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

Differential binding efficiency between the envelope protein of Japanese encephalitis virus variants and heparan sulfate on the cell surface.

Journal of medical virology - 1 Apr 2004

Liu Hsiuan, Chiou Shyan-Song, Chen Wei-June

Abstract excerpt

Japanese encephalitis (JE) virus infects a number of host cells, either mosquitoes or vertebrates, in nature. The viral envelope (E) protein is known to interact with molecule(s) on the cell membrane during the early stage of virus infection. In this study, two sets of virus variants including T1P1-L4/T1P1-S1 and CJN-L1/CJN-S1 derived from two strains (T1P1 and CJN) of the JE virus were used to evaluate the...

Read the complete abstract on PubMed

Topics

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

Share to CHO Cells
Share to Cricetinae
Share to Encephalitis Virus, Japanese

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Heparitin Sulfate

Share to Membrane Glycoproteins

Share to Receptors, Virus

Share to Viral Envelope Proteins

Share to Viral Plaque Assay

Source

Identifiers

PMID: 14981764
DOI: 10.1002/jmv.20025

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

Differential binding efficiency between the envelope protein of Japanese encephalitis virus variants and heparan sulfate on the cell surface.PMID 14981764Read ↗

Role of heparan sulfate for attachment and entry of tick-borne encephalitis virus.Semantic proximity Read ↗

Interaction of E2 glycoprotein with heparan sulfate is crucial for cellular infection of Sindbis virus.Semantic proximity Read ↗

The mutation of Japanese encephalitis virus envelope protein residue 389 attenuates viral neuroinvasiveness.Semantic proximity Read ↗

Pteropine orthoreoviruses use cell surface heparan sulphate as an attachment receptorSemantic proximity Read ↗

Role of N-linked glycosylation for sindbis virus infection and replication in vertebrate and invertebrate systems.Semantic proximity Read ↗

Genome-Wide Screening Uncovers the Significance of N-Sulfation of Heparan Sulfate as a Host Cell Factor for Chikungunya Virus InfectionSemantic proximity Read ↗

Adaptation of tick-borne encephalitis virus to BHK-21 cells results in the formation of multiple heparan sulfate binding sites in the envelope protein and attenuation in vivo.Semantic proximity Read ↗

Three positively charged binding sites on the eastern equine encephalitis virus E2 glycoprotein coordinate heparan sulfate- and protein receptor-dependent infectionSemantic proximity Read ↗

Herpes simplex virus types 1 and 2 differ in their interaction with heparan sulfate.Semantic proximity Read ↗

Fitness of Japanese encephalitis virus to Neuro‐2a cells is determined by interactions of the viral envelope protein with highly sulfated glycosaminoglycans on the cell surfaceSemantic proximity Read ↗

Heparan sulfate binding can contribute to the neurovirulence of neuroadapted and nonneuroadapted Sindbis viruses.Semantic proximity Read ↗

VP1 residues around the five-fold axis of enterovirus A71 mediate heparan sulfate interaction.Semantic proximity Read ↗

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