Evidence map›Paper›PMID 11390578›Full record

ArticleJournal of virology2001

A particle-associated glycoprotein signal peptide essential for virus maturation and infectivity.

D Lindemann, T Pietschmann, M Picard-Maureau, A Berg, M Heinkelein, J Thurow, P Knaus, H Zentgraf, A Rethwilm

Abstract read
In one paragraph

Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing 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

76 citing papers in PubMed.

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16 more citing papers are in PubMed but not listed here.

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

9 authors.

D LindemannInstitut für Virologie und Immunbiologie, Universität Würzburg, Versbacher Str. 7, 97078 Würzburg, 01307 Dresden, Germany. lindemann@mail.uni-wuerzburg.de
T Pietschmann
M Picard-Maureau
A Berg
M Heinkelein
J Thurow
P Knaus
H Zentgraf
A Rethwilm

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Signal peptides (SP) are key determinants for targeting glycoproteins to the secretory pathway. Here we describe the involvement in particle maturation as an additional function of a viral glycoprotein SP. The SP of foamy virus (FV) envelope glycoprotein is predicted to be unusually long. Using an SP-specific antiserum, we demonstrate that its proteolytic removal occurs posttranslationally by a cellular protease and that the major N-terminal cleavage product, gp18, is found in purified viral particles. Analysis of mutants in proposed signal peptidase cleavage positions and N-glycosylation sites revealed an SP about 148 amino acids (aa) in length. FV particle release from infected cells requires the presence of cognate envelope protein and cleavage of its SP sequence. An N-terminal 15-aa SP domain with two conserved tryptophan residues was found to be essential for the egress of FV particles. While the SP N terminus was found to mediate the specificity of FV Env to interact with FV capsids, it was dispensable for Env targeting to the secretory pathway and FV envelope-mediated infectivity of murine leukemia virus pseudotypes.

Indexed as

Cell LineGlycosylationHumansMembrane GlycoproteinsProtein Sorting SignalsSpumavirusViral Envelope ProteinsVirionMembrane GlycoproteinsProtein Sorting SignalsViral Envelope Proteins

Identifiers

PMID11390578
PMCPMC114292

What OpenQuestion holds

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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.