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

Three YXXL Sequences of a Bovine Leukemia Virus Transmembrane Protein are Independently Required for Fusion Activity by Controlling Expression on the Cell Membrane.

Viruses - 10 Dec 2019

Matsuura Ryosuke, Inabe Kazunori, Otsuki Hiroyuki, Kurokawa Kazuo, Dohmae Naoshi, Aida Yoko

Abstract excerpt

Bovine leukemia virus (BLV), which is closely related to human T-cell leukemia viruses, is the causative agent of enzootic bovine leukosis, the most common neoplastic disease of cattle. The transmembrane subunit of the BLV envelope glycoprotein, gp30, contains three completely conserved YXXL sequences that fit an endocytic sorting motif. The two N-terminal YXXL sequences are reportedly critical for viral...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Fluorescent Antibody Technique

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Host-Pathogen Interactions

Share to Leukemia Virus, Bovine

Share to Membrane Fusion

Share to Viral Envelope Proteins

Share to Virus Attachment

Share to Virus Release

Source

Open in PubMed Open full text

Identifiers

PMID: 31835517
DOI: 10.3390/v11121140
PMCID: PMC6950344

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

Three YXXL Sequences of a Bovine Leukemia Virus Transmembrane Protein are Independently Required for Fusion Activity by Controlling Expression on the Cell Membrane.PMID 31835517Read ↗

Identification and characterization of common B cell epitope in bovine leukemia virus via high-throughput peptide screening system in infected cattle.Semantic proximity Read ↗

Mutation of a Single Envelope N-Linked Glycosylation Site Enhances the Pathogenicity of Bovine Leukemia Virus.Semantic proximity Read ↗

The Cytoplasmic Tail Domain of Epstein-Barr Virus gH Regulates Membrane Fusion Activity through Altering gH Binding to gp42 and Epithelial Cell Attachment.Semantic proximity Read ↗

The Epstein-Barr virus (EBV) glycoprotein B cytoplasmic C-terminal tail domain regulates the energy requirement for EBV-induced membrane fusion.Semantic proximity Read ↗

Natural genetic variations in bovine leukemia virus envelope gene: possible effects of selection and escape.Semantic proximity Read ↗

Role of the proline-rich motif of bovine leukemia virus transmembrane protein gp30 in viral load and pathogenicity in sheep.Semantic proximity Read ↗

Functional interaction between the N- and C-terminal domains of murine leukemia virus surface envelope protein.Semantic proximity Read ↗

Characterization of R peptide of murine leukemia virus envelope glycoproteins in syncytium formation and entry.Semantic proximity Read ↗

Genetic analysis of the pX region of bovine leukemia virus genotype 1 in Holstein Friesian cattle with different stages of infection.Semantic proximity Read ↗

Conservative mutations in the immunosuppressive region of the bovine leukemia virus transmembrane protein affect fusion but not infectivity in vivo.Semantic proximity Read ↗

Mutagenesis of tyrosine and di-leucine motifs in the HIV-1 envelope cytoplasmic domain results in a loss of Env-mediated fusion and infectivitySemantic proximity Read ↗

Epstein-Barr Virus Fusion with Epithelial Cells Triggered by gB Is Restricted by a gL Glycosylation Site.Semantic proximity Read ↗

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