Lydia Kasper

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About Lydia Kasper:

No description specified

SEEK ID: https://funginet.hki-jena.de/people/50

Location: Germany

ORCID: Not specified

Joined: 2nd Apr 2014

Expertise: Candida albicans, Host-Pathogen Interaction, Molecular Biology, pathogenesis, fungal pathogens, Immune evasion, infection models, innate immunity

Tools: Cell and tissue culture, Cytometry and fluorescent microscopy, Genetic analysis, Immunological techniques, Molecular Biology

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Collaborative Research Center / Transregio 124 "Pathogenic fungi and their human host: Networks of Interaction - FungiNet"

The yeast Candida albicans and the filamentous fungus Aspergillus fumigatus are by far the most important causes of life-threatening invasive mycoses in Europe. Despite the increasing incidence of these infections, the current diagnosis is still difficult and often too late, and options for therapies are limited. Moreover, A. fumigatus and C. albicans have developed multiple sophisticated, specific and unique pathogenicity mechanisms. Many of these mechanisms are not well understood. Research on ...

Projects: FungiNet total, FungiNet A - Aspergillus projects, FungiNet B - Bioinformatics projects, FungiNet C - Candida projects, INF, A1, A2, A3, A4 (E), A5, B1, B2, B3 (E), B4, C1, C2, C3, C4 (E), C5, C6 (E), Z2, Z1, B5, A6, A7, A8, C7

Web page: http://www.funginet.de/home.html

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FungiNet total

No description specified

Programme: Collaborative Research Center / Transregio 124 "Pathogenic fungi and their human host: Networks of Interaction - FungiNet"

Public web page: http://www.funginet.de/home.html

Organisms: Aspergillus fumigatus, Candida albicans

Molecular mycology, fungal/host interactions, pathogenicity mechanisms of Candida albicans

Programme: Collaborative Research Center / Transregio 124 "Pathogenic fungi and their human host: Networks of Interaction - FungiNet"

Public web page: http://www.funginet.de/project-c1.html

Organisms: Candida albicans, Homo sapiens, Candida glabrata, Candida parapsilosis, Candida tropicalis

FungiNet C - Candida projects

No description specified

Programme: Collaborative Research Center / Transregio 124 "Pathogenic fungi and their human host: Networks of Interaction - FungiNet"

Public web page: http://www.funginet.de/project-area-c.html

Organisms: Candida albicans

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Leibniz-Institute for Natural Product Research and Infection Biology Hans Knöll Institute (HKI)

Country: Germany

City: 07745 Jena

Web page: http://www.hki-jena.de

Showing 5 out of a possible 6 Publications Advanced Publications list for this Person with search and filtering

Lysosome Fusion Maintains Phagosome Integrity during Fungal Infection.

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Phagosomes must maintain membrane integrity to exert their microbicidal function. Some microorganisms, however, survive and grow within phagosomes. In such instances, phagosomes must expand to avoid …

Authors: J. Westman, G. F. W. Walpole, L. Kasper, B. Y. Xue, O. Elshafee, B. Hube, S. Grinstein

Date Published: 9th Dec 2020

Publication Type: Not specified

PubMed ID: 33022213

Citation: Cell Host Microbe. 2020 Dec 9;28(6):798-812.e6. doi: 10.1016/j.chom.2020.09.004. Epub 2020 Oct 5.

Created: 16th Feb 2021 at 11:58, Last updated: 17th Jan 2024 at 10:24

The Dual Function of the Fungal Toxin Candidalysin during Candida albicans-Macrophage Interaction and Virulence.

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The dimorphic fungus Candida albicans is both a harmless commensal organism on mucosal surfaces and an opportunistic pathogen. Under certain predisposing conditions, the fungus can overgrow the mucosal …

Authors: A. Konig, B. Hube, L. Kasper

Date Published: 24th Jul 2020

Publication Type: Not specified

PubMed ID: 32722029

Citation: Toxins (Basel). 2020 Jul 24;12(8). pii: toxins12080469. doi: 10.3390/toxins12080469.

Created: 16th Feb 2021 at 12:00, Last updated: 17th Jan 2024 at 10:24

The fungal peptide toxin Candidalysin activates the NLRP3 inflammasome and causes cytolysis in mononuclear phagocytes.

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Clearance of invading microbes requires phagocytes of the innate immune system. However, successful pathogens have evolved sophisticated strategies to evade immune killing. The opportunistic human …

Authors: L. Kasper, A. Konig, P. A. Koenig, M. S. Gresnigt, J. Westman, R. A. Drummond, M. S. Lionakis, O. Gross, J. Ruland, J. R. Naglik, B. Hube

Date Published: 15th Oct 2018

Publication Type: Not specified

PubMed ID: 30323213

Citation: Nat Commun. 2018 Oct 15;9(1):4260. doi: 10.1038/s41467-018-06607-1.

Created: 16th Feb 2021 at 12:03, Last updated: 17th Jan 2024 at 10:24

Candida albicans-Induced Epithelial Damage Mediates Translocation through Intestinal Barriers.

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Life-threatening systemic infections often occur due to the translocation of pathogens across the gut barrier and into the bloodstream. While the microbial and host mechanisms permitting bacterial gut … translocation are well characterized, these mechanisms are still unclear for fungal pathogens such as Candida albicans, a leading cause of nosocomial fungal bloodstream infections. In this study, we dissected the cellular mechanisms of translocation of C. albicans across intestinal epithelia in vitro and identified fungal genes associated with this process. We show that fungal translocation is a dynamic process initiated by invasion and followed by cellular damage and loss of epithelial integrity. A screen of >2,000 C. albicans deletion mutants identified genes required for cellular damage of and translocation across enterocytes. Correlation analysis suggests that hypha formation, barrier damage above a minimum threshold level, and a decreased epithelial integrity are required for efficient fungal translocation. Translocation occurs predominantly via a transcellular route, which is associated with fungus-induced necrotic epithelial damage, but not apoptotic cell death. The cytolytic peptide toxin of C. albicans, candidalysin, was found to be essential for damage of enterocytes and was a key factor in subsequent fungal translocation, suggesting that transcellular translocation of C. albicans through intestinal layers is mediated by candidalysin. However, fungal invasion and low-level translocation can also occur via non-transcellular routes in a candidalysin-independent manner. This is the first study showing translocation of a human-pathogenic fungus across the intestinal barrier being mediated by a peptide toxin.IMPORTANCECandida albicans, usually a harmless fungus colonizing human mucosae, can cause lethal bloodstream infections when it manages to translocate across the intestinal epithelium. This can result from antibiotic treatment, immune dysfunction, or intestinal damage (e.g., during surgery). However, fungal processes may also contribute. In this study, we investigated the translocation process of C. albicans using in vitro cell culture models. Translocation occurs as a stepwise process starting with invasion, followed by epithelial damage and loss of epithelial integrity. The ability to secrete candidalysin, a peptide toxin deriving from the hyphal protein Ece1, is key: C. albicans hyphae, secreting candidalysin, take advantage of a necrotic weakened epithelium to translocate through the intestinal layer.

Authors: S. Allert, T. M. Forster, C. M. Svensson, J. P. Richardson, T. Pawlik, B. Hebecker, S. Rudolphi, M. Juraschitz, M. Schaller, M. Blagojevic, J. Morschhauser, M. T. Figge, I. D. Jacobsen, J. R. Naglik, L. Kasper, S. Mogavero, B. Hube

Date Published: 5th Jun 2018

Publication Type: Not specified

PubMed ID: 29871918

Citation: mBio. 2018 Jun 5;9(3). pii: mBio.00915-18. doi: 10.1128/mBio.00915-18.

Created: 11th Feb 2021 at 15:45, Last updated: 17th Jan 2024 at 10:24

Immunoproteomic Analysis of Antibody Responses to Extracellular Proteins of Candida albicans Revealing the Importance of Glycosylation for Antigen Recognition.

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During infection, the human pathogenic fungus Candida albicans undergoes a yeast-to-hypha transition, secretes numerous proteins for invasion of host tissues, and modulates the host's immune response. …

Authors: T. Luo, T. Kruger, U. Knupfer, L. Kasper, N. Wielsch, B. Hube, A. Kortgen, M. Bauer, E. J. Giamarellos-Bourboulis, G. Dimopoulos, A. A. Brakhage, O. Kniemeyer