Identification of Critical Molecular Determinants of West Nile Virus PrM Protein: A Potential Site for Antiviral Targeting

Tan, Ting; Bhuvanakantham, Raghavan; Li, J.; Howe, J.; Ng, Mah Lee

doi:10.1016/j.ijid.2008.05.788

Cited by 1 publication

(1 citation statement)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Several residues within the prM protein have been shown to be key in the heterodimerization of prM with E protein after translation. These studies demonstrated that a tyrosine residue at position 78 in WNV ( Tan et al, 2008 ), a histidine residue at position 99 in JEV ( Lin and Wu, 2005 ), and a histidine residue at position 130 in DENV2 ( Pryor et al, 2004 ) were all paramount in the formation and stability of prM-E heterodimers as well as efficient viral assembly. Another study reported that mutations at residues 120, 123 and 127 in DENV2 prM resulted in reduced viral titers via plaque assay and reduced virus assembly efficiency via ELISA analysis ( Hsieh et al, 2011 ).…”

Section: Flavivirus Structural Proteins: Structure and Functionmentioning

confidence: 99%

Structure-guided paradigm shifts in flavivirus assembly and maturation mechanisms

Nicholls

Sevvana

Kühn

2020

Advances in Virus Research

View full text Add to dashboard Cite

The flavivirus genus encompasses more than 75 unique viruses, including dengue virus which accounts for almost 390 million global infections annually. Flavivirus infection can result in a myriad of symptoms ranging from mild rash and flu-like symptoms, to severe encephalitis and even hemorrhagic fever. Efforts to combat the impact of these viruses have been hindered due to limited antiviral drug and vaccine development. However, the advancement of knowledge in the structural biology of flaviviruses over the last 25 years has produced unique perspectives for the identification of potential therapeutic targets. With particular emphasis on the assembly and maturation stages of the flavivirus life cycle, it is the goal of this review to comparatively analyze the structural similarities between flaviviruses to provide avenues for new research and innovation.

show abstract