Next Article in Journal
A Novel Role for PX, a Structural Protein of Fowl Adenovirus Serotype 4 (FAdV4), as an Apoptosis-Inducer in Leghorn Male Hepatocellular Cell
Previous Article in Journal
Analytical Performance of the RIDASCREEN® Hantavirus Puumala IgG/IgM ELISA Assay
Open AccessArticle

The Major Capsid Protein, VP1, of the Mouse Polyomavirus Stimulates the Activity of Tubulin Acetyltransferase 1 by Microtubule Stabilization

1
Department of Genetics and Microbiology, Faculty of Science, Charles University, BIOCEV, 25250 Vestec, Czech Republic
2
Institute of Biotechnology of the Czech Academy of Sciences, BIOCEV, 25250 Vestec, Czech Republic
3
Faculty of Mathematics and Physics, Charles University, 12844 Prague, Czech Republic
*
Author to whom correspondence should be addressed.
Current address: Paul Langerhans Institute Dresden of the Helmholtz Center Munich at University Hospital and Faculty of Medicine, Technische Universität Dresden, 01307 Dresden, Germany.
Current address: German Center for Diabetes Research (DZD e.V.), 85764 Neuherberg, Germany.
Viruses 2020, 12(2), 227; https://doi.org/10.3390/v12020227
Received: 22 January 2020 / Revised: 12 February 2020 / Accepted: 14 February 2020 / Published: 18 February 2020
(This article belongs to the Section Animal Viruses)
Viruses have evolved mechanisms to manipulate microtubules (MTs) for the efficient realization of their replication programs. Studying the mechanisms of replication of mouse polyomavirus (MPyV), we observed previously that in the late phase of infection, a considerable amount of the main structural protein, VP1, remains in the cytoplasm associated with hyperacetylated microtubules. VP1–microtubule interactions resulted in blocking the cell cycle in the G2/M phase. We are interested in the mechanism leading to microtubule hyperacetylation and stabilization and the roles of tubulin acetyltransferase 1 (αTAT1) and deacetylase histone deacetylase 6 (HDAC6) and VP1 in this mechanism. Therefore, HDAC6 inhibition assays, αTAT1 knock out cell infections, in situ cell fractionation, and confocal and TIRF microscopy were used. The experiments revealed that the direct interaction of isolated microtubules and VP1 results in MT stabilization and a restriction of their dynamics. VP1 leads to an increase in polymerized tubulin in cells, thus favoring αTAT1 activity. The acetylation status of MTs did not affect MPyV infection. However, the stabilization of MTs by VP1 in the late phase of infection may compensate for the previously described cytoskeleton destabilization by MPyV early gene products and is important for the observed inhibition of the G2→M transition of infected cells to prolong the S phase. View Full-Text
Keywords: mouse polyomavirus; VP1; microtubules; α-tubulin acetyltransferase 1; histone deacetylase 6; microtubule acetylation; microtubule stabilization mouse polyomavirus; VP1; microtubules; α-tubulin acetyltransferase 1; histone deacetylase 6; microtubule acetylation; microtubule stabilization
Show Figures

Figure 1

MDPI and ACS Style

Horníková, L.; Bruštíková, K.; Ryabchenko, B.; Zhernov, I.; Fraiberk, M.; Mariničová, Z.; Lánský, Z.; Forstová, J. The Major Capsid Protein, VP1, of the Mouse Polyomavirus Stimulates the Activity of Tubulin Acetyltransferase 1 by Microtubule Stabilization. Viruses 2020, 12, 227.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop