Limits...
An update on the transport and metabolism of iron in Listeria monocytogenes: the role of proteins involved in pathogenicity.

Lechowicz J, Krawczyk-Balska A - Biometals (2015)

Bottom Line: In the human body it infects many different cell types, where it lives intracellularly, however it may also temporarily live extracellularly.In this review, data about the mechanisms of transport, metabolism and regulation of iron, including recent findings in these areas, are summarized with focus on the importance of these mechanisms for the virulence of L. monocytogenes.Furthermore, some of the proteins involved in iron homeostasis like Fri and FrvA seem to deserve special attention due to their potential use in the development of new therapeutic antilisterial strategies.

View Article: PubMed Central - PubMed

Affiliation: Department of Applied Microbiology, Faculty of Biology, University of Warsaw, Miecznikowa 1, 02-096, Warsaw, Poland.

ABSTRACT
Listeria monocytogenes is a Gram-positive bacterium that causes a rare but severe human disease with high mortality rate. The microorganism is widespread in the natural environment where it shows a saprophytic lifestyle. In the human body it infects many different cell types, where it lives intracellularly, however it may also temporarily live extracellularly. The ability to survive and grow in such diverse niches suggests that this bacterium has a wide range of mechanisms for both the acquisition of various sources of iron and effective management of this microelement. In this review, data about the mechanisms of transport, metabolism and regulation of iron, including recent findings in these areas, are summarized with focus on the importance of these mechanisms for the virulence of L. monocytogenes. These data indicate the key role of haem transport and maintenance of intracellular iron homeostasis for the pathogenesis of L. monocytogenes. Furthermore, some of the proteins involved in iron homeostasis like Fri and FrvA seem to deserve special attention due to their potential use in the development of new therapeutic antilisterial strategies.

No MeSH data available.


Related in: MedlinePlus

Systems of iron transport in L. monocytogenesa Transport of hydroxamate siderophores. The transport system consists of FhuD receptor protein, membrane permeases FhuB and FhuG and protein FhuC which is the ATP binding component of the system. b Transport of haem. Sortase-independent transport of haem involves the HupD receptor, membrane permease HupG and protein HupC, which is the ATP binding component of the system. Sortase-dependent transport of haem takes place under conditions of low extracellular concentrations of haem (<50 nM). In this case, in addition to proteins HupDCG, the process of haem acquisition involves proteins Hbp1 and Hbp2, which are responsible for capturing porphyrin from the environment. c Reductive iron uptake. In the proposed model FepB is translocated across the membrane by Tat translocon. At extracellular surface of membrane FepB acts as the ferric reductase enzyme. After reduction, ferrous ions are bound by the iron binding lipoprotein FepA, and then are transported into the cell by ferrous permease FepC. d Export of haem. Haem present in excess is exported to the external environment most probably with the involvement of protein FrvA. Catabolic pathway of exogenous haem in L. monocytogenes cells is also shown. Haem acquired from the external environment is degraded by Isd-LmHde enzyme to free iron and biliverdin or, would be degraded by IsgG protein to staphylobilin and Fe2+
© Copyright Policy - OpenAccess
Related In: Results  -  Collection


getmorefigures.php?uid=PMC4481299&req=5

Fig1: Systems of iron transport in L. monocytogenesa Transport of hydroxamate siderophores. The transport system consists of FhuD receptor protein, membrane permeases FhuB and FhuG and protein FhuC which is the ATP binding component of the system. b Transport of haem. Sortase-independent transport of haem involves the HupD receptor, membrane permease HupG and protein HupC, which is the ATP binding component of the system. Sortase-dependent transport of haem takes place under conditions of low extracellular concentrations of haem (<50 nM). In this case, in addition to proteins HupDCG, the process of haem acquisition involves proteins Hbp1 and Hbp2, which are responsible for capturing porphyrin from the environment. c Reductive iron uptake. In the proposed model FepB is translocated across the membrane by Tat translocon. At extracellular surface of membrane FepB acts as the ferric reductase enzyme. After reduction, ferrous ions are bound by the iron binding lipoprotein FepA, and then are transported into the cell by ferrous permease FepC. d Export of haem. Haem present in excess is exported to the external environment most probably with the involvement of protein FrvA. Catabolic pathway of exogenous haem in L. monocytogenes cells is also shown. Haem acquired from the external environment is degraded by Isd-LmHde enzyme to free iron and biliverdin or, would be degraded by IsgG protein to staphylobilin and Fe2+

Mentions: In summary, despite L. monocytogenes being able to use a wide range of compounds as a source of iron, transport systems for only a few of them have so far been identified. The current state of knowledge on transport systems involved in the acquisition of iron is schematically shown in Fig. 1a, b, c.Fig. 1


An update on the transport and metabolism of iron in Listeria monocytogenes: the role of proteins involved in pathogenicity.

Lechowicz J, Krawczyk-Balska A - Biometals (2015)

Systems of iron transport in L. monocytogenesa Transport of hydroxamate siderophores. The transport system consists of FhuD receptor protein, membrane permeases FhuB and FhuG and protein FhuC which is the ATP binding component of the system. b Transport of haem. Sortase-independent transport of haem involves the HupD receptor, membrane permease HupG and protein HupC, which is the ATP binding component of the system. Sortase-dependent transport of haem takes place under conditions of low extracellular concentrations of haem (<50 nM). In this case, in addition to proteins HupDCG, the process of haem acquisition involves proteins Hbp1 and Hbp2, which are responsible for capturing porphyrin from the environment. c Reductive iron uptake. In the proposed model FepB is translocated across the membrane by Tat translocon. At extracellular surface of membrane FepB acts as the ferric reductase enzyme. After reduction, ferrous ions are bound by the iron binding lipoprotein FepA, and then are transported into the cell by ferrous permease FepC. d Export of haem. Haem present in excess is exported to the external environment most probably with the involvement of protein FrvA. Catabolic pathway of exogenous haem in L. monocytogenes cells is also shown. Haem acquired from the external environment is degraded by Isd-LmHde enzyme to free iron and biliverdin or, would be degraded by IsgG protein to staphylobilin and Fe2+
© Copyright Policy - OpenAccess
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4481299&req=5

Fig1: Systems of iron transport in L. monocytogenesa Transport of hydroxamate siderophores. The transport system consists of FhuD receptor protein, membrane permeases FhuB and FhuG and protein FhuC which is the ATP binding component of the system. b Transport of haem. Sortase-independent transport of haem involves the HupD receptor, membrane permease HupG and protein HupC, which is the ATP binding component of the system. Sortase-dependent transport of haem takes place under conditions of low extracellular concentrations of haem (<50 nM). In this case, in addition to proteins HupDCG, the process of haem acquisition involves proteins Hbp1 and Hbp2, which are responsible for capturing porphyrin from the environment. c Reductive iron uptake. In the proposed model FepB is translocated across the membrane by Tat translocon. At extracellular surface of membrane FepB acts as the ferric reductase enzyme. After reduction, ferrous ions are bound by the iron binding lipoprotein FepA, and then are transported into the cell by ferrous permease FepC. d Export of haem. Haem present in excess is exported to the external environment most probably with the involvement of protein FrvA. Catabolic pathway of exogenous haem in L. monocytogenes cells is also shown. Haem acquired from the external environment is degraded by Isd-LmHde enzyme to free iron and biliverdin or, would be degraded by IsgG protein to staphylobilin and Fe2+
Mentions: In summary, despite L. monocytogenes being able to use a wide range of compounds as a source of iron, transport systems for only a few of them have so far been identified. The current state of knowledge on transport systems involved in the acquisition of iron is schematically shown in Fig. 1a, b, c.Fig. 1

Bottom Line: In the human body it infects many different cell types, where it lives intracellularly, however it may also temporarily live extracellularly.In this review, data about the mechanisms of transport, metabolism and regulation of iron, including recent findings in these areas, are summarized with focus on the importance of these mechanisms for the virulence of L. monocytogenes.Furthermore, some of the proteins involved in iron homeostasis like Fri and FrvA seem to deserve special attention due to their potential use in the development of new therapeutic antilisterial strategies.

View Article: PubMed Central - PubMed

Affiliation: Department of Applied Microbiology, Faculty of Biology, University of Warsaw, Miecznikowa 1, 02-096, Warsaw, Poland.

ABSTRACT
Listeria monocytogenes is a Gram-positive bacterium that causes a rare but severe human disease with high mortality rate. The microorganism is widespread in the natural environment where it shows a saprophytic lifestyle. In the human body it infects many different cell types, where it lives intracellularly, however it may also temporarily live extracellularly. The ability to survive and grow in such diverse niches suggests that this bacterium has a wide range of mechanisms for both the acquisition of various sources of iron and effective management of this microelement. In this review, data about the mechanisms of transport, metabolism and regulation of iron, including recent findings in these areas, are summarized with focus on the importance of these mechanisms for the virulence of L. monocytogenes. These data indicate the key role of haem transport and maintenance of intracellular iron homeostasis for the pathogenesis of L. monocytogenes. Furthermore, some of the proteins involved in iron homeostasis like Fri and FrvA seem to deserve special attention due to their potential use in the development of new therapeutic antilisterial strategies.

No MeSH data available.


Related in: MedlinePlus