Protein interactions entered into by the measles virus P, V, and C proteins

Liston, Peter; DiFlumeri, C.; Briedis, Dalius J.

doi:10.1016/0168-1702(95)00067-z

Cited by 58 publications

(42 citation statements)

References 55 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The same results were obtained by gradually increasing the amounts of PNT to molar excesses as high as 5 (data not shown). These results can be accounted for by assuming either that the two proteins do not interact, in agreement with the results reported in the literature (9,68), or that the interaction does not imply any concomitant unstructured-to-structured transition.…”

Section: Resultssupporting

confidence: 79%

“…The P protein of MV consists of an N-terminal moiety (aa 1-230), PNT, responsible for binding to N CORE within the N°⅐P complex (26), and of a C-terminal moiety (aa 231-507), PCT, responsible for binding to N TAIL in both N°⅐P and N NUC ⅐P complexes (9,68). We have recently shown that the PNT domain of MV P is intrinsically disordered when expressed alone (41) and probably also in the context of full-length P. 3 Therefore, the interaction between N TAIL and P may result in a possible induced folding of PNT concomitantly to the possible induced folding of N TAIL .…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

The C-terminal Domain of the Measles Virus Nucleoprotein Is Intrinsically Disordered and Folds upon Binding to the C-terminal Moiety of the Phosphoprotein

Longhi

Receveur-Brechot

Karlin

et al. 2003

Journal of Biological Chemistry

268

324

View full text Add to dashboard Cite

The nucleoprotein of measles virus consists of an Nterminal moiety, N CORE , resistant to proteolysis and a C-terminal moiety, N TAIL , hypersensitive to proteolysis and not visible as a distinct domain by electron microscopy. We report the bacterial expression, purification, and characterization of measles virus N TAIL . Using nuclear magnetic resonance, circular dichroism, gel filtration, dynamic light scattering, and small angle x-ray scattering, we show that N TAIL is not structured in solution. Its sequence and spectroscopic and hydrodynamic properties indicate that N TAIL belongs to the premolten globule subfamily within the class of intrinsically disordered proteins. The same epitopes are exposed in N TAIL and within the nucleoprotein, which rules out dramatic conformational changes in the isolated N TAIL domain compared with the full-length nucleoprotein. Most unstructured proteins undergo some degree of folding upon binding to their partners, a process termed "induced folding." We show that N TAIL is able to bind its physiological partner, the phosphoprotein, and that it undergoes such an unstructured-to-structured transition upon binding to the C-terminal moiety of the phosphoprotein. The presence of flexible regions at the surface of the viral nucleocapsid would enable plastic interactions with several partners, whereas the gain of structure arising from induced folding would lead to modulation of these interactions. These results contribute to the study of the emerging field of natively unfolded proteins.

show abstract

Section: Resultssupporting

confidence: 79%

Section: Resultsmentioning

confidence: 99%

The C-terminal Domain of the Measles Virus Nucleoprotein Is Intrinsically Disordered and Folds upon Binding to the C-terminal Moiety of the Phosphoprotein

Longhi

Receveur-Brechot

Karlin

et al. 2003

Journal of Biological Chemistry

268

324

View full text Add to dashboard Cite

show abstract

“…Organization of P-The P protein of MV consists of an N-terminal moiety, PNT (aa 1-230), which is responsible for binding to N CORE within the N 0 -P complex (21), and of a Cterminal moiety, PCT (aa 231-507), which is responsible for binding to N TAIL in both N 0 -P and N NUC -P complexes (9,29). We have recently reported that PCT interacts with the Cterminal moiety of N, N TAIL , and induces folding of the latter.…”

Section: Modularmentioning

confidence: 99%

“…The main N 0 -binding site of MV PNT has been mapped to the extreme N terminus of P (21). Paramyxovirinae PCT share three common features: (i) oligomerization through a coiled-coil region, (ii) the presence at the extreme C terminus of a short predicted bundle of three ␣-helices, which is involved in binding to N (27), and (iii) the presence of an L binding site (28,29). The P protein of the related Sendai virus (SeV), a member of the Respirovirus genus, is tetrameric, whereas the oligomeric state of MV P is unknown (21,27).…”

mentioning

confidence: 99%

Crystal Structure of the Measles Virus Phosphoprotein Domain Responsible for the Induced Folding of the C-terminal Domain of the Nucleoprotein

Johansson

Bourhis

Campanacci

et al. 2003

Journal of Biological Chemistry

147

215

View full text Add to dashboard Cite

Measles virus (MV) 1 is a member of the Paramyxovirinae sub-family within the Mononegavirales order. Its non-segmented, negative-sense, single-stranded RNA genome is packaged by the viral nucleoprotein (N) within a helical nucleocapsid. Mononegavirales use this N-RNA complex as a template for both transcription and replication. These reactions are carried out by the RNA-dependent RNA polymerase polymerase (L) in conjuction with the phosphoprotein (P) (for a review see Ref.

show abstract

“…Cyt & Nuc (Palosaari et al, 2003;Ramachandran et al, 2008) Cyt & Nuc (Wardrop & Briedis, 1991) N & P?# (Liston et al, 1995;Tober et al, 1998) MDA5 (Cyt) ;…”

Section: Mevmentioning

confidence: 99%

Roles of nuclear trafficking in infection by cytoplasmic negative-strand RNA viruses: paramyxoviruses and beyond

Audsley

Jans

Moseley

2016

Journal of General Virology

View full text Add to dashboard Cite

Genome replication and virion production by most negative-sense RNA viruses (NSVs) occurs exclusively in the cytoplasm, but many NSV-expressed proteins undergo active nucleocytoplasmic trafficking via signals that exploit cellular nuclear transport pathways. Nuclear trafficking has been reported both for NSV accessory proteins (including isoforms of the rabies virus phosphoprotein, and V, W and C proteins of paramyxoviruses) and for structural proteins. Trafficking of the former is thought to enable accessory functions in viral modulation of antiviral responses including the type I IFN system, but the intranuclear roles of structural proteins such as nucleocapsid and matrix proteins, which have critical roles in extranuclear replication and viral assembly, are less clear. Nevertheless, nuclear trafficking of matrix protein has been reported to be critical for efficient production of Nipah virus and Respiratory syncytial virus, and nuclear localization of nucleocapsid protein of several morbilliviruses has been linked to mechanisms of immune evasion. Together, these data point to the nucleus as a significant host interface for viral proteins during infection by NSVs with otherwise cytoplasmic life cycles. Importantly, several lines of evidence now suggest that nuclear trafficking of these proteins may be critical to pathogenesis and thus could provide new targets for vaccine development and antiviral therapies.

show abstract

Protein interactions entered into by the measles virus P, V, and C proteins

Cited by 58 publications

References 55 publications

The C-terminal Domain of the Measles Virus Nucleoprotein Is Intrinsically Disordered and Folds upon Binding to the C-terminal Moiety of the Phosphoprotein

The C-terminal Domain of the Measles Virus Nucleoprotein Is Intrinsically Disordered and Folds upon Binding to the C-terminal Moiety of the Phosphoprotein

Crystal Structure of the Measles Virus Phosphoprotein Domain Responsible for the Induced Folding of the C-terminal Domain of the Nucleoprotein

Roles of nuclear trafficking in infection by cytoplasmic negative-strand RNA viruses: paramyxoviruses and beyond

Contact Info

Product

Resources

About