scholarly journals Hijack it, change it: how do plant viruses utilize the host secretory pathway for efficient viral replication and spread?

2013 ◽  
Vol 3 ◽  
Author(s):  
Camilo Patarroyo ◽  
Jean-François Laliberté ◽  
Huanquan Zheng
Keyword(s):  
Viral Replication ◽  
Secretory Pathway ◽  
Plant Viruses ◽  
Efficient Viral Replication

scholarly journals Prolonged activation of NF-κB by human cytomegalovirus promotes efficient viral replication and late gene expression

Virology ◽  
2006 ◽  
Vol 346 (1) ◽  
pp. 15-31 ◽  
Author(s):  
Ian B. DeMeritt ◽  
Jagat P. Podduturi ◽  
A. Michael Tilley ◽  
Maciej T. Nogalski ◽  
Andrew D. Yurochko
Keyword(s):  
Gene Expression ◽  
Viral Replication ◽  
Human Cytomegalovirus ◽  
Late Gene ◽  
Late Gene Expression ◽  
Efficient Viral Replication

Annexin A2 associates to feline calicivirus RNA in the replication complexes from infected cells and participates in an efficient viral replication

2019 ◽  
Vol 261 ◽  
pp. 1-8 ◽  
Author(s):  
Juan Carlos Santos-Valencia ◽  
Clotilde Cancio-Lonches ◽  
Adrian Trujillo-Uscanga ◽  
Beatriz Alvarado-Hernández ◽  
Anel Lagunes-Guillén ◽  
...  
Keyword(s):  
Viral Replication ◽  
Annexin A2 ◽  
Feline Calicivirus ◽  
Infected Cells ◽  
Efficient Viral Replication

scholarly journals Late activation of theRaf/MEK/ERKpathway is required for translocation of the respiratory syncytial virusFprotein to the plasma membrane and efficient viral replication

2018 ◽  
Vol 21 (1) ◽  
pp. e12955 ◽  
Author(s):  
Hannah F. Preugschas ◽  
Eike R. Hrincius ◽  
Carolin Mewis ◽  
Giao V.Q. Tran ◽  
Stephan Ludwig ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Viral Replication ◽  
Efficient Viral Replication

scholarly journals Baculovirus Infection Induces a DNA Damage Response That Is Required for Efficient Viral Replication

2011 ◽  
Vol 85 (23) ◽  
pp. 12547-12556 ◽  
Author(s):  
N. Huang ◽  
W. Wu ◽  
K. Yang ◽  
A. L. Passarelli ◽  
G. F. Rohrmann ◽  
...  
Keyword(s):  
Dna Damage ◽  
Viral Replication ◽  
Dna Damage Response ◽  
Baculovirus Infection ◽  
Damage Response ◽  
Efficient Viral Replication

scholarly journals Aquareovirus NS80 Initiates Efficient Viral Replication by Retaining Core Proteins within Replication-Associated Viral Inclusion Bodies

PLoS ONE ◽  
2015 ◽  
Vol 10 (5) ◽  
pp. e0126127 ◽  
Author(s):  
Liming Yan ◽  
Jie Zhang ◽  
Hong Guo ◽  
Shicui Yan ◽  
Qingxiu Chen ◽  
...  
Keyword(s):  
Viral Replication ◽  
Inclusion Bodies ◽  
Core Proteins ◽  
Viral Inclusion ◽  
Efficient Viral Replication

scholarly journals Transcription elongation regulator 1 (TCERG1) regulates competent RNA polymerase II-mediated elongation of HIV-1 transcription and facilitates efficient viral replication

Retrovirology ◽  
2013 ◽  
Vol 10 (1) ◽  
pp. 124 ◽  
Author(s):  
Mayte Coiras ◽  
Marta Montes ◽  
Immaculada Montanuy ◽  
María López-Huertas ◽  
Elena Mateos ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Viral Replication ◽  
Rna Polymerase Ii ◽  
Transcription Elongation ◽  
Hiv 1 ◽  
Efficient Viral Replication

scholarly journals Inclusion Body Fusion of Human Parainfluenza Virus Type 3 Regulated by Acetylated α-Tubulin Enhances Viral Replication

2016 ◽  
Vol 91 (3) ◽  
Author(s):  
Shengwei Zhang ◽  
Yanliang Jiang ◽  
Qi Cheng ◽  
Yi Zhong ◽  
Yali Qin ◽  
...  
Keyword(s):  
Viral Replication ◽  
Virus Type ◽  
Inclusion Bodies ◽  
Viral Proteins ◽  
Cellular Proteins ◽  
Parainfluenza Virus ◽  
Syncytial Virus ◽  
Human Parainfluenza Virus ◽  
Type 3 ◽  
Efficient Viral Replication

ABSTRACT Viral inclusion bodies (IBs), or replication factories, are unique structures generated by viral proteins together with some cellular proteins as a platform for efficient viral replication, but little is known about the mechanism underlying IB formation and fusion. Our previous study demonstrated that the interaction between the nucleoprotein (N) and phosphoprotein (P) of human parainfluenza virus type 3 (HPIV3), an enveloped virus with great medical impact, can form IBs. In this study, we found that small IBs can fuse with each other to form large IBs that enhance viral replication. Furthermore, we found that acetylated α-tubulin interacts with the N-P complex and colocalizes with IBs of HPIV3 but does not interact with the N-P complex of human respiratory syncytial virus or vesicular stomatitis virus and does not colocalize with IBs of human respiratory syncytial virus. Most importantly, enhancement of α-tubulin acetylation using the pharmacological inhibitor trichostatin A (TSA), RNA interference (RNAi) knockdown of the deacetylase enzymes histone deacetylase 6 (HDAC6) and sirtuin 2 (SIRT2), or expression of α-tubulin acetyltransferase 1 (α-TAT1) resulted in the fusion of small IBs into large IBs and effective viral replication. In contrast, suppression of acetylation of α-tubulin by overexpressing HDAC6 and SIRT2 profoundly inhibited the fusion of small IBs and viral replication. Our findings offer previously unidentified mechanistic insights into the regulation of viral IB fusion by acetylated α-tubulin, which is critical for viral replication. IMPORTANCE Inclusion bodies (IBs) are unique structures generated by viral proteins and some cellular proteins as a platform for efficient viral replication. Human parainfluenza virus type 3 (HPIV3) is a nonsegmented single-stranded RNA virus that mainly causes lower respiratory tract disease in infants and young children. However, no vaccines or antiviral drugs for HPIV3 are available. Therefore, understanding virus-host interactions and developing new antiviral strategies are increasingly important. Acetylation on lysine (K) 40 of α-tubulin is an evolutionarily conserved modification and plays an important role in many cellular processes, but its role in viral IB dynamics has not been fully explored. To our knowledge, our findings are the first to show that acetylated α-tubulin enhances viral replication by regulating HPIV3 IB fusion.

scholarly journals The Intra- and Intercellular Movement of Melon necrotic spot virus (MNSV) Depends on an Active Secretory Pathway

2010 ◽  
Vol 23 (3) ◽  
pp. 263-272 ◽  
Author(s):  
Ainhoa Genovés ◽  
Jose Antonio Navarro ◽  
Vicente Pallás
Keyword(s):  
Intracellular Transport ◽  
Secretory Pathway ◽  
Fluorescent Proteins ◽  
Plant Viruses ◽  
Cell Periphery ◽  
Dependent Manner ◽  
Necrotic Spot ◽  
Spot Virus ◽  
Melon Necrotic Spot Virus ◽  
Viral Movement Protein

Plant viruses hijack endogenous host transport machinery to aid their intracellular spread. Here, we study the localization of the p7B, the membrane-associated viral movement protein (MP) of the Melon necrotic spot virus (MNSV), and also the potential involvement of the secretory pathway on the p7B targeting and intra- and intercellular virus movements. p7B fused to fluorescent proteins was located throughout the endoplasmic reticulum (ER) at motile Golgi apparatus (GA) stacks that actively tracked the actin microfilaments, and at the plasmodesmata (PD). Hence, the secretory pathway inhibitor, Brefeldin A (BFA), and the overexpression of the GTPase-defective mutant of Sar1p, Sar1[H74L], fully retained the p7B within the ER, revealing that the protein is delivered to PD in a BFA-sensitive and COPII-dependent manner. Disruption of the actin cytoskeleton with latrunculin B led to the accumulation of p7B in the ER, which strongly suggests that p7B is also targeted to the cell periphery in an actin-dependent manner. Remarkably, the local spread of the viral infection was significantly restricted either with the presence of BFA or under the overexpression of Sar1[H74L], thus revealing the involvement of an active secretory pathway in the intracellular movement of MNSV. Overall, these findings support a novel route for the intracellular transport of a plant virus led by the GA.

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