Evidence map›Paper›PMID 26370492›Full record

ArticleMolecular microbiology2016

Borrelia burgdorferi HtrA: evidence for twofold proteolysis of outer membrane protein p66.

James L Coleman, Alvaro Toledo, Jorge L Benach

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

19 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Endogenous and Borrowed Proteolytic Activity in theMicrobiology and molecular biology reviews : MMBR · 2021
    Review
  9. Article
  10. Lyme Disease Pathogenesis.Current issues in molecular biology · 2021
    Review
  11. In Silico Structural and Functional Characterization of HtrA Proteins ofTropical medicine and infectious disease · 2020
    Article
  12. Article
  13. Article
  14. Assessing the Contribution of an HtrA Family Serine Protease DuringFrontiers in cellular and infection microbiology · 2019
    Article
  15. Article
  16. Article
  17. Review
  18. Frontiers in immunology · 2017
    Review
  19. 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.

James L ColemanNew York State Department of Health, Stony Brook University, Stony Brook, NY, USA.
Alvaro ToledoDepartment of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, NY, USA.
Jorge L BenachDepartment of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, NY, USA.
Stony Brook University · US

Funding

Antigen Specific Response to BorreliaR01AI027044 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI BENACH, JORGE L. · 1989 to 2020
$3.7M
ANTIGEN SPECIFIC RESPONSES TO BORRELIAR37AI027044 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI BENACH, JORGE L. · 1998 to 2007
$2.6M
Antigen Specific Responses to BorreliaR56AI027044 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI BENACH, JORGE L. · 2015 to 2015
$467k
Acquisition of an Applied Biosystems 4000 QTRAP Mass SpectrometerS10RR023680 · NCRR · STATE UNIVERSITY NEW YORK STONY BROOK · PI IDEN, CHARLES R · 2007 to 2007
$435k
NCRR NIH HHS 1 S10 RR023680-1NCRR NIH HHS S10 RR023680NIAID NIH HHS AI-027044NIAID NIH HHS R01 AI027044NIAID NIH HHS R37 AI027044NIAID NIH HHS R56 AI027044
6 · The paper itself

Abstract

In prokaryotes, members of the High Temperature Requirement A (HtrA) family of serine proteases function in the periplasm to degrade damaged or improperly folded membrane proteins. Borrelia burgdorferi, the agent of Lyme disease, codes for a single HtrA homolog. Two-dimensional electrophoresis analysis of B. burgdorferi B31A3 and a strain that overexpresses HtrA (A3HtrAOE) identified a downregulated protein in A3HtrAOE with a mass, pI and MALDI-TOF spectrum consistent with outer membrane protein p66. P66 and HtrA from cellular lysates partitioned into detergent-resistant membranes, which contain cholesterol-glycolipid-rich membrane regions known as lipid rafts, suggesting that HtrA and p66 may reside together in lipid rafts also. This agrees with previous work from our laboratory, which showed that HtrA and p66 are constituents of B. burgdorferi outer membrane vesicles. HtrA degraded p66 in vitro and A3HtrAOE expressed reduced levels of p66 in vivo. Fluorescence confocal microscopy revealed that HtrA and p66 colocalize in the membrane. The association of HtrA and p66 establishes that they could interact efficiently and their protease/substrate relationship provides functional relevance to this interaction. A3HtrAOE also showed reduced levels of p66 transcript in comparison with wild-type B31A3, indicating that HtrA-mediated regulation of p66 may occur at multiple levels.

Indexed as

ProteolysisBacterial Outer Membrane ProteinsBacterial ProteinsBorrelia burgdorferiMicroscopy, ConfocalMicroscopy, FluorescencePorinsSerine EndopeptidasesBacterial Outer Membrane ProteinsBacterial ProteinsOms66 protein, BorreliaPorinsSerine Endopeptidases

Identifiers

PMID26370492
PMCPMC5004887
OpenAlexW1918524909

What OpenQuestion holds

Textmetadata
LicenceTDM
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.