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Proteomic analysis of Rickettsia akari proposes a 44 kDa-OMP as a potential biomarker for Rickettsialpox diagnosis

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dc.rights.license CC BY eng
dc.contributor.author Csicsay, Frantisek cze
dc.contributor.author Flores-Ramirez, Gabriela cze
dc.contributor.author Zuniga-Navarrete, Fernando cze
dc.contributor.author Bartošová, Maria cze
dc.contributor.author Myslivcová Fučíková, Alena cze
dc.contributor.author Pajer, Petr cze
dc.contributor.author Dresler, Jiri cze
dc.contributor.author Skultety, Ludovit cze
dc.contributor.author Quevedo-Diaz, Marco Antonio cze
dc.date.accessioned 2025-12-05T09:23:36Z
dc.date.available 2025-12-05T09:23:36Z
dc.date.issued 2020 eng
dc.identifier.issn 1471-2180 eng
dc.identifier.uri http://hdl.handle.net/20.500.12603/1128
dc.description.abstract Background Rickettsialpox is a febrile illness caused by the mite-borne pathogenRickettsia akari. Several cases of this disease are reported worldwide annually. Nevertheless, the relationship between the immunogenicity ofR. akariand disease development is still poorly understood. Thus, misdiagnosis is frequent. Our study is aiming to identify immunogenic proteins that may improve disease recognition and enhance subsequent treatment. To achieve this goal, two proteomics methodologies were applied, followed by immunoblot confirmation. Results Three hundred and sixteen unique proteins were identified in the whole-cell extract ofR. akari. The most represented protein groups were found to be those involved in translation, post-translational modifications, energy production, and cell wall development. A significant number of proteins belonged to amino acid transport and intracellular trafficking. Also, some proteins affecting the virulence were detected. In silico analysis of membrane enriched proteins revealed 25 putative outer membrane proteins containing beta-barrel structure and 11 proteins having a secretion signal peptide sequence. Using rabbit and human sera, various immunoreactive proteins were identified from which the 44 kDa uncharacterized protein (A8GP63) has demonstrated a unique detection capability. It positively distinguished the sera of patients with Rickettsialpox from other rickettsiae positive human sera. Conclusion Our proteomic analysis certainly contributed to the lack of knowledge ofR. akaripathogenesis.The result obtained may also serve as a guideline for a more accurate diagnosis of rickettsial diseases. The identified 44 kDa uncharacterized protein can be certainly used as a unique marker of rickettsialpox or as a target molecule for the development of more effective treatment. eng
dc.format p. "Article Number: 200" eng
dc.language.iso eng eng
dc.publisher BMC eng
dc.relation.ispartof BMC Microbiology, volume 20, issue: 1 eng
dc.subject Rickettsia akari eng
dc.subject Rickettsialpox eng
dc.subject Proteome eng
dc.subject Surface-exposed proteins eng
dc.subject Outer membrane proteins eng
dc.title Proteomic analysis of Rickettsia akari proposes a 44 kDa-OMP as a potential biomarker for Rickettsialpox diagnosis eng
dc.type article eng
dc.identifier.obd 43876924 eng
dc.identifier.doi 10.1186/s12866-020-01877-6 eng
dc.publicationstatus postprint eng
dc.peerreviewed yes eng
dc.source.url https://bmcmicrobiol.biomedcentral.com/track/pdf/10.1186/s12866-020-01877-6.pdf cze
dc.relation.publisherversion https://bmcmicrobiol.biomedcentral.com/track/pdf/10.1186/s12866-020-01877-6.pdf eng
dc.rights.access Open Access eng


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