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  1. Article ; Online: Discovery of the extracytoplasmic function σ factors.

    Lonetto, Michael A / Donohue, Timothy J / Gross, Carol A / Buttner, Mark J

    Molecular microbiology

    2019  Volume 112, Issue 2, Page(s) 348–355

    Abstract: This special issue of Molecular Microbiology marks the ... ...

    Abstract This special issue of Molecular Microbiology marks the 25
    MeSH term(s) Bacteria/genetics ; Bacteria/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Extracellular Space/genetics ; Extracellular Space/metabolism ; Gene Expression Regulation, Bacterial ; Sigma Factor/genetics ; Sigma Factor/metabolism ; Signal Transduction
    Chemical Substances Bacterial Proteins ; Sigma Factor
    Language English
    Publishing date 2019-06-17
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 619315-8
    ISSN 1365-2958 ; 0950-382X
    ISSN (online) 1365-2958
    ISSN 0950-382X
    DOI 10.1111/mmi.14307
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 2502: Show issues Location:
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  2. Article ; Online: mTOR inhibition improves immune function in the elderly.

    Mannick, Joan B / Del Giudice, Giuseppe / Lattanzi, Maria / Valiante, Nicholas M / Praestgaard, Jens / Huang, Baisong / Lonetto, Michael A / Maecker, Holden T / Kovarik, John / Carson, Simon / Glass, David J / Klickstein, Lloyd B

    Science translational medicine

    2014  Volume 6, Issue 268, Page(s) 268ra179

    Abstract: Inhibition of the mammalian target of rapamycin (mTOR) pathway extends life span in all species studied to date, and in mice delays the onset of age-related diseases and comorbidities. However, it is unknown if mTOR inhibition affects aging or its ... ...

    Abstract Inhibition of the mammalian target of rapamycin (mTOR) pathway extends life span in all species studied to date, and in mice delays the onset of age-related diseases and comorbidities. However, it is unknown if mTOR inhibition affects aging or its consequences in humans. To begin to assess the effects of mTOR inhibition on human aging-related conditions, we evaluated whether the mTOR inhibitor RAD001 ameliorated immunosenescence (the decline in immune function during aging) in elderly volunteers, as assessed by their response to influenza vaccination. RAD001 enhanced the response to the influenza vaccine by about 20% at doses that were relatively well tolerated. RAD001 also reduced the percentage of CD4 and CD8 T lymphocytes expressing the programmed death-1 (PD-1) receptor, which inhibits T cell signaling and is more highly expressed with age. These results raise the possibility that mTOR inhibition may have beneficial effects on immunosenescence in the elderly.
    MeSH term(s) Aged ; Antibodies, Viral/immunology ; CD4-Positive T-Lymphocytes/drug effects ; CD4-Positive T-Lymphocytes/immunology ; CD8-Positive T-Lymphocytes/drug effects ; CD8-Positive T-Lymphocytes/immunology ; Cohort Studies ; Everolimus ; Humans ; Immunity/drug effects ; Influenza Vaccines/immunology ; Placebos ; Programmed Cell Death 1 Receptor/metabolism ; Protein Kinase Inhibitors/pharmacology ; Seasons ; Sirolimus/analogs & derivatives ; Sirolimus/pharmacology ; TOR Serine-Threonine Kinases/antagonists & inhibitors ; TOR Serine-Threonine Kinases/metabolism ; Vaccination
    Chemical Substances Antibodies, Viral ; Influenza Vaccines ; PDCD1 protein, human ; Placebos ; Programmed Cell Death 1 Receptor ; Protein Kinase Inhibitors ; Everolimus (9HW64Q8G6G) ; MTOR protein, human (EC 2.7.1.1) ; TOR Serine-Threonine Kinases (EC 2.7.1.1) ; Sirolimus (W36ZG6FT64)
    Language English
    Publishing date 2014-12-24
    Publishing country United States
    Document type Journal Article ; Randomized Controlled Trial ; Research Support, Non-U.S. Gov't
    ZDB-ID 2518854-9
    ISSN 1946-6242 ; 1946-6234
    ISSN (online) 1946-6242
    ISSN 1946-6234
    DOI 10.1126/scitranslmed.3009892
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 6941: Show issues Location:
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  3. Article: Characterization of a novel fucose-regulated promoter (PfcsK) suitable for gene essentiality and antibacterial mode-of-action studies in Streptococcus pneumoniae.

    Chan, Pan F / O'Dwyer, Karen M / Palmer, Leslie M / Ambrad, Jennifer D / Ingraham, Karen A / So, Chi / Lonetto, Michael A / Biswas, Sanjoy / Rosenberg, Martin / Holmes, David J / Zalacain, Magdalena

    Journal of bacteriology

    2003  Volume 185, Issue 6, Page(s) 2051–2058

    Abstract: The promoter of the Streptococcus pneumoniae putative fuculose kinase gene (fcsK), the first gene of a novel fucose utilization operon, is induced by fucose and repressed by glucose or sucrose. When the streptococcal polypeptide deformylase (PDF) gene ( ... ...

    Abstract The promoter of the Streptococcus pneumoniae putative fuculose kinase gene (fcsK), the first gene of a novel fucose utilization operon, is induced by fucose and repressed by glucose or sucrose. When the streptococcal polypeptide deformylase (PDF) gene (def1, encoding PDF) was placed under the control of P(fcsK), fucose-dependent growth of the S. pneumoniae (P(fcsK)::def1) strain was observed, confirming the essential nature of PDF in this organism. The mode of antibacterial action of actinonin, a known PDF inhibitor, was also confirmed with this strain. The endogenous fuculose kinase promoter is a tightly regulated, titratable promoter which will be useful for target validation and for confirmation of the mode of action of novel antibacterial drugs in S. pneumoniae.
    MeSH term(s) Amidohydrolases ; Aminopeptidases/antagonists & inhibitors ; Aminopeptidases/genetics ; Anti-Bacterial Agents/pharmacology ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Base Sequence ; Enzyme Inhibitors/pharmacology ; Fucose/metabolism ; Gene Expression Regulation, Bacterial ; Genes, Essential ; Humans ; Hydroxamic Acids/pharmacology ; Molecular Sequence Data ; Operon ; Promoter Regions, Genetic/genetics ; Streptococcus pneumoniae/drug effects ; Streptococcus pneumoniae/genetics ; Streptococcus pneumoniae/growth & development ; Streptococcus pneumoniae/metabolism
    Chemical Substances Anti-Bacterial Agents ; Bacterial Proteins ; Enzyme Inhibitors ; Hydroxamic Acids ; Fucose (28RYY2IV3F) ; Aminopeptidases (EC 3.4.11.-) ; Amidohydrolases (EC 3.5.-) ; peptide deformylase (EC 3.5.1.88) ; actinonin (P18SPA8N0K)
    Language English
    Publishing date 2003-03
    Publishing country United States
    Document type Evaluation Study ; Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/JB.185.6.2051-2058.2003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Characterization of the Streptococcus pneumoniae NADH oxidase that is required for infection.

    Yu, Jun / Bryant, Alexander P / Marra, Andrea / Lonetto, Michael A / Ingraham, Karen A / Chalker, Alison F / Holmes, David J / Holden, David / Rosenberg, Martin / McDevitt, Damien

    Microbiology (Reading, England)

    2001  Volume 147, Issue Pt 2, Page(s) 431–438

    Abstract: Streptococcus pneumoniae is an important human pathogen capable of causing serious infections. NADH oxidase, a factor necessary for infection, was previously identified as part of a signature-tagged mutagenesis screen of a S. pneumoniae clinical isolate, ...

    Abstract Streptococcus pneumoniae is an important human pathogen capable of causing serious infections. NADH oxidase, a factor necessary for infection, was previously identified as part of a signature-tagged mutagenesis screen of a S. pneumoniae clinical isolate, 0100993. The mutant, with a plasmid insertion disrupting the nox gene, was attenuated for virulence in a murine respiratory tract infection model. A complete refined nox deletion mutant was generated by allelic-replacement mutagenesis and found to be attenuated for virulence 10(5)-fold in the murine respiratory tract infection model and at least 10(4)-fold in a Mongolian gerbil otitis media infection model, confirming the importance of the NADH oxidase for both types of S. pneumoniae infection. NADH oxidase converts O(2) to H(2)O. If O(2) is not fully reduced, it can form superoxide anion (O2(-)) and hydrogen peroxide (H(2)O(2)), both of which can be toxic to cells. Bacterial cell extracts from the allelic-replacement mutant were found to lack NADH oxidase activity and the mutant was unable to grow exponentially under conditions of vigorous aeration. In contrast, the mutant displayed normal growth characteristics under conditions of limited aeration. The S. pneumoniae nox gene was cloned and expressed in E. coli. The purified His-tagged NADH oxidase was shown to oxidize NADH with a K:(m) of 32 microM, but was unable to oxidize NADPH. Oxidation of NADH was independent of exogenous FAD or FMN.
    MeSH term(s) Alleles ; Animals ; Disease Models, Animal ; Humans ; Mice ; Multienzyme Complexes/genetics ; Multienzyme Complexes/metabolism ; Mutation ; NADH, NADPH Oxidoreductases/genetics ; NADH, NADPH Oxidoreductases/metabolism ; Otitis Media/microbiology ; Otitis Media/physiopathology ; Phylogeny ; Pneumococcal Infections/microbiology ; Pneumococcal Infections/physiopathology ; Respiratory Tract Infections/microbiology ; Respiratory Tract Infections/physiopathology ; Streptococcus pneumoniae/enzymology ; Streptococcus pneumoniae/genetics ; Streptococcus pneumoniae/growth & development ; Streptococcus pneumoniae/pathogenicity ; Virulence
    Chemical Substances Multienzyme Complexes ; NADH oxidase (EC 1.6.-) ; NADH, NADPH Oxidoreductases (EC 1.6.-)
    Language English
    Publishing date 2001-02
    Publishing country England
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1180712-x
    ISSN 1465-2080 ; 1350-0872
    ISSN (online) 1465-2080
    ISSN 1350-0872
    DOI 10.1099/00221287-147-2-431
    Database MEDical Literature Analysis and Retrieval System OnLINE

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