Association of the Tobacco mosaic virus 126kDa replication protein with a GDI protein affects host susceptibility

An interaction between the Tobacco mosaic virus (TMV) 126kDa replication protein and a host-encoded Rab GDP dissociation inhibitor (GDI2) was identified and investigated for its role in infection. GDI proteins are essential components of vesicle trafficking pathways. TMV infection alters the localiz...

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Published inVirology (New York, N.Y.) Vol. 414; no. 2; pp. 110 - 118
Main Authors Kramer, Sabrina R., Goregaoker, Sameer P., Culver, James N.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 05.06.2011
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Abstract An interaction between the Tobacco mosaic virus (TMV) 126kDa replication protein and a host-encoded Rab GDP dissociation inhibitor (GDI2) was identified and investigated for its role in infection. GDI proteins are essential components of vesicle trafficking pathways. TMV infection alters the localization of GDI2 from the cytoplasm to ER-associated complexes. Partial silencing of GDI2 results in significant increases in the number of TMV infection foci observed in inoculated tissues. However, GDI2 silencing does not affect TMV accumulation at the infection site, cell-to-cell movement, or susceptibility of the host to mechanical inoculation. Furthermore, increases in the number of successful infection foci were specific to TMV and correlated with the appearance of vesicle-like rearrangements in the vacuolar membrane. Tissue infiltrations with brefeldin A, an inhibitor of vesicle trafficking, also enhanced host susceptibility to TMV. Combined these findings suggest that the 126kDa–GDI2 interaction alters vesicle trafficking to enhance the establishment of an infection.
AbstractList An interaction between the Tobacco mosaic virus (TMV) 126kDa replication protein and a host-encoded Rab GDP dissociation inhibitor (GDI2) was identified and investigated for its role in infection. GDI proteins are essential components of vesicle trafficking pathways. TMV infection alters the localization of GDI2 from the cytoplasm to ER-associated complexes. Partial silencing of GDI2 results in significant increases in the number of TMV infection foci observed in inoculated tissues. However, GDI2 silencing does not affect TMV accumulation at the infection site, cell-to-cell movement, or susceptibility of the host to mechanical inoculation. Furthermore, increases in the number of successful infection foci were specific to TMV and correlated with the appearance of vesicle-like rearrangements in the vacuolar membrane. Tissue infiltrations with brefeldin A, an inhibitor of vesicle trafficking, also enhanced host susceptibility to TMV. Combined these findings suggest that the 126kDa-GDI2 interaction alters vesicle trafficking to enhance the establishment of an infection.
Author Goregaoker, Sameer P.
Culver, James N.
Kramer, Sabrina R.
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  givenname: Sabrina R.
  surname: Kramer
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  surname: Culver
  fullname: Culver, James N.
  email: jculver@umd.edu
  organization: Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, MD 20742, USA
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Issue 2
Keywords Virus replication complex
Susceptibility
Vesicle trafficking
Language English
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Snippet An interaction between the Tobacco mosaic virus (TMV) 126kDa replication protein and a host-encoded Rab GDP dissociation inhibitor (GDI2) was identified and...
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SubjectTerms Guanine Nucleotide Dissociation Inhibitors - genetics
Guanine Nucleotide Dissociation Inhibitors - metabolism
Host Specificity
Nicotiana - genetics
Nicotiana - metabolism
Nicotiana - virology
Plant Diseases - genetics
Plant Diseases - virology
Plant Proteins - genetics
Plant Proteins - metabolism
Protein Binding
RNA-Dependent RNA Polymerase - genetics
RNA-Dependent RNA Polymerase - metabolism
Susceptibility
Tobacco Mosaic Virus - enzymology
Tobacco Mosaic Virus - genetics
Tobacco Mosaic Virus - physiology
Vesicle trafficking
Viral Proteins - genetics
Viral Proteins - metabolism
Virus Replication
Virus replication complex
Title Association of the Tobacco mosaic virus 126kDa replication protein with a GDI protein affects host susceptibility
URI https://dx.doi.org/10.1016/j.virol.2010.12.030
https://www.ncbi.nlm.nih.gov/pubmed/21492894
https://search.proquest.com/docview/867324558
Volume 414
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