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  • 1
    Online Resource
    Online Resource
    Epidemiological Association of Different Campylobacter jejuni Groups with Metabolism-Associated Genetic Markers
    American Society for Microbiology ; 2011
    In:  Applied and Environmental Microbiology Vol. 77, No. 7 ( 2011-04), p. 2359-2365
    Details
    In: Applied and Environmental Microbiology, American Society for Microbiology, Vol. 77, No. 7 ( 2011-04), p. 2359-2365
    Abstract: In this study, multilocus sequence typing (MLST) was combined with the genetic detection of six genetic markers, ansB , dmsA , ggt , cj1585c , cjj81176 - 1367/71 ( cj1365c ), and the two-gene marker tlp7 ( cj0951c plus cj0952c ), to assess if their presence correlated with different C. jejuni clonal groups. Using a collection of 266 C. jejuni isolates from (in decreasing order of sample size) humans, chickens, cattle, and turkeys, it was further investigated whether the resulting genotypes correlated with the isolation source. We found combinations of the six marker genes to be mutually exclusive, and their patterns of presence or absence correlated to some degree with animal source. Together with MLST results, the obtained genotypes could be segregated into six groups. An association was identified for ansB , dmsA , and ggt with the MLST-clonal complexes (MLST-CC) 22, 42, 45, and 283, which formed the most prominent group, in which chickens were the most prevalent animal source. Two other groups, characterized by the presence of cj1585c , cjj81176 - 1367/71 , and the two-gene marker tlp7 , associated with either MLST-CC 21 or 61, were overrepresented in isolates of bovine origin. Mutually exclusive marker gene combinations were observed for ansB , dmsA , and ggt , typically found in CC 45 and the related CC 22, 42, and 283, whereas the other three marker genes were found mostly in CC 21, 48, and 206. The presence of the two-gene marker tlp7 , which is typical for MLST 21 and 53 as well as for MLST-CC 61, strongly correlates with a bovine host; this is interpreted as an example of host adaptation. In cases of C. jejuni outbreaks, these genetic markers could be helpful for more effective source tracking.
    Type of Medium: Online Resource
    ISSN: 0099-2240 , 1098-5336
    URL: Article
    DOI: 10.1128/AEM.02403-10
    RVK:
    WA 15000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2011
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    SSG: 12
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  • 2
    Online Resource
    Online Resource
    Proteome Analysis Reveals the Conidial Surface Protein CcpA Essential for Virulence of the Pathogenic Fungus Aspergillus fumigatus
    American Society for Microbiology ; 2018
    In:  mBio Vol. 9, No. 5 ( 2018-11-07)
    Details
    In: mBio, American Society for Microbiology, Vol. 9, No. 5 ( 2018-11-07)
    Abstract: Aspergillus fumigatus is a common airborne fungal pathogen of humans and a significant source of mortality in immunocompromised individuals. Here, we provide the most extensive cell wall proteome profiling to date of A. fumigatus resting conidia, the fungal morphotype pertinent to first contact with the host. Using liquid chromatography-tandem mass spectrometry (LC-MS/MS), we identified proteins within the conidial cell wall by hydrogen-fluoride (HF)–pyridine extraction and proteins exposed on the surface using a trypsin-shaving approach. One protein, designated c onidial c ell wall p rotein A (CcpA), was identified by both methods and was found to be nearly as abundant as hydrophobic rodlet layer-forming protein RodA. CcpA, an amphiphilic protein, like RodA, peaks in expression during sporulation on resting conidia. Despite high cell wall abundance, the cell surface structure of Δ ccpA resting conidia appeared normal. However, trypsin shaving of Δ ccpA conidia revealed novel surface-exposed proteins not detected on conidia of the wild-type strain. Interestingly, the presence of swollen Δ ccpA conidia led to higher activation of neutrophils and dendritic cells than was seen with wild-type conidia and caused significantly less damage to epithelial cells in vitro . In addition, virulence was highly attenuated when cortisone-treated, immunosuppressed mice were infected with Δ ccpA conidia. CcpA-specific memory T cell responses were detectable in healthy human donors naturally exposed to A. fumigatus conidia, suggesting a role for CcpA as a structural protein impacting conidial immunogenicity rather than possessing a protein-intrinsic immunosuppressive effect. Together, these data suggest that CcpA serves as a conidial stealth protein by altering the conidial surface structure to minimize innate immune recognition. IMPORTANCE The mammalian immune system relies on recognition of pathogen surface antigens for targeting and clearance. In the absence of immune evasion strategies, pathogen clearance is rapid. In the case of Aspergillus fumigatus , the successful fungus must avoid phagocytosis in the lung to establish invasive infection. In healthy individuals, fungal spores are cleared by immune cells; however, in immunocompromised patients, clearance mechanisms are impaired. Here, using proteome analyses, we identified CcpA as an important fungal spore protein involved in pathogenesis. A. fumigatus lacking CcpA was more susceptible to immune recognition and prompt eradication and, consequently, exhibited drastically attenuated virulence. In infection studies, CcpA was required for virulence in infected immunocompromised mice, suggesting that it could be used as a possible immunotherapeutic or diagnostic target in the future. In summary, our report adds a protein to the list of those known to be critical to the complex fungal spore surface environment and, more importantly, identifies a protein important for conidial immunogenicity during infection.
    Type of Medium: Online Resource
    ISSN: 2161-2129 , 2150-7511
    URL: Article
    DOI: 10.1128/mBio.01557-18
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2018
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  • 3
    Online Resource
    Online Resource
    Vaccination Approaches Against Opportunistic Fungal Infections Caused by Aspergillus fumigatus
    Bentham Science Publishers Ltd. ; 2014
    In:  Current Protein & Peptide Science Vol. 15, No. 5 ( 2014-05-31), p. 424-429
    Details
    In: Current Protein & Peptide Science, Bentham Science Publishers Ltd., Vol. 15, No. 5 ( 2014-05-31), p. 424-429
    Type of Medium: Online Resource
    ISSN: 1389-2037
    URL: Article
    DOI: 10.2174/1389203715666140512122037
    Language: English
    Publisher: Bentham Science Publishers Ltd.
    Publication Date: 2014
    SSG: 12
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