Peter Zipfel

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About Peter Zipfel:

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SEEK ID: https://funginet.hki-jena.de/people/12

Location: Germany

ORCID: Not specified

Joined: 19th Feb 2021

Expertise: Not specified

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Their tags

Candida albicans Complement system Homo sapiens Immune evasion Integrative Data Analysis

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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

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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

C6 (E)

Role of secreted Candida albicans proteins in immune evasion and pathogenicity

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

Public web page: http://www.funginet.de/project-c6.html

Organisms: Candida albicans

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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Friedrich-Schiller-University

Country: Germany

City: 07745 Jena

Web page: Not specified

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

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Showing 5 out of a possible 15 Publications Advanced Publications list for this Person with search and filtering

Molecular analyses identifies new domains and structural differences among Streptococcus pneumoniae immune evasion proteins PspC and Hic.

FungiNet C - Candida projects, C6 (E)

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The PspC and Hic proteins of Streptococcus pneumoniae are some of the most variable microbial immune evasion proteins identified to date. Due to structural similarities and conserved binding profiles, …

Authors: S. Du, C. Vilhena, S. King, A. Sahagun-Ruiz, S. Hammerschmidt, C. Skerka, P. F. Zipfel

Date Published: 18th Jan 2021

Publication Type: Not specified

PubMed ID: 33462258

Citation: Sci Rep. 2021 Jan 18;11(1):1701. doi: 10.1038/s41598-020-79362-3.

Created: 19th Feb 2021 at 08:51, Last updated: 17th Jan 2024 at 10:24

Quantification of Factor H Mediated Self vs. Non-self Discrimination by Mathematical Modeling.

FungiNet C - Candida projects, B4

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The complement system is part of the innate immune system and plays an important role in the host defense against infectious pathogens. One of the main effects is the opsonization of foreign invaders … and subsequent uptake by phagocytosis. Due to the continuous default basal level of active complement molecules, a tight regulation is required to protect the body's own cells (self cells) from opsonization and from complement damage. A major complement regulator is Factor H, which is recruited from the fluid phase and attaches to cell surfaces where it effectively controls complement activation. Besides self cells, pathogens also have the ability to bind Factor H; they can thus escape opsonization and phagocytosis causing severe infections. In order to advance our understanding of the opsonization process at a quantitative level, we developed a mathematical model for the dynamics of the complement system-termed DynaCoSys model-that is based on ordinary differential equations for cell surface-bound molecules and on partial differential equations for concentration profiles of the fluid phase molecules in the environment of cells. This hybrid differential equation approach allows to model the complement cascade focusing on the role of active C3b in the fluid phase and on the cell surface as well as on its inactivation on the cell surface. The DynaCoSys model enables us to quantitatively predict the conditions under which Factor H mediated complement evasion occurs. Furthermore, investigating the quantitative impact of model parameters by a sensitivity analysis, we identify the driving processes of complement activation and regulation in both the self and non-self regime. The two regimes are defined by a critical Factor H concentration on the cell surface and we use the model to investigate the differential impact of complement model parameters on this threshold value. The dynamic modeling on the surface of pathogens are further relevant to understand pathophysiological situations where Factor H mutants and defective Factor H binding to target surfaces results in pathophysiology such as renal and retinal disease. In the future, this DynaCoSys model will be extended to also enable evaluating treatment strategies of complement-related diseases.

Authors: A. Tille, T. Lehnert, P. F. Zipfel, M. T. Figge

Date Published: 5th Oct 2020

Publication Type: Not specified

PubMed ID: 33013842

Citation: Front Immunol. 2020 Sep 2;11:1911. doi: 10.3389/fimmu.2020.01911. eCollection 2020.

Created: 16th Feb 2021 at 16:08, Last updated: 17th Jan 2024 at 10:24

Immune modulation by complement receptor 3-dependent human monocyte TGF-beta1-transporting vesicles.

C4 (E)

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Extracellular vesicles have an important function in cellular communication. Here, we show that human and mouse monocytes release TGF-beta1-transporting vesicles in response to the pathogenic fungus …

Authors: L. D. Halder, E. A. H. Jo, M. Z. Hasan, M. Ferreira-Gomes, T. Kruger, M. Westermann, D. I. Palme, G. Rambach, N. Beyersdorf, C. Speth, I. D. Jacobsen, O. Kniemeyer, B. Jungnickel, P. F. Zipfel, C. Skerka

Date Published: 11th May 2020

Publication Type: Not specified

PubMed ID: 32393780

Citation: Nat Commun. 2020 May 11;11(1):2331. doi: 10.1038/s41467-020-16241-5.

Created: 18th Feb 2021 at 11:05, Last updated: 17th Jan 2024 at 10:24

Human Neutrophils Produce Antifungal Extracellular Vesicles against Aspergillus fumigatus.

A1, B4, C6 (E), Z2

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Polymorphonuclear granulocytes (PMNs) are indispensable for controlling life-threatening fungal infections. In addition to various effector mechanisms, PMNs also produce extracellular vesicles (EVs). … Their contribution to antifungal defense has remained unexplored. We reveal that the clinically important human-pathogenic fungus Aspergillus fumigatus triggers PMNs to release a distinct set of antifungal EVs (afEVs). Proteome analyses indicated that afEVs are enriched in antimicrobial proteins. The cargo and the release kinetics of EVs are modulated by the fungal strain confronted. Tracking of afEVs indicated that they associated with fungal cells and even entered fungal hyphae, resulting in alterations in the morphology of the fungal cell wall and dose-dependent antifungal effects. To assess as a proof of concept whether the antimicrobial proteins found in afEVs might contribute to growth inhibition of hyphae when present in the fungal cytoplasm, two human proteins enriched in afEVs, cathepsin G and azurocidin, were heterologously expressed in fungal hyphae. This led to reduced fungal growth relative to that of a control strain producing the human retinol binding protein 7. In conclusion, extracellular vesicles produced by neutrophils in response to A. fumigatus infection are able to associate with the fungus, limit growth, and elicit cell damage by delivering antifungal cargo. This finding offers an intriguing, previously overlooked mechanism of antifungal defense against A. fumigatus IMPORTANCE Invasive fungal infections caused by the mold Aspergillus fumigatus are a growing concern in the clinic due to the increasing use of immunosuppressive therapies and increasing antifungal drug resistance. These infections result in high rates of mortality, as treatment and diagnostic options remain limited. In healthy individuals, neutrophilic granulocytes are critical for elimination of A. fumigatus from the host; however, the exact extracellular mechanism of neutrophil-mediated antifungal activity remains unresolved. Here, we present a mode of antifungal defense employed by human neutrophils against A. fumigatus not previously described. We found that extracellular vesicles produced by neutrophils in response to A. fumigatus infection are able to associate with the fungus, limit growth, and elicit cell damage by delivering antifungal cargo. In the end, antifungal extracellular vesicle biology provides a significant step forward in our understanding of A. fumigatus host pathogenesis and opens up novel diagnostic and therapeutic possibilities.

Authors: I. A. Shopova, I. Belyaev, P. Dasari, S. Jahreis, M. C. Stroe, Z. Cseresnyes, A. K. Zimmermann, A. Medyukhina, C. M. Svensson, T. Kruger, V. Szeifert, S. Nietzsche, T. Conrad, M. G. Blango, O. Kniemeyer, M. von Lilienfeld-Toal, P. F. Zipfel, E. Ligeti, M. T. Figge, A. A. Brakhage

Date Published: 14th Apr 2020

Publication Type: Not specified

PubMed ID: 32291301

Citation: mBio. 2020 Apr 14;11(2). pii: mBio.00596-20. doi: 10.1128/mBio.00596-20.

Created: 15th Feb 2021 at 09:34, Last updated: 17th Jan 2024 at 10:24

Unaltered Fungal Burden and Lethality in Human CEACAM1-Transgenic Mice During Candida albicans Dissemination and Systemic Infection.

FungiNet total, A5

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Carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1, CD66a) is a receptor for Candida albicans. It is crucial for the immune response of intestinal epithelial cells to this opportunistic …

Authors: E. Klaile, M. M. Muller, C. Zubiria-Barrera, S. Brehme, T. E. Klassert, M. Stock, A. Durotin, T. D. Nguyen, S. Feer, B. B. Singer, P. F. Zipfel, S. Rudolphi, I. D. Jacobsen, H. Slevogt

Date Published: 19th Dec 2019

Publication Type: Not specified

PubMed ID: 31849868

Citation: Front Microbiol. 2019 Nov 26;10:2703. doi: 10.3389/fmicb.2019.02703. eCollection 2019.

Created: 16th Feb 2021 at 16:43, Last updated: 17th Jan 2024 at 10:24

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