Five Proteins of Laodelphax striatellus Are Potentially Involved in the Interactions between Rice Stripe Virus and Vector

Rice stripe virus (RSV) is the type member of the genus Tenuivirus, which relies on the small brown planthopper (Laodelphax striatellus Fallén) for its transmission in a persistent, circulative-propagative manner. To be transmitted, virus must cross the midgut and salivary glands epithelial barriers...

Full description

Bibliographic Details
Main Authors: Li, Shuo, Xiong, Ruyi, Wang, Xifeng, Zhou, Yijun
Format: Online
Language:English
Published: Public Library of Science 2011
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3197656/
id pubmed-3197656
recordtype oai_dc
spelling pubmed-31976562011-10-25 Five Proteins of Laodelphax striatellus Are Potentially Involved in the Interactions between Rice Stripe Virus and Vector Li, Shuo Xiong, Ruyi Wang, Xifeng Zhou, Yijun Research Article Rice stripe virus (RSV) is the type member of the genus Tenuivirus, which relies on the small brown planthopper (Laodelphax striatellus Fallén) for its transmission in a persistent, circulative-propagative manner. To be transmitted, virus must cross the midgut and salivary glands epithelial barriers in a transcytosis mechanism where vector receptors interact with virions, and as propagative virus, RSV need utilize host components to complete viral propagation in vector cells. At present, these mechanisms remain unknown. In this paper, we screened L. striatellus proteins, separated by two-dimensional electrophoresis (2-DE), as potential RSV binding molecules using a virus overlay assay of protein blots. The results, five L. striatellus proteins that bound to purified RSV particles in vitro were resolved and identified using mass spectrometry. The virus-binding capacities of five proteins were further elucidated in yeast two-hybrid screen (YTHS) and virus-binding experiments of expressed proteins. Among five proteins, the receptor for activated protein kinase C (RACK) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH3) did not interact with RSV nucleocapsid protein (NCP) in YTHS and in far-Western blot, and three ribosomal proteins (RPL5, RPL7a and RPL8) had specific interactions with RSV. In dot immunobinding assay (DIBA), all five proteins were able to bind to RSV particles. The five proteins' potential contributions to the interactions between RSV and L. striatellus were discussed. We proposed that RACK and GAPDH3 might be involved in the epithelial transcytosis of virus particles, and three ribosomal proteins probably played potential crucial roles in the infection and propagation of RSV in vector cells. Public Library of Science 2011-10-20 /pmc/articles/PMC3197656/ /pubmed/22028913 http://dx.doi.org/10.1371/journal.pone.0026585 Text en Li et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Li, Shuo
Xiong, Ruyi
Wang, Xifeng
Zhou, Yijun
spellingShingle Li, Shuo
Xiong, Ruyi
Wang, Xifeng
Zhou, Yijun
Five Proteins of Laodelphax striatellus Are Potentially Involved in the Interactions between Rice Stripe Virus and Vector
author_facet Li, Shuo
Xiong, Ruyi
Wang, Xifeng
Zhou, Yijun
author_sort Li, Shuo
title Five Proteins of Laodelphax striatellus Are Potentially Involved in the Interactions between Rice Stripe Virus and Vector
title_short Five Proteins of Laodelphax striatellus Are Potentially Involved in the Interactions between Rice Stripe Virus and Vector
title_full Five Proteins of Laodelphax striatellus Are Potentially Involved in the Interactions between Rice Stripe Virus and Vector
title_fullStr Five Proteins of Laodelphax striatellus Are Potentially Involved in the Interactions between Rice Stripe Virus and Vector
title_full_unstemmed Five Proteins of Laodelphax striatellus Are Potentially Involved in the Interactions between Rice Stripe Virus and Vector
title_sort five proteins of laodelphax striatellus are potentially involved in the interactions between rice stripe virus and vector
description Rice stripe virus (RSV) is the type member of the genus Tenuivirus, which relies on the small brown planthopper (Laodelphax striatellus Fallén) for its transmission in a persistent, circulative-propagative manner. To be transmitted, virus must cross the midgut and salivary glands epithelial barriers in a transcytosis mechanism where vector receptors interact with virions, and as propagative virus, RSV need utilize host components to complete viral propagation in vector cells. At present, these mechanisms remain unknown. In this paper, we screened L. striatellus proteins, separated by two-dimensional electrophoresis (2-DE), as potential RSV binding molecules using a virus overlay assay of protein blots. The results, five L. striatellus proteins that bound to purified RSV particles in vitro were resolved and identified using mass spectrometry. The virus-binding capacities of five proteins were further elucidated in yeast two-hybrid screen (YTHS) and virus-binding experiments of expressed proteins. Among five proteins, the receptor for activated protein kinase C (RACK) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH3) did not interact with RSV nucleocapsid protein (NCP) in YTHS and in far-Western blot, and three ribosomal proteins (RPL5, RPL7a and RPL8) had specific interactions with RSV. In dot immunobinding assay (DIBA), all five proteins were able to bind to RSV particles. The five proteins' potential contributions to the interactions between RSV and L. striatellus were discussed. We proposed that RACK and GAPDH3 might be involved in the epithelial transcytosis of virus particles, and three ribosomal proteins probably played potential crucial roles in the infection and propagation of RSV in vector cells.
publisher Public Library of Science
publishDate 2011
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3197656/
_version_ 1611482259668336640