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Arginine Decarboxylase Is Essential for Pneumococcal Stress Responses

Polyamines such as putrescine, cadaverine, and spermidine are small cationic molecules that play significant roles in cellular processes, including bacterial stress responses and host–pathogen interactions. Streptococcus pneumoniae is an opportunistic human pathogen, which causes several diseases th...

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Autores principales: Frances Nakamya, Mary, Ayoola, Moses B., Shack, Leslie A., Mohamed, Mirghani, Swiatlo, Edwin, Nanduri, Bindu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7998104/
https://www.ncbi.nlm.nih.gov/pubmed/33801541
http://dx.doi.org/10.3390/pathogens10030286
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author Frances Nakamya, Mary
Ayoola, Moses B.
Shack, Leslie A.
Mohamed, Mirghani
Swiatlo, Edwin
Nanduri, Bindu
author_facet Frances Nakamya, Mary
Ayoola, Moses B.
Shack, Leslie A.
Mohamed, Mirghani
Swiatlo, Edwin
Nanduri, Bindu
author_sort Frances Nakamya, Mary
collection PubMed
description Polyamines such as putrescine, cadaverine, and spermidine are small cationic molecules that play significant roles in cellular processes, including bacterial stress responses and host–pathogen interactions. Streptococcus pneumoniae is an opportunistic human pathogen, which causes several diseases that account for significant morbidity and mortality worldwide. As it transits through different host niches, S. pneumoniae is exposed to and must adapt to different types of stress in the host microenvironment. We earlier reported that S. pneumoniae TIGR4, which harbors an isogenic deletion of an arginine decarboxylase (ΔspeA), an enzyme that catalyzes the synthesis of agmatine in the polyamine synthesis pathway, has a reduced capsule. Here, we report the impact of arginine decarboxylase deletion on pneumococcal stress responses. Our results show that ΔspeA is more susceptible to oxidative, nitrosative, and acid stress compared to the wild-type strain. Gene expression analysis by qRT-PCR indicates that thiol peroxidase, a scavenger of reactive oxygen species and aguA from the arginine deiminase system, could be important for peroxide stress responses in a polyamine-dependent manner. Our results also show that speA is essential for endogenous hydrogen peroxide and glutathione production in S. pneumoniae. Taken together, our findings demonstrate the critical role of arginine decarboxylase in pneumococcal stress responses that could impact adaptation and survival in the host.
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spelling pubmed-79981042021-03-28 Arginine Decarboxylase Is Essential for Pneumococcal Stress Responses Frances Nakamya, Mary Ayoola, Moses B. Shack, Leslie A. Mohamed, Mirghani Swiatlo, Edwin Nanduri, Bindu Pathogens Article Polyamines such as putrescine, cadaverine, and spermidine are small cationic molecules that play significant roles in cellular processes, including bacterial stress responses and host–pathogen interactions. Streptococcus pneumoniae is an opportunistic human pathogen, which causes several diseases that account for significant morbidity and mortality worldwide. As it transits through different host niches, S. pneumoniae is exposed to and must adapt to different types of stress in the host microenvironment. We earlier reported that S. pneumoniae TIGR4, which harbors an isogenic deletion of an arginine decarboxylase (ΔspeA), an enzyme that catalyzes the synthesis of agmatine in the polyamine synthesis pathway, has a reduced capsule. Here, we report the impact of arginine decarboxylase deletion on pneumococcal stress responses. Our results show that ΔspeA is more susceptible to oxidative, nitrosative, and acid stress compared to the wild-type strain. Gene expression analysis by qRT-PCR indicates that thiol peroxidase, a scavenger of reactive oxygen species and aguA from the arginine deiminase system, could be important for peroxide stress responses in a polyamine-dependent manner. Our results also show that speA is essential for endogenous hydrogen peroxide and glutathione production in S. pneumoniae. Taken together, our findings demonstrate the critical role of arginine decarboxylase in pneumococcal stress responses that could impact adaptation and survival in the host. MDPI 2021-03-02 /pmc/articles/PMC7998104/ /pubmed/33801541 http://dx.doi.org/10.3390/pathogens10030286 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ).
spellingShingle Article
Frances Nakamya, Mary
Ayoola, Moses B.
Shack, Leslie A.
Mohamed, Mirghani
Swiatlo, Edwin
Nanduri, Bindu
Arginine Decarboxylase Is Essential for Pneumococcal Stress Responses
title Arginine Decarboxylase Is Essential for Pneumococcal Stress Responses
title_full Arginine Decarboxylase Is Essential for Pneumococcal Stress Responses
title_fullStr Arginine Decarboxylase Is Essential for Pneumococcal Stress Responses
title_full_unstemmed Arginine Decarboxylase Is Essential for Pneumococcal Stress Responses
title_short Arginine Decarboxylase Is Essential for Pneumococcal Stress Responses
title_sort arginine decarboxylase is essential for pneumococcal stress responses
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7998104/
https://www.ncbi.nlm.nih.gov/pubmed/33801541
http://dx.doi.org/10.3390/pathogens10030286
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