“…FuzDrop indicated that the L-protein has a low pLLPS value of 0.11860 and does not contain any DPRs. However, this protein possesses 24 In addition to be involved in interaction with the RABV L-and N-proteins and the viral ribonucleocapsids, the P-protein is known to bind to the multitude of host proteins, such as dynein light chain 1 and 2 (DYNLL1 (UniProt ID: P63167) and DYNLL2 (UniProt ID: Q96FJ2), respectively) [129], as well as host signal transducer and activator of transcription 1-alpha/beta and signal transducer and activator of transcription 2 (STAT1 (Uni-Prot ID: P42224) and STAT2 proteins (UniProt ID: P52630), respectively) [16,17,[100][101][102][103], promyelocytic leukemia (PML) protein (UniProt ID: P29590) [109], the ribosomal protein L9 (UniProt ID: Q02878) [15], STAT3 (UniProt ID: P40763), nucleolin (NCL; UniProt ID: P19338), focal adhesion kinase (FAK; UniProt ID: Q05397), Janus kinase 1 (JAK1; UniProt ID: P23458), inhibitor of nuclear factor kappa-B kinase subunit epsilon (IKKε; UniProt ID: Q14164), Beclin-1 (BECN1; UniProt ID: Q14457), tubulin alpha (TUB-α; UniProt ID: Q71U36 for tubulin alpha-1A chain), tubulin beta (TUB-β; UniProt ID: Q9H4B7 for tubulin beta-1 chain), ATP-binding cassette sub-family E member 1 (ABCE1; UniProt ID: P61221), T-complex protein 1 subunit gamma (CCTγ; UniProt ID: P49368), Hsp90 co-chaperone Cdc37 (CDC37; UniProt ID: Q16543), and heat shock protein HSP 90-alpha (Hsp90AA1; UniProt ID: P07900) [71]. Furthermore, P-protein can interact with the complex I in mitochondria leading to mitochondrial dysfunction, increased generation of reactive oxygen species (ROS), and oxidative stress [130].…”