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Book ; Online: Advances in Aspergillus fumigatus pathobiology

Steinbach, William J. / Juvvadi, Praveen R. / Lamoth, Frederic

2016

Abstract: Aspergillus fumigatus is a human fungal pathogen that causes invasive aspergillosis (IA), a major infectious cause of death in the expanding population of immunocompromised individuals such as cancer patients and transplant recipients. The mortality of ... ...

Abstract	Aspergillus fumigatus is a human fungal pathogen that causes invasive aspergillosis (IA), a major infectious cause of death in the expanding population of immunocompromised individuals such as cancer patients and transplant recipients. The mortality of IA remains high (30-70%) and emerging resistance to triazoles, the first-line antifungal drug class, is of particular concern. Second-line therapies for IA are limited by their toxicity (polyenes) or their lack of fungicidal activity (echinocandins). Identification of novel antifungal targets is an urgent need for improving the outcome of IA. A. fumigatus is a filamentous fungus exhibiting a complex developmental cycle and elaborated mechanisms of adaptation to allow the initiation and progression of infection in the human host. The fungal cell wall, with its unique and dynamic structure, is crucial for protecting cell integrity and evading the host immune system, also contributing to biofilm formation and virulence, and thus representing an ideal antifungal target. The emergence of azole resistance implies various and complex mechanisms that need to be further elucidated. Other important processes, such as biosynthetic pathways and toxin/metabolite production are important for fungal survival and propagation in the host environment, ultimately leading to disease. Moreover, the host immune response is a determinant factor in influencing the course of infection. The objective of this topic issue is to provide an overview of the recent advances in our understanding of A. fumigatus pathobiology and of IA pathogenesis to outline future research
Keywords	Microbiology ; Science (General)
Size	1 electronic resource (109 p.)
Publisher	Frontiers Media SA
Document type	Book ; Online
Note	English ; Open Access
HBZ-ID	HT020091212
ISBN	9782889197897 ; 2889197891
Database	ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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Article ; Online: Balancing iron and calcium: Flavin carrier family proteins in Aspergillus fumigatus virulence.

Juvvadi, Praveen R

Virulence

2016 Volume 8, Issue 6, Page(s) 621–624

MeSH term(s)	Aspergillosis ; Aspergillus fumigatus ; Calcium ; Carrier Proteins ; Flavins ; Fungal Proteins ; Iron ; Virulence
Chemical Substances	Carrier Proteins ; Flavins ; Fungal Proteins ; Iron (E1UOL152H7) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2016-11-07
Publishing country	United States
Document type	Editorial ; Comment
ZDB-ID	2657572-3
ISSN	2150-5608 ; 2150-5594
ISSN (online)	2150-5608
ISSN	2150-5594
DOI	10.1080/21505594.2016.1257459
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Calcineurin Inhibitor CN585 Exhibits Off-Target Effects in the Human Fungal Pathogen

Juvvadi, Praveen R / Bobay, Benjamin G / Cole, D Christopher / Awwa, Monaf / Steinbach, William J

Journal of fungi (Basel, Switzerland)

2022 Volume 8, Issue 12

Abstract: Calcineurin (CN) is an attractive antifungal target as it is critical for growth, stress response, drug resistance, and virulence in fungal pathogens. The immunosuppressive drugs, tacrolimus (FK506) and cyclosporin A (CsA), are fungistatic and ... ...

Abstract	Calcineurin (CN) is an attractive antifungal target as it is critical for growth, stress response, drug resistance, and virulence in fungal pathogens. The immunosuppressive drugs, tacrolimus (FK506) and cyclosporin A (CsA), are fungistatic and specifically inhibit CN through binding to their respective immunophilins, FK506-binding protein (FKBP12), and cyclophilin (CypA). We are focused on CN structure-based approaches for the development of non-immunosuppressive FK506 analogs as antifungal therapeutics. Here, we examined the effect of the novel CN inhibitor, CN585, on the growth of the human pathogen
Language	English
Publishing date	2022-12-07
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2784229-0
ISSN	2309-608X ; 2309-608X
ISSN (online)	2309-608X
ISSN	2309-608X
DOI	10.3390/jof8121281
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: The class V myosin interactome of the human pathogen Aspergillus fumigatus reveals novel interactions with COPII vesicle transport proteins.

Renshaw, Hilary / Juvvadi, Praveen R / Cole, D Christopher / Steinbach, William J

Biochemical and biophysical research communications

2020 Volume 527, Issue 1, Page(s) 232–237

Abstract: The human fungal pathogen Aspergillus fumigatus causes life-threatening invasive aspergillosis in immunocompromised individuals. Adaptation to the host environment is integral to survival of A. fumigatus and requires the coordination of short- and long- ... ...

Abstract	The human fungal pathogen Aspergillus fumigatus causes life-threatening invasive aspergillosis in immunocompromised individuals. Adaptation to the host environment is integral to survival of A. fumigatus and requires the coordination of short- and long-distance vesicular transport to move essential components throughout the fungus. We previously reported the importance of MyoE, the only class V myosin, for hyphal growth and virulence of A. fumigatus. Class V myosins are actin-based, cargo-carrying motor proteins that contain unique binding sites for specific cargo. Specific cargo carried by myosin V has not been identified in any fungus, and previous studies have only identified single components that interact with class V myosins. Here we utilized a mass spectrometry-based whole proteomic approach to identify MyoE interacting proteins in A. fumigatus for the first time. Several proteins previously shown to interact with myosin V through physical and genetic approaches were confirmed, validating our proteomic analysis. Importantly, we identified novel MyoE-interacting proteins, including members of the cytoskeleton network, cell wall synthesis, calcium signaling and a group of coat protein complex II (COPII) proteins involved in the endoplasmic reticulum (ER) to Golgi transport. Furthermore, we analyzed the localization patterns of the COPII proteins, UsoA (Uso1), SrgE (Sec31), and SrgF (Sec23), which suggested a potential role for MyoE in ER to Golgi trafficking.
MeSH term(s)	Aspergillus fumigatus/chemistry ; Biological Transport ; COP-Coated Vesicles/chemistry ; COP-Coated Vesicles/metabolism ; Humans ; Microscopy, Fluorescence ; Myosin Type V/chemistry ; Myosin Type V/isolation & purification ; Myosin Type V/metabolism
Chemical Substances	Myosin Type V (EC 3.6.1.-)
Language	English
Publishing date	2020-05-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2020.04.111
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: The class V myosin interactome of the human pathogen Aspergillus fumigatus reveals novel interactions with COPII vesicle transport proteins

Renshaw, Hilary / Juvvadi, Praveen R / Cole, D. Christopher / Steinbach, William J

Biochemical and biophysical research communications. 2020 June 18, v. 527, no. 1

2020

Abstract	The human fungal pathogen Aspergillus fumigatus causes life-threatening invasive aspergillosis in immunocompromised individuals. Adaptation to the host environment is integral to survival of A. fumigatus and requires the coordination of short- and long-distance vesicular transport to move essential components throughout the fungus. We previously reported the importance of MyoE, the only class V myosin, for hyphal growth and virulence of A. fumigatus. Class V myosins are actin-based, cargo-carrying motor proteins that contain unique binding sites for specific cargo. Specific cargo carried by myosin V has not been identified in any fungus, and previous studies have only identified single components that interact with class V myosins. Here we utilized a mass spectrometry-based whole proteomic approach to identify MyoE interacting proteins in A. fumigatus for the first time. Several proteins previously shown to interact with myosin V through physical and genetic approaches were confirmed, validating our proteomic analysis. Importantly, we identified novel MyoE-interacting proteins, including members of the cytoskeleton network, cell wall synthesis, calcium signaling and a group of coat protein complex II (COPII) proteins involved in the endoplasmic reticulum (ER) to Golgi transport. Furthermore, we analyzed the localization patterns of the COPII proteins, UsoA (Uso1), SrgE (Sec31), and SrgF (Sec23), which suggested a potential role for MyoE in ER to Golgi trafficking.
Keywords	Aspergillus fumigatus ; animal pathogenic fungi ; aspergillosis ; calcium ; cell walls ; coat proteins ; cytoskeleton ; endoplasmic reticulum ; hyphae ; mass spectrometry ; myosin ; physiological transport ; proteomics ; research ; virulence
Language	English
Dates of publication	2020-0618
Size	p. 232-237.
Publishing place	Elsevier Inc.
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2020.04.111
Database	NAL-Catalogue (AGRICOLA)

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Article: Calcineurin Orchestrates Hyphal Growth, Septation, Drug Resistance and Pathogenesis of Aspergillus fumigatus: Where Do We Go from Here?

Juvvadi, Praveen R / Steinbach, William J

Pathogens (Basel, Switzerland)

2015 Volume 4, Issue 4, Page(s) 883–893

Abstract: Studies on fungal pathogens belonging to the ascomycota phylum are critical given the ubiquity and frequency with which these fungi cause infections in humans. Among these species, Aspergillus fumigatus causes invasive aspergillosis, a leading cause of ... ...

Abstract	Studies on fungal pathogens belonging to the ascomycota phylum are critical given the ubiquity and frequency with which these fungi cause infections in humans. Among these species, Aspergillus fumigatus causes invasive aspergillosis, a leading cause of death in immunocompromised patients. Fundamental to A. fumigatus pathogenesis is hyphal growth. However, the precise mechanisms underlying hyphal growth and virulence are poorly understood. Over the past 10 years, our research towards the identification of molecular targets responsible for hyphal growth, drug resistance and virulence led to the elucidation of calcineurin as a key signaling molecule governing these processes. In this review, we summarize our salient findings on the significance of calcineurin for hyphal growth and septation in A. fumigatus and propose future perspectives on exploiting this pathway for designing new fungal-specific therapeutics.
Language	English
Publishing date	2015-12-16
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2695572-6
ISSN	2076-0817
ISSN	2076-0817
DOI	10.3390/pathogens4040883
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Article: Enhanced fungal specificity and

Rivera, Angela / Lim, Won Young / Park, Eunchong / Dome, Patrick A / Hoy, Michael J / Spasojevic, Ivan / Sun, Sheng / Averette, Anna Floyd / Pina-Oviedo, Sergio / Juvvadi, Praveen R / Steinbach, William J / Ciofani, Maria / Hong, Jiyong / Heitman, Joseph

bioRxiv : the preprint server for biology

2023

Abstract: Fungal infections are of mounting global concern, and the current limited treatment arsenal poses challenges when treating such infections. In particular, infections by : Importance: Fungal infections cause significant morbidity and mortality globally. ...

Abstract	Fungal infections are of mounting global concern, and the current limited treatment arsenal poses challenges when treating such infections. In particular, infections by Importance: Fungal infections cause significant morbidity and mortality globally. The therapeutic armamentarium against these infections is limited and development of antifungal drugs has been hindered by the evolutionary conservation between fungi and the human host. With rising resistance to the current antifungal arsenal and an increasing at-risk population, there is an urgent need for the development of new antifungal compounds. The FK520 analogs described in this study display potent antifungal activity as a novel class of antifungals centered on modifying an existing orally-active FDA approved therapy. This research advances the development of much needed newer antifungal treatment options with novel mechanisms of action.
Language	English
Publishing date	2023-07-11
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.06.05.543712
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Article ; Online: Aspergillus fumigatus Cyp51A and Cyp51B Proteins Are Compensatory in Function and Localize Differentially in Response to Antifungals and Cell Wall Inhibitors.

Roundtree, Mark T / Juvvadi, Praveen R / Shwab, E Keats / Cole, D Christopher / Steinbach, William J

Antimicrobial agents and chemotherapy

2020 Volume 64, Issue 10

Abstract: Triazole antifungals are the primary therapeutic option against invasive aspergillosis. However, resistance to azoles has increased dramatically over the last decade. Azole resistance is known to primarily occur due to point mutations in the azole target ...

Abstract	Triazole antifungals are the primary therapeutic option against invasive aspergillosis. However, resistance to azoles has increased dramatically over the last decade. Azole resistance is known to primarily occur due to point mutations in the azole target protein Cyp51A, one of two paralogous 14-α sterol demethylases found in
MeSH term(s)	Antifungal Agents/pharmacology ; Aspergillus fumigatus/genetics ; Azoles/pharmacology ; Cell Wall ; Cytochrome P-450 Enzyme System/genetics ; Drug Resistance, Fungal/genetics ; Fungal Proteins/genetics ; Microbial Sensitivity Tests
Chemical Substances	Antifungal Agents ; Azoles ; Fungal Proteins ; Cytochrome P-450 Enzyme System (9035-51-2)
Language	English
Publishing date	2020-09-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	217602-6
ISSN	1098-6596 ; 0066-4804
ISSN (online)	1098-6596
ISSN	0066-4804
DOI	10.1128/AAC.00735-20
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Article: Heat shock protein 90 (Hsp90): A novel antifungal target against Aspergillus fumigatus

Lamoth, Frédéric / Juvvadi, Praveen R / Steinbach, William J

Critical reviews in microbiology. 2016 Mar. 3, v. 42, no. 2

2016

Abstract: Invasive aspergillosis is a life-threatening and difficult to treat infection in immunosuppressed patients. The efficacy of current anti-Aspergillus therapies, targeting the cell wall or membrane, is limited by toxicity (polyenes), fungistatic activity ... ...

Abstract	Invasive aspergillosis is a life-threatening and difficult to treat infection in immunosuppressed patients. The efficacy of current anti-Aspergillus therapies, targeting the cell wall or membrane, is limited by toxicity (polyenes), fungistatic activity and some level of basal resistance (echinocandins), or the emergence of acquired resistance (triazoles). The heat shock protein 90 (Hsp90) is a conserved molecular chaperone involved in the rapid development of antifungal resistance in the yeast Candida albicans. Few studies have addressed its role in filamentous fungi such as Aspergillus fumigatus, in which mechanisms of resistance may differ substantially. Hsp90 is at the center of a complex network involving calcineurin, lysine deacetylases (KDAC) and other client proteins, which orchestrate compensatory repair mechanisms of the cell wall in response to the stress induced by antifungals. In A. fumigatus, Hsp90 is a trigger for resistance to high concentrations of caspofungin, known as the paradoxical effect. Disrupting Hsp90 circuitry by different means (Hsp90 inhibitors, KDAC inhibitors and anti-calcineurin drugs) potentiates the antifungal activity of caspofungin, thus representing a promising novel antifungal approach. This review will discuss the specific features of A. fumigatus Hsp90 and the potential for antifungal strategies of invasive aspergillosis targeting this essential chaperone.
Keywords	Aspergillus fumigatus ; Candida albicans ; antifungal agents ; antifungal properties ; aspergillosis ; caspofungin ; cell walls ; enzymes ; heat-shock protein 90 ; patients ; polyenes ; toxicity ; triazoles ; yeasts
Language	English
Dates of publication	2016-0303
Size	p. 310-321.
Publishing place	Taylor & Francis
Document type	Article
ZDB-ID	1053620-6
ISSN	1549-7828 ; 1040-841X
ISSN (online)	1549-7828
ISSN	1040-841X
DOI	10.3109/1040841X.2014.947239
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Leveraging Fungal and Human Calcineurin-Inhibitor Structures, Biophysical Data, and Dynamics To Design Selective and Nonimmunosuppressive FK506 Analogs.

Gobeil, Sophie M-C / Bobay, Benjamin G / Juvvadi, Praveen R / Cole, D Christopher / Heitman, Joseph / Steinbach, William J / Venters, Ronald A / Spicer, Leonard D

mBio

2021 Volume 12, Issue 6, Page(s) e0300021

Abstract: Calcineurin is a critical enzyme in fungal pathogenesis and antifungal drug tolerance and, therefore, an attractive antifungal target. Current clinically accessible calcineurin inhibitors, such as FK506, are immunosuppressive to humans, so exploiting ... ...

Abstract	Calcineurin is a critical enzyme in fungal pathogenesis and antifungal drug tolerance and, therefore, an attractive antifungal target. Current clinically accessible calcineurin inhibitors, such as FK506, are immunosuppressive to humans, so exploiting calcineurin inhibition as an antifungal strategy necessitates fungal specificity in order to avoid inhibiting the human pathway. Harnessing fungal calcineurin-inhibitor crystal structures, we recently developed a less immunosuppressive FK506 analog, APX879, with broad-spectrum antifungal activity and demonstrable efficacy in a murine model of invasive fungal infection. Our overarching goal is to better understand, at a molecular level, the interaction determinants of the human and fungal FK506-binding proteins (FKBP12) required for calcineurin inhibition in order to guide the design of fungus-selective, nonimmunosuppressive FK506 analogs. To this end, we characterized high-resolution structures of the Mucor circinelloides FKBP12 bound to FK506 and of the Aspergillus fumigatus,
MeSH term(s)	Amino Acid Sequence ; Antifungal Agents/chemistry ; Antifungal Agents/pharmacology ; Calcineurin/chemistry ; Calcineurin/genetics ; Calcineurin/metabolism ; Calcineurin Inhibitors/chemistry ; Calcineurin Inhibitors/pharmacology ; Drug Design ; Fungal Proteins/chemistry ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Host-Pathogen Interactions ; Humans ; Mucor/drug effects ; Mucor/genetics ; Mucor/metabolism ; Mucormycosis/drug therapy ; Mucormycosis/genetics ; Mucormycosis/metabolism ; Mucormycosis/microbiology ; Sequence Alignment ; Tacrolimus/chemistry ; Tacrolimus/pharmacology ; Tacrolimus Binding Protein 1A/chemistry ; Tacrolimus Binding Protein 1A/genetics ; Tacrolimus Binding Protein 1A/metabolism
Chemical Substances	Antifungal Agents ; Calcineurin Inhibitors ; Fungal Proteins ; Calcineurin (EC 3.1.3.16) ; Tacrolimus Binding Protein 1A (EC 5.2.1.-) ; Tacrolimus (WM0HAQ4WNM)
Language	English
Publishing date	2021-11-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2557172-2
ISSN	2150-7511 ; 2161-2129
ISSN (online)	2150-7511
ISSN	2161-2129
DOI	10.1128/mBio.03000-21
Database	MEDical Literature Analysis and Retrieval System OnLINE

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