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Biosynthesis of a broad-spectrum nicotianamine-like metallophore in Staphylococcus aureus.

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Title: Biosynthesis of a broad-spectrum nicotianamine-like metallophore in Staphylococcus aureus.
Authors: Ghssein, Ghassan, Brutesco, Catherine, Ouerdane, Laurent, Fojcik, Clémentine, Izaute, Amélie, Shuanglong Wang, Hajjar, Christine, Lobinski, Ryszard, Lemaire, David, Richaud, Pierre, Voulhoux, Romé, Espaillat, Akbar, Cava, Felipe, Pignol, David, Borezée-Durant, Elise, Arnoux, Pascal
Source: Science (pre-March 2025). 5/27/2016, Vol. 352 Issue 6289, p1105-1109. 5p.
Subjects: Biosynthesis, Staphylococcus aureus, Nicotianamine, Histidine, Enzymes
Abstract: Metal acquisition is a vital microbial process in metal-scarce environments, such as inside a host. Using metabolomic exploration, targeted mutagenesis, and biochemical analysis, we discovered an operon in Staphylococcus aureus that encodes the different functions required for the biosynthesis and trafficking of a broad-spectrum metallophore related to plant nicotianamine (here called staphylopine). The biosynthesis of staphylopine reveals the association of three enzyme activities: a histidine racemase, an enzyme distantly related to nicotianamine synthase, and a staphylopine dehydrogenase belonging to the DUF2338 family. Staphylopine is involved in nickel, cobalt, zinc, copper, and iron acquisition, depending on the growth conditions. This biosynthetic pathway is conserved across other pathogens, thus underscoring the importance of this metal acquisition strategy in infection. [ABSTRACT FROM AUTHOR]
Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Psychology and Behavioral Sciences Collection
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  Data: Biosynthesis of a broad-spectrum nicotianamine-like metallophore in Staphylococcus aureus.
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  Data: <searchLink fieldCode="AR" term="%22Ghssein%2C+Ghassan%22">Ghssein, Ghassan</searchLink><br /><searchLink fieldCode="AR" term="%22Brutesco%2C+Catherine%22">Brutesco, Catherine</searchLink><br /><searchLink fieldCode="AR" term="%22Ouerdane%2C+Laurent%22">Ouerdane, Laurent</searchLink><br /><searchLink fieldCode="AR" term="%22Fojcik%2C+Clémentine%22">Fojcik, Clémentine</searchLink><br /><searchLink fieldCode="AR" term="%22Izaute%2C+Amélie%22">Izaute, Amélie</searchLink><br /><searchLink fieldCode="AR" term="%22Shuanglong+Wang%22">Shuanglong Wang</searchLink><br /><searchLink fieldCode="AR" term="%22Hajjar%2C+Christine%22">Hajjar, Christine</searchLink><br /><searchLink fieldCode="AR" term="%22Lobinski%2C+Ryszard%22">Lobinski, Ryszard</searchLink><br /><searchLink fieldCode="AR" term="%22Lemaire%2C+David%22">Lemaire, David</searchLink><br /><searchLink fieldCode="AR" term="%22Richaud%2C+Pierre%22">Richaud, Pierre</searchLink><br /><searchLink fieldCode="AR" term="%22Voulhoux%2C+Romé%22">Voulhoux, Romé</searchLink><br /><searchLink fieldCode="AR" term="%22Espaillat%2C+Akbar%22">Espaillat, Akbar</searchLink><br /><searchLink fieldCode="AR" term="%22Cava%2C+Felipe%22">Cava, Felipe</searchLink><br /><searchLink fieldCode="AR" term="%22Pignol%2C+David%22">Pignol, David</searchLink><br /><searchLink fieldCode="AR" term="%22Borezée-Durant%2C+Elise%22">Borezée-Durant, Elise</searchLink><br /><searchLink fieldCode="AR" term="%22Arnoux%2C+Pascal%22">Arnoux, Pascal</searchLink>
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  Data: <searchLink fieldCode="JN" term="%22Science+%28pre-March+2025%29%22">Science (pre-March 2025)</searchLink>. 5/27/2016, Vol. 352 Issue 6289, p1105-1109. 5p.
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  Data: <searchLink fieldCode="DE" term="%22Biosynthesis%22">Biosynthesis</searchLink><br /><searchLink fieldCode="DE" term="%22Staphylococcus+aureus%22">Staphylococcus aureus</searchLink><br /><searchLink fieldCode="DE" term="%22Nicotianamine%22">Nicotianamine</searchLink><br /><searchLink fieldCode="DE" term="%22Histidine%22">Histidine</searchLink><br /><searchLink fieldCode="DE" term="%22Enzymes%22">Enzymes</searchLink>
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  Data: Metal acquisition is a vital microbial process in metal-scarce environments, such as inside a host. Using metabolomic exploration, targeted mutagenesis, and biochemical analysis, we discovered an operon in Staphylococcus aureus that encodes the different functions required for the biosynthesis and trafficking of a broad-spectrum metallophore related to plant nicotianamine (here called staphylopine). The biosynthesis of staphylopine reveals the association of three enzyme activities: a histidine racemase, an enzyme distantly related to nicotianamine synthase, and a staphylopine dehydrogenase belonging to the DUF2338 family. Staphylopine is involved in nickel, cobalt, zinc, copper, and iron acquisition, depending on the growth conditions. This biosynthetic pathway is conserved across other pathogens, thus underscoring the importance of this metal acquisition strategy in infection. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=pbh&AN=115780822
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