PXD014197

PXD014197 is an original dataset announced via ProteomeXchange.

Title	The heat shock protein family A (HSPA8) acts as a surface receptor of alveolar macrophages specific for recognition and phagocytosis of Lichtheimia corymbifera spores
Description	Mucormycosis is a life-threatening disease especially in immunocompromised patients that was caused my mucoralean fungi. The rate of mortality is tremendously increased in the last decades due to the lack of appropriate diagnostic tools, insufficient knowledge about the immune response toward the mucormycosis and unavailability of specific antifungal drugs. Several species of mucoralean fungi cause mucormycosis such as Lichtheimia, Rhizopus, and Mucor. Lichtheimia species ranks the second and third cause of mucormycosis in Europe and the USA, respectively. In this study, we investigated the receptors present on the surface of immune cells that bind to the spores of Lichtheimia. We focus on two strains of L. corymbifera (FSU:9682 and FSU:10164) using resting and heat-killed spores. Additionally, we choose alveolar macrophages (MH-S) to carry out our experiment. MH-S is the first line of defense in the lung and the major component in the innate immune system. MH-S surface proteins were biotinylated and incubated with Lichtheimia spores. The surface proteins and putative binding partners were enriched by streptavidin. LC-MS/MS analysis showed that several proteins are highly expressed in presence of Lichtheimia spores, of which the heat shock protein family A (HSPA8) was one of the most abundant proteins. FACS analysis and immunofluorescence examination confirmed that HSPA8 is highly abundant on the surface of the MH-S, but not on the surface of Lichtheimia spores. Moreover, our study showed that the intensity of HSPA8 on the surface of MH-S depends on the multiplicity of infection (MOI). Additionally, the blocking with anti-HSPA8 antibody reduced the capability of MH-S to engulf the Lichtheimia spores, but not Aspergillus fumigatus spores. This confirms that HSPA8 is specific to Lichtheimia. THis is the first study addressing the determination of surface receptors of alveolar macrophages that in the context of Mucoralean fungi.
HostingRepository	PRIDE
AnnounceDate	2020-07-17
AnnouncementXML	Submission_2020-07-16_18:13:16.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Thomas Krüger
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090; scientific name: Lichtheimia corymbifera JMRC:FSU:9682; NCBI TaxID: 1263082;
ModificationList	biotinylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2019-06-10 03:19:00	ID requested
⏵ 1	2020-07-16 18:13:17	announced

Hassan MIA, Kruse JM, Kr, ü, ger T, Dahse HM, Cseresny, é, s Z, Blango MG, Slevogt H, H, ö, rhold F, Ast V, K, ö, nig R, Figge MT, Kniemeyer O, Brakhage AA, Voigt K, Functional surface proteomic profiling reveals the host heat-shock protein A8 as a mediator of Lichtheimia corymbifera recognition by murine alveolar macrophages. Environ Microbiol, 22(9):3722-3740(2020) [pubmed]

submitter keyword: Lichtheimia corymbifera, alveolar macrophages, surface receptor, HSPA8, mass spectrometry, biotinylation

Axel A. Brakhage
contact affiliation	Department of Molecular and Applied Microbiology Leibniz Institute for Natural Product Research and Infection Biology - Hans Knoell Institute Adolf-Reichwein-Str. 23, 07745, Jena, Germany
contact email	Axel.Brakhage@leibniz-hki.de
lab head
Thomas Krüger
contact affiliation	Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute
contact email	thomas.krueger@leibniz-hki.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD014197
     1. Label: PRIDE project
     2. Name: The heat shock protein family A (HSPA8) acts as a surface receptor of alveolar macrophages specific for recognition and phagocytosis of Lichtheimia corymbifera spores