Evidence map›Paper›PMID 24214942›Full record

ArticleJournal of bacteriology2014

Modulation of the Bacillus anthracis secretome by the immune inhibitor A1 protease.

Kathryn J Pflughoeft, Michelle C Swick, David A Engler, Hye-Jeong Yeo, Theresa M Koehler

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

21 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
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  11. TheMicrobiology spectrum · 2019
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  13. A Dual Role for theFrontiers in microbiology · 2018
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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

5 authors at 3 institutions in 1 country.

Kathryn J PflughoeftDepartment of Microbiology and Molecular Genetics, Medical School, University of Texas Health Science Center at Houston, Houston, Texas, USA.
Michelle C Swick
David A Engler
Hye-Jeong Yeo
Theresa M Koehler
The University of Texas Health Science Center at Houston · USHouston Methodist · USUniversity of Houston · US

Funding

WRCE Nonhuman Primate CoreU54AI057156 · NIAID · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI WALKER, DAVID H · 2003 to 2013
$102.6M
Research Training in Pediatrics GastroenterolgyT32DK007664 · NIDDK · BAYLOR COLLEGE OF MEDICINE · PI DOUGLAS G BURRIN · 1991 to 2026
$8.4M
VIRULENCE GENE EXPRESSION BY BACILLUS ANTHRACISR01AI033537 · NIAID · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI KOEHLER, THERESA M. · 1998 to 2020
$5.4M
Molecular Basis of Infectious Diseases Training GrantT32AI055449 · NIAID · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI LORENZ, MICHAEL C · 2005 to 2025
$2.6M
CONTROL OF PROTECTIVE ANTIGEN SYNTHESIS BY B ANTHRACISR29AI033537 · NIAID · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI KOEHLER, THERESA M. · 1993 to 1997
–
NIAID NIH HHS AI033537NIAID NIH HHS R01 AI033537NIAID NIH HHS T32 AI055449NIAID NIH HHS T32 AI55449NIAID NIH HHS U54 AI057156NIDDK NIH HHS T32 DK007664PHS HHS R01
6 · The paper itself

Abstract

The Bacillus anthracis secretome includes protective antigen, lethal factor, and edema factor, which are the components of anthrax toxin, and other proteins with known or potential roles in anthrax disease. Immune inhibitor A1 (InhA1) is a secreted metalloprotease that is unique to pathogenic members of the Bacillus genus and has been associated with cleavage of host proteins during infection. Here, we report the effect of InhA1 on the B. anthracis secretome. Differential in-gel electrophoresis of proteins present in culture supernatants from a parent strain and an isogenic inhA1-null mutant revealed multiple differences. Of the 1,340 protein spots observed, approximately one-third were less abundant and one-third were more abundant in the inhA1 secretome than in the parent strain secretome. Proteases were strongly represented among those proteins exhibiting a 9-fold or greater change. InhA1 purified from a B. anthracis culture supernatant directly cleaved each of the anthrax toxin proteins as well as an additional secreted protease, Npr599. The conserved zinc binding motif HEXXH of InhA1 (HEYGH) was critical for its proteolytic activity. Our data reveal that InhA1 directly and indirectly modulates the form and/or abundance of over half of all the secreted proteins of B. anthracis. The proteolytic activity of InhA1 on established secreted virulence factors, additional proteases, and other secreted proteins suggests that this major protease plays an important role in virulence not only by cleaving mammalian substrates but also by modulating the B. anthracis secretome itself.

Indexed as

Amino Acid MotifsAntigens, BacterialBacillus anthracisBacterial ProteinsBacterial ToxinsBinding SitesElectrophoresisGene DeletionMetalloendopeptidasesProtein BindingProteomeZincanthrax toxinAntigens, BacterialBacterial ProteinsBacterial ToxinsMetalloendopeptidasesmicrobial metalloproteinasesProteomeZinc

Identifiers

PMID24214942
PMCPMC3911237
OpenAlexW2162915355

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.