Dataset Information

Multi-omics analysis of Histoplasma capsulatum treated with monoclonal antibodies

ABSTRACT: Multi-omics analysis of Histoplasma capsulatum treated with monoclonal antibodies.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Histoplasma Capsulatum G217b

TISSUE(S): Yeast

DISEASE(S): Histoplasmosis

SUBMITTER: Ernesto Nakayasu

LAB HEAD: Ernesto Nakayasu

PROVIDER: PXD017864 | Pride | 2021-06-16

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	Hc_WC_PEP_18B7_S2_01_21Aug17_Precious_17-08-02.raw	Raw
	Hc_WC_PEP_18B7_S2_02_21Aug17_Precious_17-08-02.raw	Raw
	Hc_WC_PEP_18B7_S2_03_21Aug17_Precious_17-08-02.raw	Raw
	Hc_WC_PEP_18B7_S2_04_21Aug17_Precious_17-08-02.raw	Raw
	Hc_WC_PEP_6B7_S2_01_21Aug17_Precious_17-08-02.raw	Raw

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Publications

Remodeling of the <i>Histoplasma Capsulatum</i> Membrane Induced by Monoclonal Antibodies.

Burnet Meagan C MC Zamith-Miranda Daniel D Heyman Heino M HM Weitz Karl K KK Bredeweg Erin L EL Nosanchuk Joshua D JD Nakayasu Ernesto S ES

Vaccines 20200602 2

Antibodies play a central role in host immunity by directly inactivating or recognizing an invading pathogen to enhance different immune responses to combat the invader. However, the cellular responses of pathogens to the presence of antibodies are not well-characterized. Here, we used different mass spectrometry techniques to study the cellular responses of the pathogenic fungus <i>Histoplasma capsulatum</i> to monoclonal antibodies (mAb) against HSP60, the surface protein involved in infection ...[more]

PMID: 32498228

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Project description:Histoplasma capsulatum is a thermally dimorphic fungus with worldwide distribution, and high incidence in the Americas. It is the etiologic agent of histoplasmosis, an important life-threatening systemic mycosis. Dimorphism is an important feature for fungal survival in different environments and it has been related to the virulence of H. capsulatum, and essential to the establishment of infection. Proteomic profiles have brought important contributions to the knowledge of metabolism and pathogenicity in several biological models. However, studies of the H. capsulatum proteome have been underexplored. In the present study, we report the first proteomic comparison between the mycelium and the yeast cells of H. capsulatum. Liquid chromatography coupled to mass spectrometry was used to evaluate the proteomic profile of the two phases of H. capsulatum. In summary, 214 proteins were only detected/or preferentially abundant in mycelium, while the same occurred to 335 proteins in yeast cells. In mycelium, enzymes related to the glycolytic pathway and to the alcoholic fermentation showed greater abundance, suggesting a higher use of anaerobic pathways for energy production. In yeast cells, proteins related to the tricarboxylic acid cycle and response to temperature stress showed high abundance. Proteins related to oxidative stress response or involved with cell wall metabolism were identified with differential abundance in both conditions. Validation of proteomic data was performed by enzymatic activity determination, western blot assays, or immunofluorescence microscopy. These experiments corroborated, directly or indirectly, the abundance of isocitrate lyase, 2-methylcitrate synthase, catalase B, and mannosyl-oligosaccharide-1,2-alpha-mannosidase in the mycelium and heat shock protein (HSP) 30, HSP60, glucosamine-fructose-6-phosphate aminotransferase, glucosamine-6-phosphate deaminase, and N-acetylglucosamine-phosphate mutase in yeast-cells. The proteomic profile associated functional classification analyzes of proteins provided a better understanding of the metabolic reorganization and cell wall remodeling on the yeast form of H. capsulatum.