Evidence map›Paper›PMID 24757444›Full record

ArticleInterdisciplinary perspectives on infectious diseases2014

Identification of Sphingomyelinase on the Surface of Chlamydia pneumoniae: Possible Role in the Entry into Its Host Cells.

Tuula A Peñate Medina, Juha T Korhonen, Riitta Lahesmaa, Mirja Puolakkainen, Oula Peñate Medina, Paavo K J Kinnunen

Open access · goldAbstract read
In one paragraph

Article in Interdisciplinary perspectives on infectious diseases, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.4field-weighted citation impact, top 35% 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

4 citing papers in PubMed, 3 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

6 authors at 3 institutions in 2 countries.

Tuula A Peñate MedinaHelsinki Biophysics & Biomembrane Group, Medical Biochemistry, Institute of Biomedicine, University of Helsinki, 00014 Helsinki, Finland ; Molecular Imaging North Competence Center (MOIN CC), Christian-Albrechts Universität zu Kiel, AmBotanischen Garten 14, 24118 Kiel, Germany.
Juha T KorhonenTurku Centre for Biotechnology, 20520 Turku, Finland.
Riitta LahesmaaTurku Centre for Biotechnology, 20520 Turku, Finland.
Mirja PuolakkainenHUSLAB, Department of Virology, Haartman Institute, University of Helsinki, 00014 Helsinki, Finland.
Oula Peñate MedinaHelsinki Biophysics & Biomembrane Group, Medical Biochemistry, Institute of Biomedicine, University of Helsinki, 00014 Helsinki, Finland ; Molecular Imaging North Competence Center (MOIN CC), Christian-Albrechts Universität zu Kiel, AmBotanischen Garten 14, 24118 Kiel, Germany.
Paavo K J KinnunenHelsinki Biophysics & Biomembrane Group, Medical Biochemistry, Institute of Biomedicine, University of Helsinki, 00014 Helsinki, Finland ; Helsinki Biophysics & Biomembrane Group, Department of Biomedical Engineering and Computational Science, P.O. Box 12200, Rakentajanaukio 3, 00076 Aalto, Finland.
University of Helsinki · FITurku Centre for Biotechnology · FIKiel University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have recently suggested a novel mechanism, autoendocytosis, for the entry of certain microbes into their hosts, with a key role played by the sphingomyelinase-catalyzed topical conversion of sphingomyelin to ceramide, the differences in the biophysical properties of these two lipids providing the driving force. The only requirement for such microbes to utilize this mechanism is that they should have a catalytically active SMase on their outer surface while the target cells should expose sphingomyelin in the external leaflet of their plasma membrane. In pursuit of possible microbial candidates, which could utilize this putative mechanism, we conducted a sequence similarity search for SMase. Because of the intriguing cellular and biochemical characteristics of the poorly understood entry of Chlamydia into its host cells these microbes were of particular interest. SMase activity was measured in vitro from isolated C. pneumoniae elementary bodies (EB) and in the lysate from E. coli cells transfected with a plasmid expressing CPn0300 protein having sequence similarity to SMase. Finally, pretreatment of host cells with exogenous SMase resulting in loss plasma membrane sphingomyelin attenuated attachment of EB.

Identifiers

PMID24757444
PMCPMC3976853
OpenAlexW2047553389

What OpenQuestion holds

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LicenceCC BY
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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.