Evidence map›Paper›PMID 17229708›Full record

ArticleJournal of virology2007

The carboxy-terminal domain of glycoprotein N of human cytomegalovirus is required for virion morphogenesis.

Michael Mach, Karolina Osinski, Barbara Kropff, Ursula Schloetzer-Schrehardt, Magdalena Krzyzaniak, William Britt

Abstract 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 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
–field-weighted citation impact
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

38 citing papers in PubMed.

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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

6 authors.

Michael MachInstitut für Klinische und Molekulare Virologie, Universität Erlangen-Nürnberg, Schlossgarten 4, 91054 Erlangen, Germany. mlmach@viro.med.uni-erlangen.de
Karolina Osinski
Barbara Kropff
Ursula Schloetzer-Schrehardt
Magdalena Krzyzaniak
William Britt

Funding

ENVELOPE ASSEMBLY OF HUMAN CYTOMEGALOVIRUSR01AI035602 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BRITT, WILLIAM JARVIS · 1995 to 2018
$4.5M
gM/gN and Envelopment of HCMVR01AI050189 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BRITT, WILLIAM JARVIS · 2002 to 2012
$3.1M
NIAID NIH HHS R01 AI035602NIAID NIH HHS R01 AI050189NIAID NIH HHS R01 AI35602NIAID NIH HHS R01 AI50189
6 · The paper itself

Abstract

Glycoproteins M and N (gM and gN, respectively) are among the few proteins that are conserved across the herpesvirus family. The function of the complex is largely unknown. Whereas deletion from most alphaherpesviruses has marginal effects on the replication of the respective viruses, both proteins are essential for replication of human cytomegalovirus (HCMV). We have constructed a series of mutants in gN to study the function of this protein. gN of HCMV is a type I glycoprotein containing a short carboxy-terminal domain of 14 amino acids, including two cysteine residues directly adjacent to the predicted transmembrane anchor at positions 125 and 126. Deletion of the entire carboxy-terminal domain as well as substitution with the corresponding region from alpha herpesviruses or mutations of both cysteine residues resulted in a replication-incompetent virus. Recombinant viruses containing point mutations of either cysteine residue could be generated. These viruses were profoundly defective for replication. Complex formation of the mutant gNs with gM and transport of the complex to the viral assembly compartment appeared unaltered compared to the wild type. However, in infected cells, large numbers of capsids accumulated in the cytoplasm that failed to acquire an envelope. Transiently expressed gN was shown to be modified by palmitic acid at both cysteine residues. In summary, our data suggest that the carboxy-terminal domain of gN plays a critical role in secondary envelopment of HCMV and that palmitoylation of gN appears to be essential for function in secondary envelopment of HCMV and virus replication.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionCapsidCytomegalovirusCytoplasmHumansMicroscopy, ConfocalMicroscopy, Electron, TransmissionMicroscopy, FluorescenceMolecular Sequence DataMorphogenesisMutagenesis, Site-DirectedMutationProtein BindingProtein Structure, TertiaryProtein Transportglycoprotein N, Human cytomegalovirusViral Envelope Proteins

Identifiers

PMID17229708
PMCPMC1900226

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.