Interaction of canine distemper virus nucleocapsid variants with 70K heat-shock proteins

Oglesbee, Michael; Ringler, Susan S.; Krakowka, Steven

doi:10.1099/0022-1317-71-7-1585

Cited by 44 publications

(39 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For example, heat shock protein 72, an inducible member of the 70-kDa family of heat shock proteins, was previously shown to interact with the canine distemper virus ribonucleoprotein (46) and to increase polymerase activity (47). More recently, heat shock protein 72 was shown to interact with the nucleoprotein of measles viruses (48), enhance viral polymerase processivity, and subsequently increase mortality in mice, as well (34).…”

Section: Discussionmentioning

confidence: 99%

The dynein light chain 8 binding motif of rabies virus phosphoprotein promotes efficient viral transcription

Tan¹,

Preuss²,

Williams

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

121

105

View full text Add to dashboard Cite

Recent studies indicate that the interaction between rabies virus (RV) phosphoprotein and the dynein light chain 8 (LC8) is essential for RV pathogenesis. Through its association with the dynein motor complex, LC8 has been suggested as a molecular factor that links the viral ribonucleoprotein to the host cell transport system. Recent structural investigations, however, dispute this model. To understand the role of LC8 in RV pathogenesis, we generated recombinant RVs with or without the LC8 binding domain (LC8-BD) deleted from the RV phosphoprotein. Peripheral infection of adult mice showed that removal of the LC8-BD did not inhibit entry into the CNS, although it prevented onset of RV-induced CNS disease. However, deletion of the LC8-BD significantly attenuated viral transcription and replication in the CNS. Studies in RAG2 knockout (KO) mice infected with the same recombinant RVs confirmed this finding and indicated that the adaptive immune system is not a factor in the attenuation of viral replication early in the infection. In cell culture, the deletion of the LC8-BD greatly attenuated growth on neuronal cells whereas the growth pattern on nonneuronal cells remained unchanged. However, deletion of the LC8-BD did not affect production of RV virions. We provide evidence that removal of the LC8-BD decreases primary transcription. In this study, we propose that LC8 does not play a role in the retrograde axonal transport of RV and that the deletion of the LC8-BD impairs the infectivity of the virions by reducing early transcription and replication in neurons.pathogenesis ͉ negative-strand RNA viruses ͉ rhabdovirus ͉ viral transport R abies virus (RV) is a member of the family Rhabdoviridae that infects the CNS. RV has a relatively simple genome that encodes the five structural proteins: nucleoprotein (N), phosphoprotein (P), matrix (M), glycoprotein (G), and RNA polymerase (L). Pathogenic RV infection without immediate postexposure prophylaxis frequently causes fatal encephalomyelitis in both humans and animals and has the distinction of having the highest case-fatality ratio among infectious pathogens (1). Past experiments in mice have suggested that street strains of RV initiate infection at the nerve terminals of the peripheral nervous system (PNS) and then travel along the axons located in the spinal cord (2, 3). Consequently, this axonal transport leads to RV infection of the brain (4). Yet, the molecular basis for the transport of the RV particle remains unclear and controversial. Most transneuronal studies of the CNS in nonhuman primates (5, 6) and mice (7,8) reveal that fixed (laboratory-adapted) strains of RV spread exclusively in the retrograde direction; however, past in vitro and in vivo studies suggest that anterograde transport might also be involved (7, 9-11). The discovery that the dynein light chain, LC8 (DNLC1), interacts with the RV phosphoprotein (RVP) provides a putative molecular link between the virus and host cell transport system and, thus, a potential mechanism for the neuroinvasive prope...

show abstract

Section: Discussionmentioning

confidence: 99%

The dynein light chain 8 binding motif of rabies virus phosphoprotein promotes efficient viral transcription

Tan¹,

Preuss²,

Williams

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

121

105

View full text Add to dashboard Cite

show abstract

“…The molecular chaperone BiP is bound early in the molecular folding of the VSV G protein, whereas calnexin is bound to more mature folded molecules. Not only are chaperones and heat shock proteins found with purified rhabdoviruses, but they are also associated with other viruses: canine distemper (Oglesbee et al 1990), adenovirus (Macejak & Luftig 1991), sindbis virus (Mulvey & Brown 1995) and vaccinia virus (Jindal & Young 1992). Sagara et al (1995) identified the cellular actin-binding EzrinRadixin-moesin (ERM) family of proteins incorporated into the rabies virion.…”

Section: Discussionmentioning

confidence: 99%

Responses of cloned rainbow trout Oncorhynchus mykiss to an attenuated strain of infectious hematopoietic necrosis virus

Ristow¹,

LaPatra²,

Dixon³

et al. 2000

Dis. Aquat. Org.

View full text Add to dashboard Cite

The objective of this work was to examine the response of homozygous clones of rainbow trout to vaccination by an attenuated strain (Nan Scott Lake; NSL) of infectious hematopoietic necrosis virus (IHNV). Adult rainbow trout of the Hot Creek Strain (YY males maintained in a recirculating system at 12°C) were injected 3 times with 10 5 to 10 7 plaque forming units (pfu) of NSL. Intraperitoneal injections were given at Day 0 and at 2 and 4 mo post-infection. All fish were nonlethally bled at monthly intervals for 18 mo. Serum from each fish was analyzed by the complementdependent neutralization assay and by western blot against purified NSL virus. The highest virus neutralization titers were detected 4 mo after the first injection, and peaked at 1280. When sera were analyzed by western blot, the predominating responses of the serum from immunized fish on the reduced western blot were against M1, a matrix protein of the virus and to a 90 kDa stress protein.The 90 kDa protein was identified by a monoclonal antibody as a stress protein derived from the CHSE-214 cells in which the purified IHN virus was grown and which associates with the virus during purification.

show abstract

“…Stress conditioning using transient hyperthermia is protective against exposure to heavy metals and such in vivo insults as myocardial and cerebral ischaemia (Mestril et al, 1994 ;Plumier et al, 1995Plumier et al, , 1997 In contrast to the cellular protective role of HSPs, stress conditioning also increases in vitro gene expression and cytopathic effect of the morbilliviruses canine distemper virus (CDV) and measles virus (MV) (Oglesbee et al, 1990Vasconcelos et al, 1998). Cytoplasmic nucleocapsid of CDV and MV from stress conditioned Vero cells supports elevated cell-free transcriptional activity relative to nucleocapsid from non-conditioned control cells.…”

Section: Introductionmentioning

confidence: 99%

“…The specific hypothesis tested was that elevation in the predominant inducible 70 kDa HSP (hsp72) is sufficient to reproduce the effect of stress conditioning upon viral infection phenotype. Support for such a pivotal role of hsp72 was based upon the correlation between cytoplasmic concentrations of hsp72 and CDV and MV mean plaque area in Vero cells (Heller et al, 1998 ;Oglesbee et al, 1990 ;Vasconcelos et al, 1998) ; hsp72 is present at low concentrations in non-stressed cells yet becomes one of the most abundant HSPs in stress conditioned cells (Mizzen & Welch, 1988). In addition, stress conditioning promotes the interaction between hsp72 and nucleocapsid (Oglesbee et al, 1990.…”

Section: Introductionmentioning

confidence: 99%

“…Support for such a pivotal role of hsp72 was based upon the correlation between cytoplasmic concentrations of hsp72 and CDV and MV mean plaque area in Vero cells (Heller et al, 1998 ;Oglesbee et al, 1990 ;Vasconcelos et al, 1998) ; hsp72 is present at low concentrations in non-stressed cells yet becomes one of the most abundant HSPs in stress conditioned cells (Mizzen & Welch, 1988). In addition, stress conditioning promotes the interaction between hsp72 and nucleocapsid (Oglesbee et al, 1990. Functional interactions between hsp72 and nucleocapsid have been shown for both CDV and MV, where hsp72 stimulates transcription (Oglesbee et al, 1996 ;Vasconcelos et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Constitutive overexpression of the major inducible 70 kDa heat shock protein mediates large plaque formation by measles virus.

Vasconcelos

Cai

Oglesbee

1998

Journal of General Virology

View full text Add to dashboard Cite

Interaction of canine distemper virus nucleocapsid variants with 70K heat-shock proteins

Cited by 44 publications

References 16 publications

The dynein light chain 8 binding motif of rabies virus phosphoprotein promotes efficient viral transcription

The dynein light chain 8 binding motif of rabies virus phosphoprotein promotes efficient viral transcription

Responses of cloned rainbow trout Oncorhynchus mykiss to an attenuated strain of infectious hematopoietic necrosis virus

Constitutive overexpression of the major inducible 70 kDa heat shock protein mediates large plaque formation by measles virus.

Contact Info

Product

Resources

About