The blueprint of the type-3 injectisome.
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The blueprint of the type-3 injectisome. / Kosarewicz, Agata; Königsmaier, Lisa; Marlovits, Thomas.
in: PHILOS T R SOC B, Jahrgang 367, Nr. 1592, 1592, 2012, S. 1140-1154.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - The blueprint of the type-3 injectisome.
AU - Kosarewicz, Agata
AU - Königsmaier, Lisa
AU - Marlovits, Thomas
PY - 2012
Y1 - 2012
N2 - Type-3 secretion systems are sophisticated syringe-like nanomachines present in many animal and plant Gram-negative pathogens. They are capable of translocating an arsenal of specific bacterial toxins (effector proteins) from the prokaryotic cytoplasm across the three biological membranes directly into the eukaryotic cytosol, some of which modulate host cell mechanisms for the benefit of the pathogen. They populate a particular biological niche, which is maintained by specific, pathogen-dependent effectors. In contrast, the needle complex, which is the central component of this specialized protein delivery machine, is structurally well-conserved. It is a large supramolecular cylindrical structure composed of multiple copies of a relatively small subset of proteins, is embedded in the bacterial membranes and protrudes from the pathogen's surface with a needle filament. A central channel traverses the entire needle complex, and serves as a hollow conduit for proteins destined to travel this secretion pathway. In the past few years, there has been a tremendous increase in an understanding on both the structural and the mechanistic level. This review will thus focus on new insights of this remarkable molecular machine.
AB - Type-3 secretion systems are sophisticated syringe-like nanomachines present in many animal and plant Gram-negative pathogens. They are capable of translocating an arsenal of specific bacterial toxins (effector proteins) from the prokaryotic cytoplasm across the three biological membranes directly into the eukaryotic cytosol, some of which modulate host cell mechanisms for the benefit of the pathogen. They populate a particular biological niche, which is maintained by specific, pathogen-dependent effectors. In contrast, the needle complex, which is the central component of this specialized protein delivery machine, is structurally well-conserved. It is a large supramolecular cylindrical structure composed of multiple copies of a relatively small subset of proteins, is embedded in the bacterial membranes and protrudes from the pathogen's surface with a needle filament. A central channel traverses the entire needle complex, and serves as a hollow conduit for proteins destined to travel this secretion pathway. In the past few years, there has been a tremendous increase in an understanding on both the structural and the mechanistic level. This review will thus focus on new insights of this remarkable molecular machine.
KW - Protein Transport
KW - Protein Structure, Tertiary
KW - Structure-Activity Relationship
KW - Host-Pathogen Interactions
KW - Bacterial Proteins/chemistry
KW - Bacterial Secretion Systems
KW - Gram-Negative Bacteria/chemistry/pathogenicity
KW - Gram-Negative Bacterial Infections/microbiology
KW - Membrane Proteins/chemistry
KW - Multiprotein Complexes/chemistry
KW - Protein Transport
KW - Protein Structure, Tertiary
KW - Structure-Activity Relationship
KW - Host-Pathogen Interactions
KW - Bacterial Proteins/chemistry
KW - Bacterial Secretion Systems
KW - Gram-Negative Bacteria/chemistry/pathogenicity
KW - Gram-Negative Bacterial Infections/microbiology
KW - Membrane Proteins/chemistry
KW - Multiprotein Complexes/chemistry
M3 - SCORING: Journal article
VL - 367
SP - 1140
EP - 1154
JO - PHILOS T R SOC B
JF - PHILOS T R SOC B
SN - 0962-8436
IS - 1592
M1 - 1592
ER -
