Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mutations in the central domain of potato virus X TGBp2 eliminate granular vesicles and virus cell-to-cell trafficking.

Journal of virology - 1 Feb 2007

Ju Ho-Jong, Brown James E, Ye Chang-Ming, Verchot-Lubicz Jeanmarie

Abstract excerpt

Most RNA viruses remodel the endomembrane network to promote virus replication, maturation, or egress. Rearrangement of cellular membranes is a crucial component of viral pathogenesis. The PVX TGBp2 protein induces vesicles of the granular type to bud from the endoplasmic reticulum network. Green fluorescent protein (GFP) was fused to the PVX TGBp2 coding sequence and inserted into the viral genome and into pRTL2...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Substitution
Share to Locomotion

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Nicotiana

Share to Plant Diseases

Share to Plant Leaves

Share to Potexvirus

Share to Transport Vesicles

Share to Viral Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 17151124
DOI: 10.1128/JVI.02009-06
PMCID: PMC1797549

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutations in the central domain of potato virus X TGBp2 eliminate granular vesicles and virus cell-to-cell trafficking.PMID 17151124Read ↗

The potato virus X TGBp2 protein association with the endoplasmic reticulum plays a role in but is not sufficient for viral cell-to-cell movement.Semantic proximity Read ↗

The hydrophobic segment of Potato virus X TGBp3 is a major determinant of the protein intracellular trafficking.Semantic proximity Read ↗

Formation of protein complexes containing plant virus movement protein TGBp3 is necessary for its intracellular trafficking.Semantic proximity Read ↗

Transient coexpression of individual genes encoded by the triple gene block of potato mop-top virus reveals requirements for TGBp1 trafficking.Semantic proximity Read ↗

Replication and trafficking of a plant virus are coupled at the entrances of plasmodesmata.Semantic proximity Read ↗

Potato virus X TGBp1 induces plasmodesmata gating and moves between cells in several host species whereas CP moves only in N. benthamiana leaves.Semantic proximity Read ↗

Mutation of a chloroplast-targeting signal in Alternanthera mosaic virus TGB3 impairs cell-to-cell movement and eliminates long-distance virus movement.Semantic proximity Read ↗

GLUTELIN PRECURSOR ACCUMULATION3 encodes a regulator of post-Golgi vesicular traffic essential for vacuolar protein sorting in rice endosperm.Semantic proximity Read ↗

The ability of PVX p25 to form RL structures in plant cells is necessary for its function in movement, but not for its suppression of RNA silencing.Semantic proximity Read ↗

Viral protein targeting to the cortical endoplasmic reticulum is required for cell-cell spreading in plants.Semantic proximity Read ↗

Phase separation of both a plant virus movement protein and cellular factors support virus-host interactionsSemantic proximity Read ↗

Subcellular sorting of small membrane-associated triple gene block proteins: TGBp3-assisted targeting of TGBp2.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.