Association of heat shock protein 70 with enterovirus capsid precursor P1 in infected human cells

Macejak, Dennis G.; Sarnow, Peter

doi:10.1128/jvi.66.3.1520-1527.1992

Cited by 91 publications

(52 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In this study, we identified two molecular chaperones incorporated into purified NDV particles, HSP70 and HSP90. HSP70 interacts with various viral proteins and may be involved in the assembly of adenovirus [41], enterovirus [42], vaccinia virus [43] and hantaan virus [44]. Virion-associated HSP70 might participate in early events of infection, uncoating the viral capsid in a manner similar to its role in the uncoating of clathrin cages [65].…”

Section: Discussionmentioning

confidence: 99%

Proteomic analysis of purified Newcastle disease virus particles

et al. 2012

View full text Add to dashboard Cite

BackgroundNewcastle disease virus (NDV) is an enveloped RNA virus, bearing severe economic losses to the poultry industry worldwide. Previous virion proteomic studies have shown that enveloped viruses carry multiple host cellular proteins both internally and externally during their life cycle. To address whether it also occurred during NDV infection, we performed a comprehensive proteomic analysis of highly purified NDV La Sota strain particles.ResultsIn addition to five viral structural proteins, we detected thirty cellular proteins associated with purified NDV La Sota particles. The identified cellular proteins comprised several functional categories, including cytoskeleton proteins, annexins, molecular chaperones, chromatin modifying proteins, enzymes-binding proteins, calcium-binding proteins and signal transduction-associated proteins. Among these, three host proteins have not been previously reported in virions of other virus families, including two signal transduction-associated proteins (syntenin and Ras small GTPase) and one tumor-associated protein (tumor protein D52). The presence of five selected cellular proteins (i.e., β-actin, tubulin, annexin A2, heat shock protein Hsp90 and ezrin) associated with the purified NDV particles was validated by Western blot or immunogold labeling assays.ConclusionsThe current study presented the first standard proteomic profile of NDV. The results demonstrated the incorporation of cellular proteins in NDV particles, which provides valuable information for elucidating viral infection and pathogenesis.

show abstract

Section: Discussionmentioning

confidence: 99%

Proteomic analysis of purified Newcastle disease virus particles

et al. 2012

View full text Add to dashboard Cite

show abstract

“…3C and 5, we propose that the newly made capsid precursor P1 that is released from the polyprotein and myristoylated ( Fig. 3C, PV stage I) interacts with the chaperone Hsp90 to achieve a conformation (PV stage II) competent for cleavage by 3CD pro (33,34). After proteolytic processing, assembly of the cleavage products occurs in a stepwise manner.…”

Section: Model Of Enterovirus Morphogenesismentioning

confidence: 97%

“…The N-terminal glycine of the newly formed poliovirus P1 capsid precursor is rapidly modified (perhaps also cotranslationally) by covalent linkage to myristic acid (30)(31)(32), after which it becomes a client of the cellular chaperone Hsp90 to attain a processing-competent conformation (referred to as P1* in Fig. 3C, step II) (33,34). It is not known whether myristoylation of PV P1 is a prerequisite for its interaction with the chaperone Hsp90.…”

Section: Figmentioning

confidence: 99%

Picornavirus Morphogenesis

Jiang

Liu

et al. 2014

Microbiol Mol Biol Rev

199

196

View full text Add to dashboard Cite

SUMMARY The Picornaviridae represent a large family of small plus-strand RNA viruses that cause a bewildering array of important human and animal diseases. Morphogenesis is the least-understood step in the life cycle of these viruses, and this process is difficult to study because encapsidation is tightly coupled to genome translation and RNA replication. Although the basic steps of assembly have been known for some time, very few details are available about the mechanism and factors that regulate this process. Most of the information available has been derived from studies of enteroviruses, in particular poliovirus, where recent evidence has shown that, surprisingly, the specificity of encapsidation is governed by a viral protein-protein interaction that does not involve an RNA packaging signal. In this review, we make an attempt to summarize what is currently known about the following topics: (i) encapsidation intermediates, (ii) the specificity of encapsidation (iii), viral and cellular factors that are required for encapsidation, (iv) inhibitors of encapsidation, and (v) a model of enterovirus encapsidation. Finally, we compare some features of picornavirus morphogenesis with those of other plus-strand RNA viruses.

show abstract

“…HSP70 and HSP90 have been found incorporated into IBV. HSP70 interacts with various viral proteins and may be involved in the assembly of adenovirus [45], enterovirus [46], vaccinia virus [47] and hantaan virus [48]. Alternatively, upon entry into susceptible target cells, virion-associated HSP70 might participate in early events of infection.…”

Section: Discussionmentioning

confidence: 99%

Proteomic analysis of purified coronavirus infectious bronchitis virus particles

et al. 2010

View full text Add to dashboard Cite

BackgroundInfectious bronchitis virus (IBV) is the coronavirus of domestic chickens causing major economic losses to the poultry industry. Because of the complexity of the IBV life cycle and the small number of viral structural proteins, important virus-host relationships likely remain to be discovered. Toward this goal, we performed two-dimensional gel electrophoresis fractionation coupled to mass spectrometry identification approaches to perform a comprehensive proteomic analysis of purified IBV particles.ResultsApart from the virus-encoded structural proteins, we detected 60 host proteins in the purified virions which can be grouped into several functional categories including intracellular trafficking proteins (20%), molecular chaperone (18%), macromolcular biosynthesis proteins (17%), cytoskeletal proteins (15%), signal transport proteins (15%), protein degradation (8%), chromosome associated proteins (2%), ribosomal proteins (2%), and other function proteins (3%). Interestingly, 21 of the total host proteins have not been reported to be present in virions of other virus families, such as major vault protein, TENP protein, ovalbumin, and scavenger receptor protein. Following identification of the host proteins by proteomic methods, the presence of 4 proteins in the purified IBV preparation was verified by western blotting and immunogold labeling detection.ConclusionsThe results present the first standard proteomic profile of IBV and may facilitate the understanding of the pathogenic mechanisms.

show abstract

Association of heat shock protein 70 with enterovirus capsid precursor P1 in infected human cells

Cited by 91 publications

References 35 publications

Proteomic analysis of purified Newcastle disease virus particles

Proteomic analysis of purified Newcastle disease virus particles

Picornavirus Morphogenesis

Proteomic analysis of purified coronavirus infectious bronchitis virus particles

Contact Info

Product

Resources

About