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

The viral chemokine MCK-2 of murine cytomegalovirus promotes infection as part of a gH/gL/MCK-2 complex.

PLoS pathogens - 1 Jan 2013

Wagner Felicia M, Brizic Ilija, Prager Adrian, Trsan Tihana, Arapovic Maja, Lemmermann Niels A W, Podlech Jürgen, Reddehase Matthias J, Lemnitzer Frederic, Bosse Jens Bernhard, Gimpfl Martina, Marcinowski Lisa, MacDonald Margaret, Adler Heiko, Koszinowski Ulrich H, Adler Barbara

Abstract excerpt

Human cytomegalovirus (HCMV) forms two gH/gL glycoprotein complexes, gH/gL/gO and gH/gL/pUL(128,130,131A), which determine the tropism, the entry pathways and the mode of spread of the virus. For murine cytomegalovirus (MCMV), which serves as a model for HCMV, a gH/gL/gO complex functionally homologous to the HCMV gH/gL/gO complex has been described. Knock-out of MCMV gO does impair, but not abolish, virus spread...

Read the complete abstract on PubMed

Topics

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

Share to Chemokines, CC
Share to Herpesviridae Infections

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

Share to Macrophages, Peritoneal

Share to Muromegalovirus

Share to Specific Pathogen-Free Organisms

Share to Viral Envelope Proteins

Share to Virion

Share to Virus Internalization

Source

Open in PubMed Open full text

Identifiers

PMID: 23935483
DOI: 10.1371/journal.ppat.1003493
PMCID: PMC3723581

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

The viral chemokine MCK-2 of murine cytomegalovirus promotes infection as part of a gH/gL/MCK-2 complex.PMID 23935483Read ↗

The m74 Gene Product of Murine Cytomegalovirus (MCMV) Is a Functional Homolog of Human CMV gO and Determines the Entry Pathway of MCMVSemantic proximity Read ↗

Principles for studying in vivo attenuation of virus mutants: defining the role of the cytomegalovirus gH/gL/gO complex as a paradigm.Semantic proximity Read ↗

A dual role in virion attachment and entry makes the human cytomegalovirus gHgLgO trimer the central player in virion infectivitySemantic proximity Read ↗

Human Cytomegalovirus gH/gL/gO Promotes the Fusion Step of Entry into All Cell Types, whereas gH/gL/UL128-131 Broadens Virus Tropism through a Distinct Mechanism.Semantic proximity Read ↗

Cytomegalovirus MCK-2 controls mobilization and recruitment of myeloid progenitor cells to facilitate disseminationSemantic proximity Read ↗

Fatal attraction: cytomegalovirus-encoded chemokine homologs.Semantic proximity Read ↗

Human cytomegalovirus glycoprotein complex gH/gL/gO uses PDGFR-α as a key for entry.Semantic proximity Read ↗

Mutagenesis of human cytomegalovirus glycoprotein L disproportionately disrupts gH/gL/gO over gH/gL/pUL128-131Semantic proximity Read ↗

A viral regulator of glycoprotein complexes contributes to human cytomegalovirus cell tropism.Semantic proximity Read ↗

The N Terminus of Human Cytomegalovirus Glycoprotein O Is Important for Binding to the Cellular Receptor PDGFRαSemantic proximity Read ↗

Mutagenesis of Human Cytomegalovirus Glycoprotein L Disproportionately Disrupts gH/gL/gO over gH/gL/pUL128-131.Semantic proximity Read ↗

Comparative analysis of gO isoforms reveals that strains of human cytomegalovirus differ in the ratio of gH/gL/gO and gH/gL/UL128-131 in the virion envelope.Semantic proximity Read ↗

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