Modulation of Host Cell Processes by T3SS Effectors

2018 ◽  
pp. 73-115 ◽  
Author(s):  
Avinash R. Shenoy ◽  
R. Christopher D. Furniss ◽  
Philippa J. Goddard ◽  
Abigail Clements
Keyword(s):  
Host Cell ◽  
Cell Processes

scholarly journals Toxoplasma gondii Development of Its Replicative Niche: in Its Host Cell and Beyond

2014 ◽  
Vol 13 (8) ◽  
pp. 965-976 ◽  
Author(s):  
Ira J. Blader ◽  
Anita A. Koshy
Keyword(s):  
Toxoplasma Gondii ◽  
Host Cell ◽  
Host Cells ◽  
Content Type ◽  
Obligate Intracellular ◽  
Cellular Processes ◽  
High Prevalence ◽  
Life Threatening ◽  
Cell Processes ◽  
Cellular Pathways

ABSTRACTIntracellular pathogens can replicate efficiently only after they manipulate and modify their host cells to create an environment conducive to replication. While diverse cellular pathways are targeted by different pathogens, metabolism, membrane and cytoskeletal architecture formation, and cell death are the three primary cellular processes that are modified by infections.Toxoplasma gondiiis an obligate intracellular protozoan that infects ∼30% of the world's population and causes severe and life-threatening disease in developing fetuses, in immune-comprised patients, and in certain otherwise healthy individuals who are primarily found in South America. The high prevalence ofToxoplasmain humans is in large part a result of its ability to modulate these three host cell processes. Here, we highlight recent work defining the mechanisms by whichToxoplasmainteracts with these processes. In addition, we hypothesize why some processes are modified not only in the infected host cell but also in neighboring uninfected cells.

Host cell processes to accomplish mechanical and non-circulative virus transmission

PROTOPLASMA ◽  
2011 ◽  
Vol 249 (3) ◽  
pp. 529-539 ◽  
Author(s):  
Aurélie Bak ◽  
Sarah L. Irons ◽  
Alexandre Martinière ◽  
Stéphane Blanc ◽  
Martin Drucker
Keyword(s):  
Host Cell ◽  
Virus Transmission ◽  
Cell Processes

Host-directed therapies targeting the tuberculosis granuloma stroma

2020 ◽  
Vol 78 (2) ◽  
Author(s):  
Elinor Hortle ◽  
Stefan H Oehlers
Keyword(s):  
Extracellular Matrix ◽  
Antimicrobial Resistance ◽  
Host Cell ◽  
Protective Immunity ◽  
Intracellular Survival ◽  
Granuloma Formation ◽  
Clinical Use ◽  
Innovative Research ◽  
Cell Processes ◽  
The Relationship

ABSTRACT Mycobacteria have co-evolved with their hosts resulting in pathogens adept at intracellular survival. Pathogenic mycobacteria actively manipulate infected macrophages to drive granuloma formation while subverting host cell processes to create a permissive niche. Granuloma residency confers phenotypic antimicrobial resistance by physically excluding or neutralising antibiotics. Host-directed therapies (HDTs) combat infection by restoring protective immunity and reducing immunopathology independent of pathogen antimicrobial resistance status. This review covers innovative research that has discovered ‘secondary’ symptoms of infection in the granuloma stroma are actually primary drivers of infection and that relieving these stromal pathologies with HDTs benefits the host. Advances in our understanding of the relationship between tuberculosis and the host vasculature, haemostatic system and extracellular matrix reorganisation are discussed. Preclinical and clinical use of HDTs against these stromal targets are summarised.

scholarly journals Hijacking and Use of Host Kinases by Chlamydiae

Pathogens ◽  
2020 ◽  
Vol 9 (12) ◽  
pp. 1034
Author(s):  
Prakash Sah ◽  
Erika I. Lutter
Keyword(s):  
Host Cell ◽  
Intracellular Pathogen ◽  
Host Proteins ◽  
Sexually Transmitted ◽  
Obligate Intracellular ◽  
Host Cell Apoptosis ◽  
Survival And Development ◽  
Causative Agents ◽  
Cell Processes ◽  
Obligate Intracellular Pathogen

Chlamydia species are causative agents of sexually transmitted infections, blinding trachoma, and animal infections with zoonotic potential. Being an obligate intracellular pathogen, Chlamydia relies on the host cell for its survival and development, subverting various host cell processes throughout the infection cycle. A key subset of host proteins utilized by Chlamydia include an assortment of host kinase signaling networks which are vital for many chlamydial processes including entry, nutrient acquisition, and suppression of host cell apoptosis. In this review, we summarize the recent advancements in our understanding of host kinase subversion by Chlamydia.

scholarly journals Of Microbes and Membranes: Pathogenic Subversion of Host Cell Processes

2008 ◽  
Vol 4 (6) ◽  
pp. 514-518 ◽  
Author(s):  
Jean Celli ◽  
Leigh A. Knodler
Keyword(s):  
Host Cell ◽  
Cell Processes

Pathogenic trickery: deception of host cell processes

2001 ◽  
Vol 2 (8) ◽  
pp. 578-588 ◽  
Author(s):  
Leigh A. Knodler ◽  
Jean Celli ◽  
B. Brett Finlay
Keyword(s):  
Host Cell ◽  
Cell Processes

scholarly journals Arcanobacterium haemolyticumUtilizes Both Phospholipase D and Arcanolysin To Mediate Its Uptake into Nonphagocytic Cells

2019 ◽  
Vol 87 (5) ◽  
Author(s):  
Patrick S. Gellings ◽  
David J. McGee
Keyword(s):  
Epithelial Cells ◽  
Host Cell ◽  
Phospholipase D ◽  
Actin Polymerization ◽  
Extracellular Calcium ◽  
Content Type ◽  
Biologically Relevant ◽  
Cell Processes ◽  
The Individual ◽  
Arcanobacterium Haemolyticum

ABSTRACTArcanobacterium haemolyticumis an emerging human pathogen that causes pharyngitis and wound infections. A few studies have suggested thatA. haemolyticumis able to induce its uptake into nonphagocytic epithelial cells, but the bacterial factors associated with host cell invasion and the host cell processes involved have yet to be studied. We investigated how twoA. haemolyticumvirulence factors, arcanolysin (ALN) and phospholipase D (PLD), affect the ability of the bacteria to adhere to and subsequently invade Detroit 562 pharyngeal epithelial cells. The sphingomyelinase activity of phospholipase D was necessary to increase bacterial adherence, while the absence of a functional arcanolysin had no effect onA. haemolyticumadherence but did lead to a decrease inA. haemolyticuminvasion into Detroit 562 cells. Because of the known roles of cholesterol-dependent cytolysins in disrupting calcium gradients and inducing F-actin-mediated bacterial internalization, we sought to determine whether ALN and PLD played a similar role in the ability ofA. haemolyticumto invade nonphagocytic cells. Elimination of extracellular calcium and inhibition of the Arp2/3 complex or F-actin polymerization also caused a decrease in the ability ofA. haemolyticumto invade Detroit 562 cells. Overall, our findings suggest thatA. haemolyticumutilizes phospholipase D primarily for adherence and utilizes arcanolysin primarily for invasion into Detroit 562 cells in a process dependent on extracellular calcium and F-actin polymerization. Our work marks the first insight into how the individual activities of arcanolysin and phospholipase D affectA. haemolyticumhost-pathogen interactions using the biologically relevant Detroit 562 cell line.

scholarly journals Alpha Enolase 1 Ubiquitination and Degradation Mediated by Ehrlichia chaffeensis TRP120 Disrupts Glycolytic Flux and Promotes Infection

Pathogens ◽  
2021 ◽  
Vol 10 (8) ◽  
pp. 962
Author(s):  
Bing Zhu ◽  
Jere W. McBride
Keyword(s):  
Host Cell ◽  
Ectopic Expression ◽  
Metabolic Reprogramming ◽  
Glycolytic Flux ◽  
Ehrlichia Chaffeensis ◽  
Direct Role ◽  
Cell Processes

Ehrlichia chaffeensis modulates numerous host cell processes, including gene transcription to promote infection of the mononuclear phagocyte. Modulation of these host cell processes is directed through E. chaffeensis effectors, including TRP120. We previously reported that TRP120 moonlights as a HECT E3 Ub ligase that ubiquitinates host cell transcription and fate regulators (PCGF5 and FBW7) to promote infection. In this study, we identified a novel TRP120 substrate and examined the relationship between TRP120 and α-enolase (ENO1), a metalloenzyme that catalyzes glycolytic pathway substrate dehydration. Immunofluorescence microscopy and coimmunoprecipitation demonstrated interaction between ENO1 and TRP120, and ubiquitination of ENO-1 by TRP120 was detected in vivo and in vitro. Further, ENO-1 degradation was observed during infection and was inhibited by the proteasomal inhibitor bortezomib. A direct role of TRP120 Ub ligase activity in ENO-1 degradation was demonstrated and confirmed by ectopic expression of TRP120 HECT Ub ligase catalytic site mutant. siRNA knockdown of ENO-1 coincided with increased E. chaffeensis infection and ENO-1 knockdown disrupted glycolytic flux by decreasing the levels of pyruvate and lactate that may contribute to changes in host cell metabolism that promote infection. In addition, we elucidated a functional role of TRP120 auto-ubiquitination as an activating event that facilitates the recruitment of the UbcH5 E2 ubiquitin-conjugating enzyme. This investigation further expands the repertoire of TRP120 substrates and extends the potential role of TRP120 Ub ligase in infection to include metabolic reprogramming.

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