ArticleJournal of virology2001
Tomato spotted wilt virus glycoproteins exhibit trafficking and localization signals that are functional in mammalian cells.
Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 66 citations in OpenAlex.
- Research Progress on the Gc Proteins of Akabane Virus.Veterinary sciences · 2025Review
- Structural and Functional Analysis of Groundnut bud necrosis virus (GBNV) Using Computational and Biochemical Approaches.Molecular biotechnology · 2025Article
- Three-dimensional analysis of membrane structures associated with tomato spotted wilt virus infection.Plant, cell & environment · 2023Article
- Article
- Determination of key residues in tospoviral NSm required for Sw-5b recognition, their potential ability to overcome resistance, and the effective resistance provided by improved Sw-5b mutants.Molecular plant pathology · 2022Article
- The Viral Class II Membrane Fusion Machinery: Divergent Evolution from an Ancestral Heterodimer.Viruses · 2021Review
- The Bunyavirales: The Plant-Infecting Counterparts.Viruses · 2021Review
- Crystal structure of tomato spotted wilt virus GProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Changes in the GVirus genes · 2020Article
- Self-association and subcellular localization of Puumala hantavirus envelope proteins.Scientific reports · 2019Article
- Monoclonal antibody-based colloid gold immunochromatographic strip for the rapid detection of Tomato zonate spot tospovirus.Virology journal · 2018Article
- Dissecting the Subcellular Localization, Intracellular Trafficking, Interactions, Membrane Association, and Topology of Citrus Leprosis Virus C Proteins.Frontiers in plant science · 2018Article
- Development of a microarray for simultaneous detection and differentiation of different tospoviruses that are serologically related to Tomato spotted wilt virus.Virology journal · 2017Article
- Intracellular Localization, Interactions and Functions of Capsicum Chlorosis Virus Proteins.Frontiers in microbiology · 2017Article
- Monoclonal antibodies for differentiating infections of three serological-related tospoviruses prevalent in Southwestern China.Virology journal · 2016Article
- Generation of marker-free transgenic plants concurrently resistant to a DNA geminivirus and a RNA tospovirus.Scientific reports · 2014Article
- The cytosolic nucleoprotein of the plant-infecting bunyavirus tomato spotted wilt recruits endoplasmic reticulum-resident proteins to endoplasmic reticulum export sites.The Plant cell · 2013Article
- Molecular characterization of the full-length L and M RNAs of Tomato yellow ring virus, a member of the genus Tospovirus.Virus genes · 2013Article
- Scientific Opinion on the pest categorisation of the tospoviruses.EFSA journal. European Food Safety Authority · 2012Article
- Role of N-linked glycans on bunyamwera virus glycoproteins in intracellular trafficking, protein folding, and virus infectivity.Journal of virology · 2005Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The glycoprotein precursor (G1/G2) gene of tomato spotted wilt virus (TSWV) was expressed in BHK cells using the Semliki Forest virus expression system. The results reveal that in this cell system, the precursor is efficiently cleaved and the resulting G1 and G2 glycoproteins are transported from the endoplasmic reticulum (ER) to the Golgi complex, where they are retained, a process that could be blocked by tunicamycin. Expression of G2 alone resulted in transport to and retention in the Golgi complex, albeit less efficient, suggesting that G2 contains a Golgi retention signal. G1 alone was retained in the ER, irrespective of whether it contained the precursor's signal sequence or its own N-terminal hydrophobic sequence. Coexpression of G1 and G2 from separate gene constructs resulted in rescue of efficient G1 transport, as the proteins coaccumulated in the Golgi complex, indicating that their interaction is essential for proper targeting to this organelle. The results demonstrate that transport and targeting of the plant TSWV glycoproteins in mammalian BHK cells are strikingly similar to those of animal-infecting bunyavirus glycoproteins in mammalian cells. The observations are likely to reflect the dual tropism of TSWV, which replicates both in its plant host and in its animal (thrips) vector.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.