Evidence map›Paper›PMID 24140648›Full record

ArticleMicrobiology (Reading, England)2014

A non-catalytic histidine residue influences the function of the metalloprotease of Listeria monocytogenes.

Brian M Forster, Alan Pavinski Bitar, Hélène Marquis

Open access · greenAbstract read
In one paragraph

Article in Microbiology (Reading, England), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 32% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. 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

3 authors at 1 institution in 1 country.

Brian M ForsterDepartment of Microbiology and Immunology, Cornell University, Ithaca, NY 14853, USA.
Alan Pavinski BitarDepartment of Microbiology and Immunology, Cornell University, Ithaca, NY 14853, USA.
Hélène MarquisDepartment of Microbiology and Immunology, Cornell University, Ithaca, NY 14853, USA.
Cornell University · US

Funding

PHS HHS A152154
6 · The paper itself

Abstract

Mpl, a thermolysin-like metalloprotease, and PC-PLC, a phospholipase C, are synthesized as proenzymes by the intracellular bacterial pathogen Listeria monocytogenes. During intracellular growth, L. monocytogenes is temporarily confined in a membrane-bound vacuole whose acidification leads to Mpl autolysis and Mpl-mediated cleavage of the PC-PLC N-terminal propeptide. Mpl maturation also leads to the secretion of both Mpl and PC-PLC across the bacterial cell wall. Previously, we identified negatively charged and uncharged amino acid residues within the N terminus of the PC-PLC propeptide that influence the ability of Mpl to mediate the maturation of PC-PLC, suggesting that these residues promote the interaction of the PC-PLC propeptide with Mpl. In the present study, we identified a non-catalytic histidine residue (H226) that influences Mpl secretion across the cell wall and its ability to process PC-PLC. Our results suggest that a positive charge at position 226 is required for Mpl functions other than autolysis. Based on the charge requirement at this position, we hypothesize that this residue contributes to the interaction of Mpl with the PC-PLC propeptide.

Indexed as

Bacterial ProteinsEnzyme PrecursorsHistidineListeria monocytogenesMetalloendopeptidasesProtein Processing, Post-TranslationalType C PhospholipasesBacterial ProteinsEnzyme PrecursorsHistidineMetalloendopeptidasesmpl protein, Listeria monocytogenesphosphatidylcholine-specific phospholipase CType C Phospholipases

Identifiers

PMID24140648
PMCPMC3917227
OpenAlexW2096203282

What OpenQuestion holds

Textmetadata
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.