| Title | : | The Actin Cytoskeleton and Bacterial Infection |
| Author | : | Hans Georg Mannherz |
| Language | : | en |
| Rating | : | 4.90 out of 5 stars |
| Type | : | PDF, ePub, Kindle |
| Uploaded | : | Apr 06, 2021 |
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[PDF] دانلود کتاب The Actin Cytoskeleton And Bacterial
Hans Georg Mannherz Editor The Actin Cytoskeleton and
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[Pathogenicity of bacteria and the actin cytoskeleton
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The Actin Cytoskeleton and Actin-Based Motility
Bacterial factors either modify actin directly as the main component of this part of the cytoskeleton or functionally subvert regulatory or signalling proteins terminating at the actin cytoskeleton.
S-(3,4-dichlorobenzyl)isothiourea (a22) disrupts the actin cytoskeleton of bacteria, causing defects of morphology and chromosome segregation. Previous studies have suggested that the actin homologue mreb itself is the target of a22, but there has been no direct observation of a22 binding to mreb and no mechanistic explanation of its mode of action.
Probably due to its conserved nature and abundance, actin and its regulating factors have emerged as prefered targets of bacterial toxins and effectors, which subvert the host actin cytoskeleton to serve bacterial needs.
Disorganization of the actin cytoskeleton induces alterations of intestinal barrier functions, leading to passage of fluids into the intestinal lumen, but to a lesser.
17 oct 2017 bacteria do possess cytoskeletons made of proteins which resemble the actin and tubulin familiar to eukaryotic cell biologists.
Keywords actin; adp-ribosylation; bacterial protein toxins; cytoskeleton; rho gtpases; thymosin-b4.
The proteins comprising the cytoskeleton can be divided into three classes: microfilaments, intermediate filaments, and microtubules. Microfilaments, also known as actin filaments, form by polymerization of a protein called actin. Individual actin molecules combine to form a long, thin helical chain called a microfilament.
Abstract cytoskeletal proteins are important mediators of cellular organization in both eukaryotes and bacteria. In the past, cytoskeletal studies have largely focused on three major cytoskeletal families, namely the eukaryotic actin, tubulin, and intermediate filament (if) proteins and their bacterial homologs mreb, ftsz, and crescentin.
Although actin is the major cytoskeletal filament exploited by pathogens, they also during zipper entry, bacterial surface proteins interact with host membrane.
Actin condensation was observed directly beneath the adherent bacteria in epithelial cells (fig. 3, a and b), although attached bacteria not associated with actin condensation was also observed.
The enteric bacterial pathogens listeria monocytogenes (listeria) and enteropathogenic escherichia coli (epec) remodel the eukaryotic actin cytoskeleton during their disease processes. Listeria generate slender actin‐rich comet/rocket tails to move intracellularly, and later, finger‐like membrane protrusions to spread amongst host cells.
Bacteria that modify the cytoskeleton in order to invade epithelial cells produce a number of effectors that can either interact directly with actin or with regulators of actin filament formation.
Microfilaments are filamentous structures of the cytoskeleton and are made up of actin monomers (f-actin). Here, globular g-actin monomers, commonly known as g-actin, polymerize to form filaments of actin polymers (f-actin). Ultimately, each strand of the filament (microfilament) is composed of two f-actin coiled in a helical fashion.
Actin is one of the most abundant proteins in any eukaryotic cell and an indispensable component of the cytoskeleton. In mammalian organisms, six highly conserved actin isoforms can be distinguished, which differ by only a few amino acids.
The actin cytoskeleton is required for the maintenance of the cell shape and viability of bacteria.
Some bacterial pathogens, including listeria monocytogenes and shigella flexneri, polymerize the host actin cytoskeleton for actin-based motility and intracellular spreading. Proteins involved in actin-based motility have been linked to autophagy.
The role of the actin cytoskeleton in plant/pathogen interactions. Jeff chang in the botany and plant pathology department on “the role of the actin cytoskeleton in plant/bacterial interactions.
نام کتاب: the actin cytoskeleton and bacterial infection نویسنده: hans georg mannherz ویرایش: 1 سال انتشار: 2017 فرمت: pdf تعداد صفحه: 242 انتشارات: springer international publishing.
Intracellular bacterial pathogens remodel and exploit the host cell environment to support their survival and growth. A common target of bacterial pathogens is the host cell actin cytoskeleton, which is a dynamic system of filaments that is central to shape determination, movement, phagocytosis and intracellular trafficking.
A defining feature of bacterial cells has long been thought to be the lack of a cytoskeleton, which in eukaryotes is indispensable for cell division, for the maintenance of cell shape, and numerous other functions. The cytoskeleton is composed of actin filaments, microtubules, and intermediate filaments.
This volume describes the mechanisms which bacteria have created to secure their survival, proliferation and dissemination by subverting the actin cytoskeleton.
(f) rescue of the developmental defect through expression of costars or mcostars in re-knockout cosa– cells. Photographs were taken after 5 days or 36 hours of development on bacterial lawn or non-nutrient agar, respectively.
Crenactin is closer in sequence to eukaryotic f-actin than any other bacterial or archaeal protein. Here we show that crenactin forms double helical filaments that are very closely related to f-actin, the structure that all bona fide actins form in eukaryotes.
The cytoskeleton probably has its origins in bacterial and/or archaeal ancestry. There are ancient relatives to both actin and tubulin in bacterial systems. In bacteria, the mreb protein and the parm protein are believed to be early ancestors to actin. Mreb functions in maintaining cell shape and parm functions in plasmid (dna) partitioning.
Until the early 1990s, cytoskeletal proteins were believed to be the hallmarks of eukaryotic cells. However, in the last three decades, the discovery of bacterial.
The activity of multiple proteins that participate in bacterial invasion. Here, we review data that sup-port a role for iqgap1 in infectious disease via its ability to regulate the actin cytoskeleton. In addi-tion, we explore other mechanisms by which iqgap1 may be exploited by microbial pathogens.
The actin cytoskeleton—a collection of actin filaments with their accessory and regulatory proteins—is the primary force-generating machinery in the cell. It can produce pushing (protrusive) forces through coordinated polymerization of multiple actin filaments or pulling (contractile) forces through sliding actin filaments along bipolar.
1 aug 2000 immediately on contact, salmonella delivers a number of bacterial effector proteins into the host cell cytosol through the function of a specialized.
Numerous bacterial toxins recognize the actin cytoskeleton as a target. The clostridial binary toxins (iota and c2 families) adp-ribosylate the actin monomers.
Known actin associations of the spectrin cytoskeleton, together with the dramatic reorganization of the host cell plasma membrane and related cytoskeletal networks during various enteric bacterial infections, suggest that the spectrin cytoskeletal system may also be a target of these pathogens.
Some bacterial toxins catalyze the covalent modification of actin or the rho gtpases, which are involved in the control of the actin cytoskeleton. Other bacteria produce toxins that act as guanine nucleotide exchange factors or gtpase-activating proteins to modulate the nucleotide state of the rho gtpases.
For successful infection and replication, many pathogens hijack the cytoskeleton using effector proteins introduced into the host cytosol by specialized secretion systems. A subset of effectors contains eukaryotic-like motifs that mimic host proteins to exploit signaling and modify specific cytoskeletal components such as actin and microtubules.
Abstract bacterial pathogens utilize several strategies to modulate the organization of the actin cytoskeleton.
The actin cytoskeleton is one of the major targets of bacterial protein toxins. The family of binary actin-adp-ribosylating toxins, including.
Provides an up-to-date handbook on the organisation and dynamics of actin and the interaction with its companions presents the cutting-edge view on the role of the actin cytoskeleton in signalling pathways; features the hot-topic research on the activity of toxins, viral and bacterial pathogens on the actin cytoskeleton.
Microinjection and growth of bacteria in the cytosol of mammalian host cells.
Thus, the importance of the actin cytoskeleton for eukaryotic host physiology from cell movement, cell-to-cell adherence, endocytosis, vesicle trafficking, and cell signaling, among others, has provided pathogenic bacteria with a plethora of opportunistic chances to be exploited.
These actin filaments are constantly growing and shrinking, and this dynamic behavior allows a network of actin to generate enough force for cell motility. The intracellular bacterial pathogen listeria monocytogenes uses actin polymerization to propel itself through the cytoplasm and to invade other cells.
Until the mid 1990s it was thought that bacteria lack a cytoskeleton it was thought that homologues of actin and tubulin (forming f-actin and microtubules in eukaryotes, respectively) are missing from all bacteria and archaea.
Particular, 1) the structure of actin was resolved from crystals in the absence of cocrystallized actin binding proteins (abps), 2) the prokaryotic ancestral gene of actin was crystallized and its function as a bacterial cytoskeleton was revealed, and 3) the structure of the arp2/3 complex was described for the first time.
Host (human) septins play a role in bacterial pathogenesis and in host defense mechanisms, mainly, autophagy. Although actin is the most commonly exploited cytoskeletal protein by many bacterial pathogens, septins, which are unique cytoskeletal components, are also found to co-localize with actin at sites of infection.
Ipac induces changes in the actin cytoskeleton, characteristic of active cdc42 ipaa promotes the cytoskeletal rearrangements necessary for bacterial entry.
It is therefore not surprising that the actin cytoskeleton is one of the main targets of bacterial protein toxins, and thus of major importance for the host–pathogen interaction. Bacteria have developed numerous toxins and effectors to target the actin cytoskeleton.
The symbiotic role of the actin filament cytoskeleton legumes interact with soil-borne bacteria (rhizobia), thus developing a symbiotic association that allows atmospheric nitrogen fixation inside specialized plant organs called root nodules (gage, 2004).
Abstract bacterial pathogens utilize several strategies to modulate the organization of the actin cytoskeleton. Some bacterial toxins catalyze the covalent modification of actin or the rho gtpases, which are involved in the control of the actin cytoskeleton. Other bacteria produce toxins that act as guanine nucleotide exchange factors or gtpase-activating proteins to modulate the nucleotide.
Fig1: bacteria exploit actin and microtubules to promote invasion and adherence. (a) zippering bacteria express an invasion protein on their surface, which binds to a host receptor and initiates actin-dependent phagocytosis.
The bacterial proteins mreb, mbl, and parm display the structural and dynamic properties of eukaryotic actin [10]. Amongst these proteins, mreb is the most homologous to actin in terms of primary sequence, structure, and size [11,12]. The most conserved region of this actin-superfamily is the atpase domain.
The bacterial cytoskeleton contains proteins that are homologous in structure to eukaryotic actin and tubulin and also other protein classes, possibly including intermediate filaments, suggesting that the eukaryotic cytoskeleton can trace its evolutionary origins to bacterial and, more closely, to archaeal.
In mammals six tissue-specific isoforms assemble to the actin containing microfilaments, which are often organized into bundles or higher ordered networks. The highly dynamic behaviour of the actin cytoskeleton is regulated by a large number of actin binding proteins (abp).
For years, the actin cytoskeleton has been assumed to play a role in plant innate immunity against fungi and oomycetes, based largely on static images and pharmacological studies. To date, however, there is little evidence that the host-cell actin cytoskeleton participates in responses to phytopathogenic bacteria.
Watch this short time- lapse video of the cell capturing two bacteria.
The dynamic prokaryotic actin-like cytoskeleton is thought to serve as a central organizer for the targeting and accurate positioning of proteins and nucleoprotein.
An interesting irony is that roles of tubulin and actin have somewhat switched from bacteria to eukaryotes. Ftsz forms the cytokinetic ring in bacteria, whereas actin provides the major cytoskeletal framework in eukaryotes. Some bacterial (plasmid) actins function for nucleoid segregation, a role performed by microtubules in eukaryotes.
(microtubules, and, forthcoming: intermediate filaments, actin filaments, and all cells, except those of most bacteria, contain components of the cytoskeleton.
The dynamic prokaryotic actin-like cytoskeleton is thought to serve as a central organizer for the targeting and accurate positioning of proteins and nucleoprotein complexes, thereby (and by analogy to the eukaryotic cytoskeleton) spatially and temporally controlling macromolecular trafficking in bacterial cells.
The actin cytoskeleton in the cellular context while much of actin's fame derives from studies of metazoan muscle actin/myosin complex, nonmuscle actin participates in a range of essential processes of eukaryotic cell morphogenesis, in motility of (nonmuscle) metazoan and amoeboid cells and in intracellular transport.
Some bacterial pathogens enter mammalian cells by on the host actin cytoskeleton and on its capacity to be by bacteria to stimulate actin rearrangements.
From narrowest to widest, they are the microfilaments (actin filaments), intermediate filaments, and microtubules. They provide rigidity and shape to the cell and facilitate cellular movements.
The actin cytoskeleton rearrangements that facilitate bacterial entry (286).
Although actin is the major cytoskeletal filament exploited by pathogens, they also manipulate microtubules, microfilaments and septins for survival within the host. Pathogens achieve control over the host cytoskeletal machinery through effector proteins that modulate cellular regulators such as the small rho-gtpases.
Bacterial factors either modify actin directly as the main component of this part of the cytoskeleton or functionally subvert regulatory or signalling proteins terminating at the actin cytoskeleton. In short, this volume provides an overview of the various tricks bacteria have evolved to “act on actin” in order to hijack this essential host.
The actin-like mreb protein family is believed to form a filamentous network within bacterial cells, coordinating the movement of chromosomes or other macromolecules, thus playing a role analogous.
Bacterial toxins modifying the actin cytoskeleton summary numerous bacterial toxins recognize the actin cytoskeleton as a target. The clostridial binary toxins (iota and c2 families) adp-ribosylate the actin monomers causing the dissociation of the actin filaments.
This chapter focuses on the bacterial manipulation of the host cell actin cytoskeleton. The first is pathogen establishment of infection/invasion, explaining.
Several unrelated intracellular bacteria use actin filament assembly for propulsion: listeria, shigella and richettsia. In the cytoplasm of an infected host cell, the bacteria assemble a halo of endogenous actin filaments and actin-binding proteins.
Actin system of eukaryotic cells creates the driving force for alteration of the phagocytic cytoplasmatic membrane shape, which is needed for cell movement in the space and for microorganism capturing. Manipulation by actin cytoskeleton mediated through specialized bacterial products can promote proliferation of bacteria in the host.
How cells create and maintain a defined shape is a fundamental problem from bacteria to humans. The eukaryotic cytoskeleton, which consists of microtubules, actin microfilaments, and intermediate filaments, determines the various cell shapes of higher organisms. A multitude of cell shapes is also encountered in the prokaryotic world.
Various bacterial protein toxins and effectors target the actin cytoskeleton. Least three groups of toxins/effectors can be identified, which directly modify actin molecules. One group of toxins/effectors causes adp-ribosylation of actin at arginine-177, thereby inhibiting actin polymerization.
6 sep 2001 actin is a major component of the cytoskeleton in yeast, plant and animal cells, but when did it evolve? the discovery of a bacterial protein that.
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