2017
DOI: 10.1128/jvi.00825-17
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Structural Insight into Nucleoprotein Conformation Change Chaperoned by VP35 Peptide in Marburg Virus

Abstract: Marburg virus (MARV) encodes a nucleoprotein (NP) to encapsidate its genome by oligomerization and form a ribonucleoprotein complex (RNP). According to previous investigation on nonsegmented negative-sense RNA viruses (nsNSV), the newly synthesized NPs must be prevented from indiscriminately binding to noncognate RNAs. During the viral RNA synthesis process, the RNPs undergo a transition from an RNA-bound form to a template-free form, to open access for the interaction between the viral polymerase and the RNA … Show more

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Cited by 31 publications
(39 citation statements)
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“…These patches are buried in the NP oligomer. In non-physiological packing within the crystallographic unit cells of filovirus NP, α17 and α18 of adjacent NPs also make contacts in almost identical configurations 8,19 (Extended Data Fig. 5f), which emphasizes the high specificity of these helix-helix interactions.…”
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confidence: 92%
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“…These patches are buried in the NP oligomer. In non-physiological packing within the crystallographic unit cells of filovirus NP, α17 and α18 of adjacent NPs also make contacts in almost identical configurations 8,19 (Extended Data Fig. 5f), which emphasizes the high specificity of these helix-helix interactions.…”
mentioning
confidence: 92%
“…Therefore, this region not only aligns the RNA but also serves as an interface for NP-RNA interactions. Positively charged residues K160, K171, R174, R298 and R401-some of which are important for RNA binding in filovirus NP 8,19 -were found in close proximity to RNA nucleotides, with their side chains pointing towards RNA-backbone phosphates (Fig. 2c).…”
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confidence: 99%
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“…A previous study from Marburg virus NP revealed that specific motion within the NP prevents indiscriminate binding of non‐cognate RNA molecules which precedes ribonucleoprotein complex formation. Subsequently, ribonucleoprotein complex must also undergo structural transition to form RNA‐free template (Liu et al., ). Residues 8–24, 83–122, and 261–340 essentially form the head region (Figure , i–iv, red cartoon) of Lassa NP, while residues 25–82 and 123–260 (Figure a, i–iv , green cartoon) form the body region.…”
Section: Resultsmentioning
confidence: 99%
“…A previous study from Marburg virus NP revealed that specific motion within the NP prevents indiscriminate binding of non-cognate RNA molecules which precedes ribonucleoprotein complex formation. Subsequently, ribonucleoprotein complex must also undergo structural transition to form RNA-free template (Liu et al, 2017). simulated over 500 ns is presented (Figure 4b, i-iv, the figures are diagonally symmetric).…”
Section: T-705 Substitution Alters the Essential Dynamic Motion Of mentioning
confidence: 99%