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The C-Terminal Domain of Staphylococcus aureus Zinc Transport Protein AdcA Binds Plasminogen and Factor H In Vitro
Bacterial acquisition of metals from a host is an essential attribute to facilitate survival and colonization within an infected organism. Staphylococcus aureus, a bacterial pathogen of medical importance, has evolved its strategies to acquire multiple metals, including iron, manganese, and zinc. Ot...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8878332/ https://www.ncbi.nlm.nih.gov/pubmed/35215183 http://dx.doi.org/10.3390/pathogens11020240 |
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author | Salazar, Natália Yamamoto, Bruno Bernardi de Souza, Matilde Costa Lima da Silva, Ludmila Bezerra Arêas, Ana Paula Mattos Barbosa, Angela Silva |
author_facet | Salazar, Natália Yamamoto, Bruno Bernardi de Souza, Matilde Costa Lima da Silva, Ludmila Bezerra Arêas, Ana Paula Mattos Barbosa, Angela Silva |
author_sort | Salazar, Natália |
collection | PubMed |
description | Bacterial acquisition of metals from a host is an essential attribute to facilitate survival and colonization within an infected organism. Staphylococcus aureus, a bacterial pathogen of medical importance, has evolved its strategies to acquire multiple metals, including iron, manganese, and zinc. Other important strategies for the colonization and infection of the host have been reported for staphylococci and include the expression of adhesins on the bacterial surface, as well as the acquisition of host plasminogen and complement regulatory proteins. Here we assess the ability of the zinc transport protein AdcA from Staphylococcus aureus, first characterized elsewhere as a zinc-binding protein of the ABC (ATP-binding cassette) transporters, to bind to host molecules. Like other staphylococcus ion-scavenging proteins, such as MntC, a manganese-binding protein, AdcA interacts with human plasminogen. Once activated, plasmin bound to AdcA cleaves fibrinogen and vitronectin. In addition, AdcA interacts with the human negative complement regulator factor H (FH). Plasminogen and FH have been shown to bind to distinct sites on the AdcA C-terminal portion. In conclusion, our in vitro data pave the way for future studies addressing the relevance of AdcA interactions with host molecules in vivo. |
format | Online Article Text |
id | pubmed-8878332 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-88783322022-02-26 The C-Terminal Domain of Staphylococcus aureus Zinc Transport Protein AdcA Binds Plasminogen and Factor H In Vitro Salazar, Natália Yamamoto, Bruno Bernardi de Souza, Matilde Costa Lima da Silva, Ludmila Bezerra Arêas, Ana Paula Mattos Barbosa, Angela Silva Pathogens Article Bacterial acquisition of metals from a host is an essential attribute to facilitate survival and colonization within an infected organism. Staphylococcus aureus, a bacterial pathogen of medical importance, has evolved its strategies to acquire multiple metals, including iron, manganese, and zinc. Other important strategies for the colonization and infection of the host have been reported for staphylococci and include the expression of adhesins on the bacterial surface, as well as the acquisition of host plasminogen and complement regulatory proteins. Here we assess the ability of the zinc transport protein AdcA from Staphylococcus aureus, first characterized elsewhere as a zinc-binding protein of the ABC (ATP-binding cassette) transporters, to bind to host molecules. Like other staphylococcus ion-scavenging proteins, such as MntC, a manganese-binding protein, AdcA interacts with human plasminogen. Once activated, plasmin bound to AdcA cleaves fibrinogen and vitronectin. In addition, AdcA interacts with the human negative complement regulator factor H (FH). Plasminogen and FH have been shown to bind to distinct sites on the AdcA C-terminal portion. In conclusion, our in vitro data pave the way for future studies addressing the relevance of AdcA interactions with host molecules in vivo. MDPI 2022-02-12 /pmc/articles/PMC8878332/ /pubmed/35215183 http://dx.doi.org/10.3390/pathogens11020240 Text en © 2022 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 (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Salazar, Natália Yamamoto, Bruno Bernardi de Souza, Matilde Costa Lima da Silva, Ludmila Bezerra Arêas, Ana Paula Mattos Barbosa, Angela Silva The C-Terminal Domain of Staphylococcus aureus Zinc Transport Protein AdcA Binds Plasminogen and Factor H In Vitro |
title | The C-Terminal Domain of Staphylococcus aureus Zinc Transport Protein AdcA Binds Plasminogen and Factor H In Vitro |
title_full | The C-Terminal Domain of Staphylococcus aureus Zinc Transport Protein AdcA Binds Plasminogen and Factor H In Vitro |
title_fullStr | The C-Terminal Domain of Staphylococcus aureus Zinc Transport Protein AdcA Binds Plasminogen and Factor H In Vitro |
title_full_unstemmed | The C-Terminal Domain of Staphylococcus aureus Zinc Transport Protein AdcA Binds Plasminogen and Factor H In Vitro |
title_short | The C-Terminal Domain of Staphylococcus aureus Zinc Transport Protein AdcA Binds Plasminogen and Factor H In Vitro |
title_sort | c-terminal domain of staphylococcus aureus zinc transport protein adca binds plasminogen and factor h in vitro |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8878332/ https://www.ncbi.nlm.nih.gov/pubmed/35215183 http://dx.doi.org/10.3390/pathogens11020240 |
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