell (Guerrero et al, 2002).…”

Section: Discussionmentioning

confidence: 99%

Autographa californica nucleopolyhedrovirus infection of Spodoptera frugiperda cells: a global analysis of host gene regulation during infection, using a differential display approach

Nobiron

O’Reilly

Olszewski

2003

Journal of General Virology

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Autographa californica nucleopolyhedrovirus (AcMNPV), the type member of the virus family Baculoviridae, infects pest insects and has been the subject of many studies for its development as a biopesticide. It is also the virus upon which most of the commercial baculovirus protein expression systems are based. AcMNPV infection of cultured host Spodoptera frugiperda (Sf9) cells can induce a number of alterations of host cell properties including altering the cellular cytoskeleton, an arrest of the cell cycle in G 2 /M, and the global shutoff of host protein translation. Additionally, several cellular transcripts have been shown to be down-regulated following AcMNPV infection. In this study, we take a differential display approach to address whether a global down-regulation of Sf9 host transcripts occurs at late times of infection. Additionally, we also use this approach to search for host mRNAs which are up-regulated at early times of infection, and may be important for facilitating baculovirus infection. From these experiments we can confirm a global down-regulation of Sf9 mRNA levels at late times of infection. We also found that up-regulation of individual host gene RNA levels at early times of infection did not occur frequently. One host transcript which was found to be transiently up-regulated as a result of AcMNPV infection was an Sf9 Hsc70 gene. Hsc70 proteins have been shown to play a vital role in the life-cycle of other large DNA viruses, which suggests that this protein is also important for baculovirus infection.

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Section: Discussionmentioning

confidence: 99%

Autographa californica nucleopolyhedrovirus infection of Spodoptera frugiperda cells: a global analysis of host gene regulation during infection, using a differential display approach

Nobiron

O’Reilly

Olszewski

2003

Journal of General Virology

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“…Also, hsc70 has been described as an enhancement factor on the surface of murine fibroblasts and in a human T-cell line for the syncytium formation induced by human T-cell lymphotropic virus type 1 (13,49). In this work, we have shown that hsc70 seems to be involved in the cell entry of rotaviruses.…”

Section: Vol 76 2002 Notes 4097mentioning

confidence: 99%

Heat Shock Cognate Protein 70 Is Involved in Rotavirus Cell Entry

Guerrero

Bouyssounade

Zárate

et al. 2002

J Virol

151

128

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In this work, we have identified the heat shock cognate protein (hsc70) as a receptor candidate for rotaviruses. hsc70 was shown to be present on the surface of MA104 cells, and antibodies to this protein blocked rotavirus infectivity, while not affecting the infectivity of reovirus and poliovirus. Preincubation of the hsc70 protein with the viruses also inhibited their infectivity. Triple-layered particles (mature virions), but not double-layered particles, bound hsc70 in a solid-phase assay, and this interaction was blocked by monoclonal antibodies to the virus surface proteins VP4 and VP7. Rotaviruses were shown to interact with hsc70 at a postattachment step, since antibodies to hsc70 and the protein itself did not inhibit the virus attachment to cells. We propose that the functional rotavirus receptor is a complex of several cell surface molecules that include, among others, hsc70.

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“…When the improperly folded or incompletely assembled proteins fail to restore their functional states, they are degraded by the ER-associated degradation (ERAD) system, which involves a retrograde transfer of proteins from the ER to the cytosol followed by degradation by the proteasome (11)(12)(13) (14 -16). It has been reported that many E3s are involved in the ERAD pathway, such as ER-embedded Hrd1 (17) and Doa10 (18), which have overlapping functions in yeast, and gp78 (19), CHIP (20) and Parkin (21), which ubiquitylate ER membrane proteins such as cystic fibrosis transmembrane conductance regulator (CFTR) and the Pael receptor in mammals. In addition, we have recently identified a novel member of the ERAD-linked E3 family, SCF Fbx2 , which participates in ERAD for selective elimination of glycoproteins (7).…”

mentioning

confidence: 99%

Fbs2 Is a New Member of the E3 Ubiquitin Ligase Family That Recognizes Sugar Chains

Yoshida

Tokunaga

Chiba

et al. 2003

Journal of Biological Chemistry

168

118

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Heat Shock Cognate Protein 70 Is a Cell Fusion-Enhancing Factor but Not an Entry Factor for Human T-Cell Lymphotropic Virus Type I

Cited by 24 publications

References 38 publications

Autographa californica nucleopolyhedrovirus infection of Spodoptera frugiperda cells: a global analysis of host gene regulation during infection, using a differential display approach

Autographa californica nucleopolyhedrovirus infection of Spodoptera frugiperda cells: a global analysis of host gene regulation during infection, using a differential display approach

Heat Shock Cognate Protein 70 Is Involved in Rotavirus Cell Entry

Fbs2 Is a New Member of the E3 Ubiquitin Ligase Family That Recognizes Sugar Chains

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