Evidence map›Paper›PMID 25512310›Full record

ArticleJournal of bacteriology2015

Variations in O-antigen biosynthesis and O-acetylation associated with altered phage sensitivity in Escherichia coli 4s.

Yuriy A Knirel, Nikolai S Prokhorov, Alexander S Shashkov, Olga G Ovchinnikova, Evelina L Zdorovenko, Bin Liu, Elena S Kostryukova, Andrey K Larin, Alla K Golomidova, Andrey V Letarov

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed, 1 pooled it
3.1field-weighted citation impact, top 9% 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

34 citing papers in PubMed, 1 synthesis or guideline pooled it, 77 citations in OpenAlex.

  1. Pooled it
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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

10 authors at 4 institutions in 2 countries.

Yuriy A KnirelN. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia yknirel@gmail.com letarov@gmail.com.
Nikolai S ProkhorovS. N. Winogradsky Institute of Microbiology, Russian Academy of Sciences, Moscow, Russia.
Alexander S ShashkovN. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia.
Olga G OvchinnikovaN. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia.
Evelina L ZdorovenkoN. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia.
Bin LiuTEDA School of Biological Sciences and Biotechnology, Nankai University, TEDA, Tianjin, People's Republic of China.
Elena S KostryukovaInstitute of Physical and Chemical Medicine, Federal Medical and Biological Agency, Moscow, Russia.
Andrey K LarinInstitute of Physical and Chemical Medicine, Federal Medical and Biological Agency, Moscow, Russia Kazan Federal University, Kazan, Russia.
Alla K GolomidovaS. N. Winogradsky Institute of Microbiology, Russian Academy of Sciences, Moscow, Russia.
Andrey V LetarovS. N. Winogradsky Institute of Microbiology, Russian Academy of Sciences, Moscow, Russia yknirel@gmail.com letarov@gmail.com.
N.D. Zelinsky Institute of Organic Chemistry · RURussian Academy of Sciences · RUFederal Medical-Biological Agency · RUTianjin Economic-Technological Development Area · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The O polysaccharide of the lipopolysaccharide (O antigen) of Gram-negative bacteria often serves as a receptor for bacteriophages that can make the phage dependent on a given O-antigen type, thus supporting the concept of the adaptive significance of the O-antigen variability in bacteria. The O-antigen layer also modulates interactions of many bacteriophages with their hosts, limiting the access of the viruses to other cell surface receptors. Here we report variations of O-antigen synthesis and structure in an environmental Escherichia coli isolate, 4s, obtained from horse feces, and its mutants selected for resistance to bacteriophage G7C, isolated from the same fecal sample. The 4s O antigen was found to be serologically, structurally, and genetically related to the O antigen of E. coli O22, differing only in side-chain α-D-glucosylation in the former, mediated by a gtr locus on the chromosome. Spontaneous mutations of E. coli 4s occurring with an unusually high frequency affected either O-antigen synthesis or O-acetylation due to the inactivation of the gene encoding the putative glycosyltransferase WclH or the putative acetyltransferase WclK, respectively, by the insertion of IS1-like elements. These mutations induced resistance to bacteriophage G7C and also modified interactions of E. coli 4s with several other bacteriophages conferring either resistance or sensitivity to the host. These findings suggest that O-antigen synthesis and O-acetylation can both ensure the specific recognition of the O-antigen receptor following infection by some phages and provide protection of the host cells against attack by other phages.

Indexed as

AcetylationAnimalsBacteriophagesCarbohydrate SequenceEscherichia coliEscherichia coli ProteinsFecesHorsesHost SpecificityMolecular Sequence DataO AntigensEscherichia coli ProteinsO Antigens

Identifiers

PMID25512310
PMCPMC4325112
OpenAlexW2100869752

What OpenQuestion holds

Textmetadata
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.