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

Attenuation of Sindbis virus variants incorporating uncleaved PE2 glycoprotein is correlated with attachment to cell-surface heparan sulfate.

Virology - 25 Apr 2004

Ryman Kate D, Klimstra William B, Johnston Robert E

Abstract excerpt

Sindbis virus virions incorporating uncleaved precursor envelope protein PE2 bind efficiently to cell-surface heparan sulfate (HS) because the furin cleavage site (a consensus HS-binding domain) is retained in the mature virus particle. However, they are essentially nonviable. Resuscitating mutations selected in the E3 or E2 protein preserve the PE2 noncleaving phenotype and HS binding, but facilitate fusion, and...

Read the complete abstract on PubMed

Topics

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

Share to Alphavirus Infections
Share to Animals, Newborn

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Heparan Sulfate Proteoglycans

Share to Membrane Glycoproteins

Share to Protein Precursors

Share to Sindbis Virus

Share to Viral Envelope Proteins

Share to Viral Proteins

Source

Identifiers

PMID: 15063111
DOI: 10.1016/j.virol.2004.01.003

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Attenuation of Sindbis virus variants incorporating uncleaved PE2 glycoprotein is correlated with attachment to cell-surface heparan sulfate.PMID 15063111Read ↗

Natural isolate and recombinant SARS-CoV-2 rapidly evolve in vitro to higher infectivity through more efficient binding to heparan sulfate and reduced S1/S2 cleavageSemantic proximity Read ↗

Lethality of PE2 incorporation into Sindbis virus can be suppressed by second-site mutations in E3 and E2.Semantic proximity Read ↗

Mutations in the E2 glycoprotein of Venezuelan equine encephalitis virus confer heparan sulfate interaction, low morbidity, and rapid clearance from blood of mice.Semantic proximity Read ↗

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

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

Mutating conserved cysteines in the alphavirus e2 glycoprotein causes virus-specific assembly defects.Semantic proximity Read ↗

Informed mutation of western equine encephalitis virus to heparan sulfate binding: Implications for rational design of alphavirus live attenuated vaccines.Semantic proximity Read ↗

Sindbis virus attachment: isolation and characterization of mutants with impaired binding to vertebrate cellsSemantic proximity Read ↗

Molecular Links between the E2 Envelope Glycoprotein and Nucleocapsid Core in Sindbis VirusSemantic proximity Read ↗

Mutation of the dengue virus type 2 envelope protein heparan sulfate binding sites or the domain III lateral ridge blocks replication in Vero cells prior to membrane fusionSemantic proximity Read ↗

The S2 Gene of Equine Infectious Anemia Virus Is a Highly Conserved Determinant of Viral Replication and Virulence Properties in Experimentally Infected PoniesSemantic proximity Read ↗

Attenuated Mutants of Venezuelan Equine Encephalitis Virus Containing Lethal Mutations in the PE2 Cleavage Signal Combined with a Second-Site Suppressor Mutation in E1Semantic proximity Read ↗

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