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  • 1
    Electronic Resource
    Electronic Resource
    Cloning and disruption of the gene encoding an extracellular metalloprotease of Aspergillus fumigatus (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 14 (1994), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Aspergillus fumigatus secretes a serine alkaline protease (ALP) and a metalloprotease (MEP) when the fungus is cultivated in the presence of collagen as sole nitrogen and carbon source. The gene encoding ALP was isolated and characterized previously. We report here the cloning and the sequencing of the gene encoding MEP. Genomic and cDNA clones were isolated from A. fumigatus libraries using synthetic oligonucleotides as probes. Stretches of the deduced amino acid sequence were found to be in agreement with the N-terminal amino acid sequence of MEP and with internal peptide sequences. The amino acid sequence of the enzyme contains a putative active-site sequence HEYTH homologous to the active site of other bacterial and eukaryotic zinc metalloproteases. Sequence analysis reveals that MEP has a pre-proregion consisting of 245 amino acid residues preceding the 388 amino acid residues of the mature region (molecular mass of 42 kDa). An alp mep mutant, deficient in proteolytic activity at neutral pH in vitro, was constructed and tested for pathogenicity in a murine model. No difference in pathogenicity was observed between the wild-type strain and the alp mep double mutant, suggesting that ALP and MEP are not essential for the invasion of the lung tissues by A. fumigatus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1994.tb01327.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Multiplicity of genes encoding secreted aspartic proteinases in Candida species (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 13 (1994), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The secreted aspartic proteinases (SAP) of Candida sp. are presumed to be potential virulence factors. In the opportunistic pathogen Candida albicans the proteinase genes identified to date, SAP1, SAP2, SAP3 and SAP4, constitute a multigene family. Before addressing the possible role of each proteinase in virulence, we sought to isolate all the members of this multigene family by screening a genomic library with a SAP1 probe for additional C. albicans SAP genes using low-stringency hybridization conditions. Three putative new members, SAP5, SAP6 and SAP7 were isolated and sequenced. The N-terminal segments of the deduced amino acid sequences of SAP5 and SAP6 contained secretion signal sequences similar to those of other Candida SAPs. Upon comparison and alignment with the other reported SAP amino acid sequences, SAP7 is not only the most divergent protein but also exhibits a much longer putative pro-sequence with a single Lys-Lys putative processing site. Using SAP1 to SAP7 as probes, the overall number of SAP genes in C. albicans was tentatively estimated by low-stringency hybridization to EcoRI-digested genomic DNA. While each isolated SAP gene could be assigned to distinct EcoRI bands, the existence of two additional genes not isolated after screening of the C. albicans gene library was inferred. Furthermore, evidence was obtained for the existence of SAP muttigene families in other Candida species such as C. tropicalis, C. parapsilosis and C. guiller-mondii.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1994.tb00429.x
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  • 3
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    Isolation and nucleotide sequence of the extracellular acid protease gene (ACP) from the yeastCandida tropicalis (1991)
    Wiley
    Details
    Publication Date: 1991-07-29
    Print ISSN: 0014-5793
    Electronic ISSN: 1873-3468
    Topics: Biology , Chemistry and Pharmacology
    Published by Wiley on behalf of Federation of European Biochemical Societies.
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  • 4
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    SARS-CoV-2 Ig G among Healthcare Workers and the General Population (2021)
    Molecular Diversity Preservation International
    Details
    Publication Date: 2021-04-12
    Description: It is assumed that healthcare workers are at the highest risk to be infected by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). However, few data from healthcare workers who do not primarily take care of patients with SARS-CoV-2 infection support this assumption. We investigated the prevalence of immunoglobulin G (Ig G) against SARS-CoV-2 among healthcare workers who do not primarily take care of patients with SARS-CoV-2 infection and the general population in a well-defined geographical area. The first part of the study was conducted in May 2020 in Val Mesolcina (Southern Switzerland), a valley with ~8000 inhabitants. All healthcare workers were invited. All participants (n = 488) of the Swiss Longitudinal Cohort Study (SWICOS), a cohort representative of the general population, were also invited. Circulating Ig G against spike protein subunit 1 of SARS-CoV-2 were tested in each subject. Subjects with positive Ig G were tested again after 6 months. The condition of being a healthcare worker, rather than a part of the general population, was tested as a predictor of seroprevalence positivity by both simple and multiple (adjusted for age and sex) logistic regression. Eleven (2.6%) of the 423 SWICOS participants and 46 (16%) out of 289 healthcare workers were positive for antibodies against SARS-CoV-2. The seroprevalence OR was 7.01 (95% CI: 3.53–15.47) for healthcare workers as compared to SWICOS participants. After adjusting for age and gender, the seroprevalence OR was 5.13 (95% CI: 2.54–10.40). About three quarters of the subjects in the SWICOS (73%) and in healthcare (79%) group with a previous positive serology still presented positive Ig G against the SARS-CoV-2 after 6 months. The present seroprevalence data point out that the SARS-CoV-2 infection is seven times higher among healthcare workers than in the general population of Val Mesolcina. Efforts to effectively protect all the healthcare personnel are needed.
    Electronic ISSN: 2076-0817
    Topics: Biology , Medicine
    Published by Molecular Diversity Preservation International
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