Pathogenicity and virulence of Streptococcus pneumoniae: Cutting to the chase on proteases
Bacterial proteases and peptidases are integral to cell physiology and stability, and their necessity in Streptococcus pneumoniae is no exception. Protein cleavage and processing mechanisms within the bacterial cell serve to ensure that the cell lives and functions in its commensal habitat and can r...
Main Author: | |
---|---|
Format: | Article |
Language: | English |
Published: |
Taylor & Francis Group
2021-01-01
|
Series: | Virulence |
Subjects: | |
Online Access: | http://dx.doi.org/10.1080/21505594.2021.1889812 |
id |
doaj-d109bb89b29646b99107392c4d62fb3b |
---|---|
record_format |
Article |
spelling |
doaj-d109bb89b29646b99107392c4d62fb3b2021-03-18T15:12:52ZengTaylor & Francis GroupVirulence2150-55942150-56082021-01-0112176678710.1080/21505594.2021.18898121889812Pathogenicity and virulence of Streptococcus pneumoniae: Cutting to the chase on proteasesMary E. Marquart0University of Mississippi Medical CenterBacterial proteases and peptidases are integral to cell physiology and stability, and their necessity in Streptococcus pneumoniae is no exception. Protein cleavage and processing mechanisms within the bacterial cell serve to ensure that the cell lives and functions in its commensal habitat and can respond to new environments presenting stressful conditions. For S. pneumoniae, the human nasopharynx is its natural habitat. In the context of virulence, movement of S. pneumoniae to the lungs, blood, or other sites can instigate responses by the bacteria that result in their proteases serving dual roles of self-protein processors and virulence factors of host protein targets.http://dx.doi.org/10.1080/21505594.2021.1889812peptidaseproteaseproteinasestreptococcus pneumoniaevirulence |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Mary E. Marquart |
spellingShingle |
Mary E. Marquart Pathogenicity and virulence of Streptococcus pneumoniae: Cutting to the chase on proteases Virulence peptidase protease proteinase streptococcus pneumoniae virulence |
author_facet |
Mary E. Marquart |
author_sort |
Mary E. Marquart |
title |
Pathogenicity and virulence of Streptococcus pneumoniae: Cutting to the chase on proteases |
title_short |
Pathogenicity and virulence of Streptococcus pneumoniae: Cutting to the chase on proteases |
title_full |
Pathogenicity and virulence of Streptococcus pneumoniae: Cutting to the chase on proteases |
title_fullStr |
Pathogenicity and virulence of Streptococcus pneumoniae: Cutting to the chase on proteases |
title_full_unstemmed |
Pathogenicity and virulence of Streptococcus pneumoniae: Cutting to the chase on proteases |
title_sort |
pathogenicity and virulence of streptococcus pneumoniae: cutting to the chase on proteases |
publisher |
Taylor & Francis Group |
series |
Virulence |
issn |
2150-5594 2150-5608 |
publishDate |
2021-01-01 |
description |
Bacterial proteases and peptidases are integral to cell physiology and stability, and their necessity in Streptococcus pneumoniae is no exception. Protein cleavage and processing mechanisms within the bacterial cell serve to ensure that the cell lives and functions in its commensal habitat and can respond to new environments presenting stressful conditions. For S. pneumoniae, the human nasopharynx is its natural habitat. In the context of virulence, movement of S. pneumoniae to the lungs, blood, or other sites can instigate responses by the bacteria that result in their proteases serving dual roles of self-protein processors and virulence factors of host protein targets. |
topic |
peptidase protease proteinase streptococcus pneumoniae virulence |
url |
http://dx.doi.org/10.1080/21505594.2021.1889812 |
work_keys_str_mv |
AT maryemarquart pathogenicityandvirulenceofstreptococcuspneumoniaecuttingtothechaseonproteases |
_version_ |
1724215618016641024 |