ArticleJournal of virology1993
Possible involvement of microtubule disruption in bipolar budding of a Sendai virus mutant, F1-R, in epithelial MDCK cells.
Article in Journal of virology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 34 citations in OpenAlex.
- Viral journeys on the intracellular highways.Cellular and molecular life sciences : CMLS · 2018Review
- Microtubule Regulation and Function during Virus Infection.Journal of virology · 2017Review
- Paramyxovirus assembly and budding: building particles that transmit infections.The international journal of biochemistry & cell biology · 2010Review
- An S101P substitution in the putative cleavage motif of the human metapneumovirus fusion protein is a major determinant for trypsin-independent growth in vero cells and does not alter tissue tropism in hamsters.Journal of virology · 2005Article
- Mutations in Sendai virus variant F1-R that correlate with plaque formation in the absence of trypsin.Medical microbiology and immunology · 2005Article
- Assembly and budding of influenza virus.Virus research · 2004Review
- Rotavirus spike protein VP4 is present at the plasma membrane and is associated with microtubules in infected cells.Journal of virology · 2000Article
- Measles virus-induced disruption of the glial-fibrillary-acidic protein cytoskeleton in an astrocytoma cell line (U-251).Journal of virology · 2000Article
- Polarized budding of measles virus is not determined by viral surface glycoproteins.Journal of virology · 1998Article
- Host cell dependence of viral morphology.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Role of actin microfilaments in Black Creek Canal virus morphogenesis.Journal of virology · 1998Article
- Association of influenza virus NP and M1 proteins with cellular cytoskeletal elements in influenza virus-infected cells.Journal of virology · 1997Article
- Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells.Journal of virology · 1996Article
- Involvement of the mutated M protein in altered budding polarity of a pantropic mutant, F1-R, of Sendai virus.Journal of virology · 1996Article
- Differential antigen burden modulates the gamma interferon but not the immunoglobulin response in mice that vary in susceptibility to Sendai virus pneumonia.Journal of virology · 1995Article
- Matrix and laminin synthesis in MDCK cells in vitro.In vitro cellular & developmental biology. Animal · 1994Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Envelope glycoproteins F and HN of wild-type Sendai virus are transported to the apical plasma membrane domain of polarized epithelial MDCK cells, where budding of progeny virus occurs. On the other hand, a pantropic mutant, F1-R, buds bipolarly at both the apical and basolateral domains, and the viral glycoproteins have also been shown to be transported to both of these domains (M. Tashiro, M. Yamakawa, K. Tobita, H.-D. Klenk, R. Rott, and J.T. Seto, J. Virol. 64:4672-4677, 1990). MDCK cells were infected with wild-type virus and treated with the microtubule-depolymerizing drugs colchicine and nocodazole. Budding of the virus and surface expression of the glycoproteins were found to occur in a nonpolarized fashion similar to that found in cells infected with F1-R. In uninfected cells, the drugs were shown to interfere with apical transport of a secretory cellular glycoprotein, gp80, and basolateral uptake of [35S]methionine as well as to disrupt microtubule structure, indicating that cellular polarity of MDCK cells depends on the presence of intact microtubules. Infection by the F1-R mutant partially affected the transport of gp80, uptake of [35S]methionine, and the microtubule network, whereas wild-type virus had a marginal effect. These results suggest that apical transport of the glycoproteins of wild-type Sendai virus in MDCK cells depends on intact microtubules and that bipolar budding by F1-R is possibly due, at least in part, to the disruption of microtubules. Nucleotide sequence analyses of the viral genes suggest that the mutated M protein of F1-R might be involved in the alteration of microtubules.
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