Evidence map›Paper›PMID 21422179›Full record

ArticleInfection and immunity2011

Serine protease PrtA from Streptococcus pneumoniae plays a role in the killing of S. pneumoniae by apolactoferrin.

Shaper Mirza, Landon Wilson, William H Benjamin, Jan Novak, Stephen Barnes, Susan K Hollingshead, David E Briles

Open access · greenAbstract read
In one paragraph

Article in Infection and immunity, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.7field-weighted citation impact, top 6% 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

24 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
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  8. Extracellular Pneumococcal Serine Proteases Affect Nasopharyngeal Colonization.Frontiers in cellular and infection microbiology · 2020
    Article
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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

7 authors at 3 institutions in 1 country.

Shaper MirzaDepartment of Microbiology, Division of Epidemiology, University of Alabama at Birmingham, 845 19th Street South, Birmingham, AL 35294-2170, USA.
Landon Wilson
William H Benjamin
Jan Novak
Stephen Barnes
Susan K Hollingshead
David E Briles
University of Alabama at Birmingham · USTarget (United States) · USThe University of Texas Health Science Center at Houston · US

Funding

PspA: A Potential Pneumococcal Vaccine ComponentR01AI021548 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BRILES, DAVID E · 1985 to 2012
$6.0M
Evolution of Virulence in Streptococcus pneumoniaeR01AI053749 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI HOLLINGSHEAD, SUSAN K. · 2003 to 2007
$1.8M
PspA mechanisms of humoral immunity, functional assays, and optimal vaccine constR56AI021548 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BRILES, DAVID E · 2014 to 2014
$543k
SPECT: POLYPHENOLS: SOY &MENARCHE,0STEOPOR, GREEN TEA&BREAST CANCER, NEURODIS S10RR019231 · NCRR · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BARNES, STEPHEN · 2004 to 2004
$465k
NCRR NIH HHS S10 RR019231NCRR NIH HHS S10 RR19231-01NIAID NIH HHS AI053749NIAID NIH HHS AI21548NIAID NIH HHS R01 AI021548NIAID NIH HHS R01 AI053749NIAID NIH HHS R56 AI021548
6 · The paper itself

Abstract

It is known that apolactoferrin, the iron-free form of human lactoferrin, can kill many species of bacteria, including Streptococcus pneumoniae. Lactoferricin, an N-terminal peptide of apolactoferrin, and fragments of it are even more bactericidal than apolactoferrin. In this study we found that apolactoferrin must be cleaved by a serine protease in order for it to kill pneumococci. The serine protease inhibitors were able to block killing by apolactoferrin but did not block killing by a lactoferrin-derived peptide. Thus, the killing of pneumococci by apolactoferrin appears to require a protease to release a lactoferricin-like peptide(s). Incubation of apolactoferrin with growing pneumococci resulted in a 12-kDa reduction in its molecular mass, of which about 7 to 8 kDa of the reduction was protease dependent. Capsular type 2 and 19F strains with mutations in the gene encoding the major cell wall-associated serine protease, prtA, lost much of their ability to degrade apolactoferrin and were relatively resistant to killing by apolactoferrin (P < 0.001). Recombinant PrtA was also able to cleave apolactoferrin, reducing its mass by about 8 kDa, and greatly enhance the killing activity of the solution containing the apolactoferrin and its cleavage products. Mass spectroscopy revealed that PrtA makes a major cut between amino acids 78 and 79 of human lactoferrin, removing the N-terminal end of the molecule (about 8.6 kDa). The simplest interpretation of these data is that the mechanism by which apolactoferrin kills Streptococcus pneumoniae requires the release of a lactoferricin-like peptide(s) and that it is this peptide(s), and not the intact apolactoferrin, which kills pneumococci.

Indexed as

ApoproteinsBlotting, WesternCloning, MolecularHost-Pathogen InteractionsHumansLactoferrinPneumococcal InfectionsRecombinant ProteinsSerine ProteasesSerine Proteinase InhibitorsStreptococcus pneumoniaeTandem Mass SpectrometryapolactoferrinApoproteinsLactoferrinRecombinant ProteinsSerine ProteasesSerine Proteinase Inhibitors

Identifiers

PMID21422179
PMCPMC3125832
OpenAlexW2131779159

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.