Phosphorylation of Nonmuscle myosin II-A regulatory light chain resists Sendai virus fusion with host cells View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2015-05-20

AUTHORS

Provas Das, Shekhar Saha, Sunandini Chandra, Alakesh Das, Sumit K. Dey, Mahua R. Das, Shamik Sen, Debi P. Sarkar, Siddhartha S. Jana

ABSTRACT

Enveloped viruses enter host cells through membrane fusion and the cells in turn alter their shape to accommodate components of the virus. However, the role of nonmuscle myosin II of the actomyosin complex of host cells in membrane fusion is yet to be understood. Herein, we show that both (-) blebbistatin, a specific inhibitor of nonmuscle myosin II (NMII) and small interfering RNA markedly augment fusion of Sendai virus (SeV), with chinese hamster ovary cells and human hepatocarcinoma cells. Inhibition of RLC phosphorylation using inhibitors against ROCK, but not PKC and MRCK, or overexpression of phospho-dead mutant of RLC enhances membrane fusion. SeV infection increases cellular stiffness and myosin light chain phosphorylation at two hour post infection. Taken together, the present investigation strongly indicates that Rho-ROCK-NMII contractility signaling pathway may provide a physical barrier to host cells against viral fusion. More... »

PAGES

10395

References to SciGraph publications

  • 2008-07-03. Viral membrane fusion in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2011-04-27. Subversion of the actin cytoskeleton during viral infection in NATURE REVIEWS MICROBIOLOGY
  • 2010-09. A mitotic spindle-independent cleavage furrow positioning pathway in NATURE
  • 2005. The Role of the Cytoskeleton During Viral Infection in MEMBRANE TRAFFICKING IN VIRAL REPLICATION
  • 2009-11. Non-muscle myosin II takes centre stage in cell adhesion and migration in NATURE REVIEWS MOLECULAR CELL BIOLOGY
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/srep10395

    DOI

    http://dx.doi.org/10.1038/srep10395

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1035304104

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/25993465


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