Evidence map›Paper›PMID 34649250›Full record

ReviewJournal of innate immunity2022

The Role of Streptococcal Cell-Envelope Proteases in Bacterial Evasion of the Innate Immune System.

Sophie McKenna, Kristin Krohn Huse, Sean Giblin, Max Pearson, Mohammed Said Majid Al Shibar, Shiranee Sriskandan, Stephen Matthews, James Edward Pease

Open access · goldAbstract readReview
In one paragraph

Review in Journal of innate immunity, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

11 citing papers in PubMed, 16 citations in OpenAlex.

  1. Review
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  5. ImmunogenicmSphere · 2025
    Article
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  7. 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

8 authors at 1 institution in 1 country.

Sophie McKennaDepartment of Life Sciences, Imperial College London, London, United Kingdom.
Kristin Krohn HuseDepartment of Infectious Disease, Imperial College London, London, United Kingdom.
Sean GiblinNational Heart and Lung Institute, Imperial College London, London, United Kingdom.
Max PearsonDepartment of Infectious Disease, Imperial College London, London, United Kingdom.
Mohammed Said Majid Al ShibarNational Heart and Lung Institute, Imperial College London, London, United Kingdom.
Shiranee SriskandanDepartment of Infectious Disease, Imperial College London, London, United Kingdom.
Stephen MatthewsDepartment of Life Sciences, Imperial College London, London, United Kingdom.
James Edward PeaseNational Heart and Lung Institute, Imperial College London, London, United Kingdom.
Imperial College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacteria possess the ability to evolve varied and ingenious strategies to outwit the host immune system, instigating an evolutionary arms race. Proteases are amongst the many weapons employed by bacteria, which specifically cleave and neutralize key signalling molecules required for a coordinated immune response. In this article, we focus on a family of S8 subtilisin-like serine proteases expressed as cell-envelope proteases (CEPs) by group A and group B streptococci. Two of these proteases known as Streptococcus pyogenes CEP (SpyCEP) and C5a peptidase cleave the chemokine CXCL8 and the complement fragment C5a, respectively. Both CXCL8 and C5a are potent neutrophil-recruiting chemokines, and by neutralizing their activity, streptococci evade a key defence mechanism of innate immunity. We review the mechanisms by which CXCL8 and C5a recruit neutrophils and the characterization of SpyCEP and C5a peptidase, including both in vitro and in vivo studies. Recently described structural insights into the function of this CEP family are also discussed. We conclude by examining the progress of prototypic vaccines incorporating SpyCEP and C5a peptidase in their preparation. Since streptococci-producing SpyCEP and C5a peptidase are responsible for a considerable global disease burden, targeting these proteases by vaccination strategies or by small-molecule antagonists should provide protection from and promote the resolution of streptococcal infections.

Indexed as

Peptide HydrolasesStreptococcal InfectionsCell WallHumansNeutrophilsStreptococcus pyogenesPeptide HydrolasesBacterial infectionCell-envelope proteaseChemoattractantsComplement systemStreptococcus

Identifiers

PMID34649250
PMCPMC9082167
OpenAlexW3205442324

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.