Evidence map›Paper›PMID 17626081›Full record

ArticleJournal of virology2007

The cytoplasmic tail of glycoprotein M (gpUL100) expresses trafficking signals required for human cytomegalovirus assembly and replication.

Magdalena Krzyzaniak, Michael Mach, William J Britt

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.7field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

36 citing papers in PubMed, 51 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 2 countries.

Magdalena KrzyzaniakDepartment of Microbiology, University of Alabama School of Medicine, and Department of Pediatrics, Room 107, Harbor Bldg. Childrens Hospital, 1600 7th Ave. South, Birmingham, AL 35233, USA.
Michael Mach
William J Britt
Universitätsklinikum Erlangen · DEUniversity of Alabama at Birmingham · US

Funding

gM/gN and Envelopment of HCMVR01AI050189 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BRITT, WILLIAM JARVIS · 2002 to 2012
$3.1M
CMV Vaccines: Reinfection and Antigenic VariationR01AI049537 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BRITT, WILLIAM JARVIS · 2002 to 2007
$1.1M
NIAID NIH HHS AI49537NIAID NIH HHS AI50189NIAID NIH HHS R01 AI049537NIAID NIH HHS R01 AI050189
6 · The paper itself

Abstract

The virion envelope of human cytomegalovirus (HCMV) is complex and consists of an incompletely defined number of glycoproteins. The gM/gN protein complex is the most abundant protein component of the envelope. Studies have indicated that deletion of the viral gene encoding either gM or gN is a lethal mutation. Analysis of the amino acid sequence of gM disclosed a C-terminal acidic cluster of amino acids and a tyrosine-containing trafficking motif, both of which are well-described trafficking/sorting signals in the cellular secretory pathway. To investigate the roles of these signals in the trafficking of the gM/gN complex during virus assembly, we made a series of gM (UL100 open reading frame) mutants in the AD169 strain of HCMV. Mutant viruses that lacked the entire C-terminal cytoplasmic tail of gM were not viable, suggesting that the cytoplasmic tail of gM is essential for virus replication. In addition, the gM mutant protein lacking the cytoplasmic domain exhibited decreased protein stability. Mutant viruses with a deletion of the acidic cluster or alanine substitutions in tyrosine-based motifs were viable but exhibited a replication-impaired phenotype suggestive of a defect in virion assembly. Analysis of these mutant gMs using static immunofluorescence and fluorescence recovery after photobleaching demonstrated delayed kinetics of intracellular localization of the gM/gN protein to the virus assembly compartment compared to the wild-type protein. These data suggest an important role of the glycoprotein gM during virus assembly, particularly in the dynamics of gM trafficking during viral-particle assembly.

Indexed as

Protein Sorting SignalsVirus AssemblyVirus ReplicationAmino Acid SequenceCytomegalovirusEndosomesGlycoproteinsHumansMolecular Sequence DataMutationProtein TransportSequence DeletionViral Envelope Proteinsglycoprotein N, Human cytomegalovirusGlycoproteinsProtein Sorting SignalsViral Envelope Proteins

Identifiers

PMID17626081
PMCPMC2045486
OpenAlexW2152480343

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.