The Molecular Length of Measles Virus RNA and the Structural Organization of Measles Nucleocapsids

Lund, Garry; Tyrrell, D. Lorne; Bradley, R.; Scraba, Douglas G.

doi:10.1099/0022-1317-65-9-1535

Cited by 34 publications

(23 citation statements)

References 23 publications

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“…Indeed, in agreement with Fooks et al (40), we observed that recombinant NP could selfassemble into nucleocapsid-like structures (similar to those described for MV nucleocapsids; Ref. 41). NP particles have also been identified in human DC after in vitro pulse with the recombinant protein (B. Dubois, personal communication).…”

Section: Discussionsupporting

confidence: 75%

Dendritic Cells Recruitment and In Vivo Priming of CD8+ CTL Induced by a Single Topical or Transepithelial Immunization Via the Buccal Mucosa with Measles Virus Nucleoprotein

Etchart¹,

Desmoulins²,

Chemin³

et al. 2001

The Journal of Immunology

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The buccal mucosa, a prototype of pluristratified mucosal epithelia, contains a network of directly accessible class II+ epithelial dendritic cells (DC), similar to skin Langerhans cells. We showed that a single buccal immunization with measles virus nucleoprotein (NP), by either topical application onto or intradermal injection in the buccal mucosa, induced in vivo priming of protective class I-restricted specific CD8+ CTL. Both routes of immunization with NP induced a rapid recruitment of DC into the mucosa, which peaked at 2 h and decreased by 24 h. Treatment of mice with Flt3 ligand resulted in an increased number of DC in the buccal mucosa and enhanced the frequency of IFN-γ-producing NP-specific effectors and the NP-specific CTL response generated after buccal immunization with NP. Finally, NP-pulsed bone marrow-derived DC induced NP-specific IFN-γ-producing cells upon adoptive transfer to naive mice. These data demonstrate that a viral protein delivered to DC of the buccal mucosa induces in vivo priming of protective anti-viral CD8+ CTL.

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Section: Discussionsupporting

confidence: 75%

Dendritic Cells Recruitment and In Vivo Priming of CD8+ CTL Induced by a Single Topical or Transepithelial Immunization Via the Buccal Mucosa with Measles Virus Nucleoprotein

Etchart¹,

Desmoulins²,

Chemin³

et al. 2001

The Journal of Immunology

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“…Measles and mumps virus nucleocapsids, as visualized by transmission electron microscopy, are flexible rods, approximately 20 nm in diameter, with a hollow central cavity approximately 5 nm in width (3,14,33,54). RNA is tightly bound within the nucleocapsid, which is not believed to dissociate during RNA synthesis.…”

mentioning

confidence: 99%

Characterization of Nucleocapsid Binding by the Measles Virus and Mumps Virus Phosphoproteins

Kingston

Baase

2004

J Virol

100

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We report an analysis of the interaction between the P protein and the RNA-associated N protein (N-RNA) for both measles and mumps viruses with proteins produced in a bacterial expression system. During this study, we verified that the C-terminal tail of the N protein is not required for nucleocapsid formation. For both measles and mumps virus N, truncated proteins encompassing amino acids 1 to 375 assemble into nucleocapsid-like particles within the bacterial cell. For measles virus N, the binding site for the P protein maps to residues 477 to 505 within the tail of the molecule, a sequence relatively conserved among the morbilliviruses. For mumps virus N, a binding site for the P protein maps to the assembly domain of N (residues 1 to 398), while no strong binding of the P protein to the tail of N was detected. These results suggest that the site of attachment for the polymerase varies among the paramyxoviruses. Pulldown experiments demonstrate that the last 50 amino acids of both measles virus and mumps virus P (measles virus P, 457 to 507; mumps virus P, 343 to 391) by themselves constitute the nucleocapsid-binding domain (NBD). Spectroscopic studies show that the NBD is predominantly ␣-helical in both viruses. However, only in measles virus P is the NBD stable and folded, having a lesser degree of tertiary organization in mumps virus P. With isothermal titration calorimetry, we demonstrate that the measles virus P NBD binds to residues 477 to 505 of measles virus N with 1:1 stoichiometry. The dissociation constant (K d ) was determined to be 13 M at 20°C and 35 M at 37°C. Our data are consistent with a model in which an ␣-helical nucleocapsid binding domain, located at the C terminus of P, is responsible for tethering the viral polymerase to its template yet also suggest that, in detail, polymerase binding in morbilliviruses and rubulaviruses differs significantly.

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“…Three remaining structural proteins are associated with the genomic RNA and form a helical ribonucleoprotein (RNP) complex ( Figure 1B). This is the basic unit of infectivity and is 1 µm in length and 18-21 nm in diameter [21]. The nucleocapsid (N) protein is the major component of the RNP, whereas the phospho-(P) and large (L) proteins are present in lower amounts, as illustrated in the schematic representation of the RNP (Figure 1).…”

Section: Molecular Biology Of the Virusmentioning

confidence: 99%

Morbilliviruses and human disease

Rima

Duprex

2005

The Journal of Pathology

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Morbilliviruses are a group of viruses that belong to the family Paramyxoviridae. The most instantly recognizable member is measles virus (MV) and individuals acutely infected with the virus exhibit a wide range of clinical symptoms ranging from a characteristic mild selflimiting infection to death. Canine distemper virus (CDV) and rinderpest virus (RPV) cause a similar but distinctive pathology in dogs and cattle, respectively, and these, alongside experimental MV infection of primates, have been useful models for MV pathogenesis. Traditionally, viruses were identified because a distinctive disease was observed in man or animals; an infectious agent was subsequently isolated, cultured, and this could be used to recapitulate the disease in an experimentally infected host. Thus, satisfying Koch's postulates has been the norm. More recently, particularly due to the advent of exceedingly sensitive molecular biological assays, many researchers have looked for infectious agents in disease conditions for which a viral aetiology has not been previously established. For these cases, the modified Koch's postulates of Bradford Hill have been developed as criteria to link a virus to a specific disease. Only in a few cases have these conditions been fulfilled. Therefore, many viruses have over the years been definitely and tentatively linked to human diseases and in this respect the morbilliviruses are no different. In this review, human diseases associated with morbillivirus infection have been grouped into three broad categories: (1) those which are definitely caused by the infection; (2) those which may be exacerbated or facilitated by an infection; and (3) those which currently have limited, weak, unsubstantiated or no credible scientific evidence to support any link to a morbillivirus. Thus, an attempt has been made to clarify the published data and separate human diseases actually linked to morbilliviruses from those that are merely anecdotally associated.

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The Molecular Length of Measles Virus RNA and the Structural Organization of Measles Nucleocapsids

Cited by 34 publications

References 23 publications

Dendritic Cells Recruitment and In Vivo Priming of CD8+ CTL Induced by a Single Topical or Transepithelial Immunization Via the Buccal Mucosa with Measles Virus Nucleoprotein

Dendritic Cells Recruitment and In Vivo Priming of CD8+ CTL Induced by a Single Topical or Transepithelial Immunization Via the Buccal Mucosa with Measles Virus Nucleoprotein

Characterization of Nucleocapsid Binding by the Measles Virus and Mumps Virus Phosphoproteins

Morbilliviruses and human disease

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