Comparison of the three large polymerase proteins of influenza A, B, and C viruses
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Comparison of antiviral resistance across acute and chronic viral infections
2018, Antiviral ResearchCitation Excerpt :Of the surface proteins, F is the most conserved with a sequence homology of 91% between RSV A and B viruses reported (Collins and Karron, 2013; Johnson and Collins, 1988). In contrast, two of the three Influenza RNA polymerase subunits, PB1 (the most conserved protein for influenza strains (Yamashita et al., 1989)) and PB2 from Influenza A and B share only 61% and 39% homology (Kemdirim et al., 1986; Schreier et al., 1988), respectively. Additionally, unlike influenza, the RSV strains responsible for seasonal outbreaks are fairly stable from season to season and one of the genotype(s) can circulate for extended periods (Tan et al., 2012; Zheng et al., 2016; Zou et al., 2016).
Synthesis and biological evaluation of a library of hybrid derivatives as inhibitors of influenza virus PA-PB1 interaction
2018, European Journal of Medicinal ChemistryCitation Excerpt :In fact, PPIs represent crucial events in many biological processes under both physiological and pathological conditions. In particular, crystallization studies have revealed that PA-PB1 interaction may be a very promising druggable target [29,49–52], because of the high degree of conservation of several interface residues among FluA, FluB and FluC [27,53,54], that suggests that its inhibitors may be active against many viral subtypes and less prone to drug-resistance, and because of the little size of the specific interface that allows small with ELISA evaluation revealed the 3-cyano-4,6-diphenyl-pyridine scaffold as a promising potential inhibitor of the PA−PB1 complex by mimicking the hydrophilic N-terminal portion of PB1 (residues 1–4) and the most important interactions with the C-terminal domain of PA. Compounds 3 and 4 (Fig. 1), showed the best activity profile [63].
Exploring the cycloheptathiophene-3-carboxamide scaffold to disrupt the interactions of the influenza polymerase subunits and obtain potent anti-influenza activity
2017, European Journal of Medicinal ChemistryCitation Excerpt :Indeed, RdRp is essential for virus transcription, replication, and evolution. Moreover, its structure is highly conserved among the different flu A, B, and C strains [3–6]. RdRp is a heterotrimeric complex composed of polymerase acidic protein (PA), polymerase basic protein 1 (PB1), and polymerase basic protein 2 (PB2) subunits that work together in a tightly associated and coupled fashion [7].
Nucleoprotein of influenza B virus binds to its type A counterpart and disrupts influenza A viral polymerase complex formation
2014, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Besides self oligomerization, NP directly interacts with PB1 and PB2 subunits of the polymerase complex, as evident from recent cryogenic electron microscopic reconstructions [2,3] and co-immunoprecipitation experiments performed on infected cell lysates [8]. Except for the additional 70 amino acids at the N-terminus of FluB’s nucleoprotein recently demonstrated to contain a nuclear localization signal (NLS) [9], all protein subunits involved in vRNP formation of FluA and FluB share significant homology, and it is assumed, based on extensive research on FluA, that the vRNP of FluB also assembles and functions in a similar manner [10–12]. Although FluA and FluB co-circulate and share close phylogenic relationship, they have not produced any natural or synthetic reassortant to date [13–16].
PA subunit of RNA polymerase as a promising target for anti-influenza virus agents
2008, Antiviral ResearchIdentification of N- and C-3-Modified Laudanosoline Derivatives as Novel Influenza PA<inf>N</inf>Endonuclease Inhibitors
2023, Journal of Medicinal Chemistry
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Visiting research scientist from Bioscience Research Laboratories, Sankyo Co. Ltd., 1-2-58, Hiromachi, Shinagawa-ku, Tokyo, Japan.