Evidence map›Paper›PMID 25271164›Full record

ArticleThe Journal of biological chemistry2014

Synthesis and assembly of a novel glycan layer in Myxococcus xanthus spores.

Carina Holkenbrink, Egbert Hoiczyk, Jörg Kahnt, Penelope I Higgs

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Milestones in the development ofJournal of bacteriology · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Article
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  16. Article
  17. TheJournal of bacteriology · 2017
    Article
  18. Review
  19. Article
  20. Article
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

4 authors.

Carina HolkenbrinkDepartment of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany.
Egbert HoiczykW. Harry Feinstone Department of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health, Baltimore, Maryland 21205, and.
Jörg KahntDepartment of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany.
Penelope I HiggsDepartment of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany,; Department of Biological Sciences, Wayne State University, Detroit, Michigan 48202. Electronic address: pihiggs@wayne.edu.

Funding

Novel ParP Pilus of Myxococcus XanthusR01GM085024 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI HOICZYK, EGBERT · 2008 to 2012
$1.6M
NIGMS NIH HHS GM85024NIGMS NIH HHS R01 GM085024
6 · The paper itself

Abstract

Myxococcus xanthus is a Gram-negative deltaproteobacterium that has evolved the ability to differentiate into metabolically quiescent spores that are resistant to heat and desiccation. An essential feature of the differentiation processes is the assembly of a rigid, cell wall-like spore coat on the surface of the outer membrane. In this study, we characterize the spore coat composition and describe the machinery necessary for secretion of spore coat material and its subsequent assembly into a stress-bearing matrix. Chemical analyses of isolated spore coat material indicate that the spore coat consists primarily of short 1-4- and 1-3-linked GalNAc polymers that lack significant glycosidic branching and may be connected by glycine peptides. We show that 1-4-linked glucose (Glc) is likely a minor component of the spore coat with the majority of the Glc arising from contamination with extracellular polysaccharides, O-antigen, or storage compounds. Neither of these structures is required for the formation of resistant spores. Our analyses indicate the GalNAc/Glc polymer and glycine are exported by the ExoA-I system, a Wzy-like polysaccharide synthesis and export machinery. Arrangement of the capsular-like polysaccharides into a rigid spore coat requires the NfsA-H proteins, members of which reside in either the cytoplasmic membrane (NfsD, -E, and -G) or outer membrane (NfsA, -B, and -C). The Nfs proteins function together to modulate the chain length of the surface polysaccharides, which is apparently necessary for their assembly into a stress-bearing matrix.

Indexed as

Bacterial ProteinsCentrifugation, Density GradientMicroscopy, ElectronMutationMyxococcus xanthusO AntigensOligosaccharidesPhenotypePolysaccharidesSpores, BacterialBacterial ProteinsO AntigensOligosaccharidesPolysaccharidesGram-negative BacteriaMembrane ProteinPeptidoglycanPolysaccharideSporulation

Identifiers

PMID25271164
PMCPMC4231708

What OpenQuestion holds

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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.