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  1. Article ; Online: Identification of a novel interaction between the M2 proton channel of influenza A virus and cyclin D3

    Zhang Y / Kien F / Ma HL / Tse Jane / Poon LLM / Nal B

    BMC Proceedings, Vol 5, Iss Suppl 1, p P

    consequences for cell cycle progression

    2011  Volume 70

    Keywords Medicine ; R ; Science ; Q
    Language English
    Publishing date 2011-01-01T00:00:00Z
    Publisher BioMed Central
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: MtnK, methylthioribose kinase, is a starvation-induced protein in Bacillus subtilis

    Tse Jane KS / Krogh Susanne / Mulard Laurence / Sekowska Agnieszka / Danchin Antoine

    BMC Microbiology, Vol 1, Iss 1, p

    2001  Volume 15

    Abstract: Abstract Background Methylthioadenosine, the main by-product of spermidine synthesis, is degraded in Bacillus subtilis as adenine and methylthioribose. The latter is an excellent sulfur source and the precursor of quorum-sensing signalling molecules. ... ...

    Abstract Abstract Background Methylthioadenosine, the main by-product of spermidine synthesis, is degraded in Bacillus subtilis as adenine and methylthioribose. The latter is an excellent sulfur source and the precursor of quorum-sensing signalling molecules. Nothing was known about methylthioribose recycling in this organism. Results Using trifluoromethylthioribose as a toxic analog to select for resistant mutants, we demonstrate that methylthioribose is first phosphorylated by MtnK, methylthioribose kinase, the product of gene mtnK (formerly ykrT ), expressed as an operon with mtnS (formerly ykrS ) in an abundant transcript with a S-box leader sequence. Although participating in methylthioribose recycling, the function of mtnS remained elusive. We also show that MtnK synthesis is boosted under starvation condition, in the following decreasing order: carbon-, sulfur- and nitrogen-starvation. We finally show that this enzyme is part of the family Pfam 01633 (choline kinases) which belongs to a large cluster of orthologs comprizing antibiotic aminoglycoside kinases and protein serine/threonine kinases. Conclusions The first step of methylthioribose recycling is phosphoryltaion by MTR kinase, coded by the mtnK (formerly ykrT ) gene. Analysis of the neighbourhood of mtnK demonstrates that genes located in its immediate vicinity (now named mtnUVWXYZ , formerly ykrUVWXYZ ) are also required for methylthioribose recycling.
    Keywords Microbiology ; QR1-502 ; Science ; Q ; DOAJ:Microbiology ; DOAJ:Biology ; DOAJ:Biology and Life Sciences
    Subject code 572
    Language English
    Publishing date 2001-08-01T00:00:00Z
    Publisher BioMed Central
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article: Antibodies against trimeric S glycoprotein protect hamsters against SARS-CoV challenge despite their capacity to mediate FcgammaRII-dependent entry into B cells in vitro.

    Kam, Yiu Wing / Kien, François / Roberts, Anjeanette / Cheung, Yan Chung / Lamirande, Elaine W / Vogel, Leatrice / Chu, Shui Ling / Tse, Jane / Guarner, Jeannette / Zaki, Sherif R / Subbarao, Kanta / Peiris, Malik / Nal, Béatrice / Altmeyer, Ralf

    Vaccine

    2006  Volume 25, Issue 4, Page(s) 729–740

    Abstract: Vaccine-induced antibodies can prevent or, in the case of feline infectious peritonitis virus, aggravate infections by coronaviruses. We investigated whether a recombinant native full-length S-protein trimer (triSpike) of severe acute respiratory ... ...

    Abstract Vaccine-induced antibodies can prevent or, in the case of feline infectious peritonitis virus, aggravate infections by coronaviruses. We investigated whether a recombinant native full-length S-protein trimer (triSpike) of severe acute respiratory syndrome coronavirus (SARS-CoV) was able to elicit a neutralizing and protective immune response in animals and analyzed the capacity of anti-S antibodies to mediate antibody-dependent enhancement (ADE) of virus entry in vitro and enhancement of replication in vivo. SARS-CoV-specific serum and mucosal immunoglobulins were readily detected in immunized animals. Serum IgG blocked binding of the S-protein to the ACE2 receptor and neutralized SARS-CoV infection in vitro. Entry into human B cell lines occurred in a FcgammaRII-dependent and ACE2-independent fashion indicating that ADE of virus entry is a novel cell entry mechanism of SARS-CoV. Vaccinated animals showed no signs of enhanced lung pathology or hepatitis and viral load was undetectable or greatly reduced in lungs following challenge with SARS-CoV. Altogether our results indicate that a recombinant trimeric S protein was able to elicit an efficacious protective immune response in vivo and warrant concern in the safety evaluation of a human vaccine against SARS-CoV.
    MeSH term(s) Animals ; Antibodies, Viral/immunology ; B-Lymphocytes/metabolism ; Cricetinae ; Dose-Response Relationship, Drug ; Immunity, Mucosal ; Immunoglobulin A/metabolism ; Immunoglobulin G/metabolism ; Membrane Glycoproteins/immunology ; Mice ; Receptors, IgG/metabolism ; SARS Virus/immunology ; Severe Acute Respiratory Syndrome/prevention & control ; Spike Glycoprotein, Coronavirus ; Viral Envelope Proteins/immunology
    Chemical Substances Antibodies, Viral ; Immunoglobulin A ; Immunoglobulin G ; MHV surface projection glycoprotein ; Membrane Glycoproteins ; Receptors, IgG ; Spike Glycoprotein, Coronavirus ; Viral Envelope Proteins ; spike glycoprotein, SARS-CoV
    Keywords covid19
    Language English
    Publishing date 2006-08-22
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 605674-x
    ISSN 1873-2518 ; 0264-410X
    ISSN (online) 1873-2518
    ISSN 0264-410X
    DOI 10.1016/j.vaccine.2006.08.011
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.MO 458: Show issues

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  4. Article: Differential maturation and subcellular localization of severe acute respiratory syndrome coronavirus surface proteins S, M and E.

    Nal, Béatrice / Chan, Cheman / Kien, Francois / Siu, Lewis / Tse, Jane / Chu, Kid / Kam, Jason / Staropoli, Isabelle / Crescenzo-Chaigne, Bernadette / Escriou, Nicolas / van der Werf, Sylvie / Yuen, Kwok-Yung / Altmeyer, Ralf

    The Journal of general virology

    2004  Volume 86, Issue Pt 5, Page(s) 1423–1434

    Abstract: Post-translational modifications and correct subcellular localization of viral structural proteins are prerequisites for assembly and budding of enveloped viruses. Coronaviruses, like the severe acute respiratory syndrome-associated virus (SARS-CoV), bud ...

    Abstract Post-translational modifications and correct subcellular localization of viral structural proteins are prerequisites for assembly and budding of enveloped viruses. Coronaviruses, like the severe acute respiratory syndrome-associated virus (SARS-CoV), bud from the endoplasmic reticulum-Golgi intermediate compartment. In this study, the subcellular distribution and maturation of SARS-CoV surface proteins S, M and E were analysed by using C-terminally tagged proteins. As early as 30 min post-entry into the endoplasmic reticulum, high-mannosylated S assembles into trimers prior to acquisition of complex N-glycans in the Golgi. Like S, M acquires high-mannose N-glycans that are subsequently modified into complex N-glycans in the Golgi. The N-glycosylation profile and the absence of O-glycosylation on M protein relate SARS-CoV to the previously described group 1 and 3 coronaviruses. Immunofluorescence analysis shows that S is detected in several compartments along the secretory pathway from the endoplasmic reticulum to the plasma membrane while M predominantly localizes in the Golgi, where it accumulates, and in trafficking vesicles. The E protein is not glycosylated. Pulse-chase labelling and confocal microscopy in the presence of protein translation inhibitor cycloheximide revealed that the E protein has a short half-life of 30 min. E protein is found in bright perinuclear patches colocalizing with endoplasmic reticulum markers. In conclusion, SARS-CoV surface proteins S, M and E show differential subcellular localizations when expressed alone suggesting that additional cellular or viral factors might be required for coordinated trafficking to the virus assembly site in the endoplasmic reticulum-Golgi intermediate compartment.
    MeSH term(s) Animals ; Cytoplasmic Vesicles/chemistry ; Endoplasmic Reticulum/chemistry ; Glycosylation ; Golgi Apparatus/chemistry ; Humans ; Mannose/analysis ; Membrane Glycoproteins/analysis ; Membrane Glycoproteins/chemistry ; Membrane Glycoproteins/metabolism ; Microscopy, Confocal ; Polysaccharides/chemistry ; Protein Processing, Post-Translational ; Protein Transport ; SARS Virus/growth & development ; Spike Glycoprotein, Coronavirus ; Viral Envelope Proteins/analysis ; Viral Envelope Proteins/chemistry ; Viral Envelope Proteins/metabolism ; Viral Matrix Proteins/analysis ; Viral Matrix Proteins/chemistry ; Viral Matrix Proteins/metabolism
    Chemical Substances M protein, Coronavirus ; Membrane Glycoproteins ; Polysaccharides ; Spike Glycoprotein, Coronavirus ; Viral Envelope Proteins ; Viral Matrix Proteins ; Mannose (PHA4727WTP)
    Keywords covid19
    Language English
    Publishing date 2004-01-29
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 219316-4
    ISSN 1465-2099 ; 0022-1317
    ISSN (online) 1465-2099
    ISSN 0022-1317
    DOI 10.1099/vir.0.80671-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 610: Show issues Location:
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    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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