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

Mutation of the nuclear localization signals of the major tegument protein pp65 leads to impairment of human cytomegalovirus progeny production.

The Journal of general virology - 1 Oct 2025

Büscher Nicole, Sinzger Christian, Lehmann Caroline, Zimmermann Christine, Schmidt Hanno, Plachter Bodo

Abstract excerpt

The phosphoprotein 65 (pp65, pUL83) of human cytomegalovirus (HCMV) serves several functions during the viral life cycle. It is one of the most abundant constituents of the virion tegument and the major component of subviral particles termed Dense Bodies. It is also one of several tegument proteins that mediate the subversion of cellular antiviral defence functions like the induction of IFNs. It is also involved...

Read the complete abstract on PubMed

Topics

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

Share to Cell Nucleus
Share to Cytomegalovirus

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

Share to Cytomegalovirus Infections

Share to Fibroblasts

Share to Nuclear Localization Signals

Share to Phosphoproteins

Share to Viral Matrix Proteins

Share to Virus Replication

Source

Identifiers

PMID: 41118246
DOI: 10.1099/jgv.0.002167

Genes

IFI16

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 23 Oct 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

Mutation of the nuclear localization signals of the major tegument protein pp65 leads to impairment of human cytomegalovirus progeny production.PMID 41118246Read ↗

The dominant phosphoprotein pp65 (UL83) of human cytomegalovirus is dispensable for growth in cell cultureSemantic proximity Read ↗

Major Tegument Protein pp65 of Human Cytomegalovirus Is Required for the Incorporation of pUL69 and pUL97 into the Virus Particle and for Viral Growth in MacrophagesSemantic proximity Read ↗

Nuclear targeting of the tegument protein pp65 (UL83) of human cytomegalovirus: an unusual bipartite nuclear localization signal functions with other portions of the protein to mediate its efficient nuclear transportSemantic proximity Read ↗

Regulatory Interaction between the Cellular Restriction Factor IFI16 and Viral pp65 (pUL83) Modulates Viral Gene Expression and IFI16 Protein StabilitySemantic proximity Read ↗

Human cytomegalovirus UL83-coded pp65 virion protein inhibits antiviral gene expression in infected cellsSemantic proximity Read ↗

Phenotypical Characterization of the Nuclear Egress of Recombinant Cytomegaloviruses Reveals Defective Replication upon ORF-UL50 Deletion but Not pUL50 Phosphosite Mutation.Semantic proximity Read ↗

Cytomegalovirus UL103 Controls Virion and Dense Body EgressSemantic proximity Read ↗

The Tegument Protein UL71 of Human Cytomegalovirus Is Involved in Late Envelopment and Affects Multivesicular BodiesSemantic proximity Read ↗

The Flexible Loop of the Human Cytomegalovirus DNA Polymerase Processivity Factor ppUL44 Is Required for Efficient DNA Binding and Replication in CellsSemantic proximity Read ↗

Nuclear localization of tegument-delivered pp71 in human cytomegalovirus-infected cells is facilitated by one or more factors present in terminally differentiated fibroblasts.Semantic proximity Read ↗

Human Cytomegalovirus Protein Kinase UL97 Forms a Complex with the Tegument Phosphoprotein pp65Semantic proximity Read ↗

Human Cytomegalovirus Tegument Protein pUL71 Is Required for Efficient Virion EgressSemantic proximity Read ↗

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