Matches in UGent Biblio for { <https://biblio.ugent.be/publication/1901516#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B447810.
- aggregation creator B447811.
- aggregation creator B447812.
- aggregation creator B447813.
- aggregation creator B447814.
- aggregation creator B447815.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2011".
- aggregation format "application/pdf".
- aggregation hasFormat 1901516.bibtex.
- aggregation hasFormat 1901516.csv.
- aggregation hasFormat 1901516.dc.
- aggregation hasFormat 1901516.didl.
- aggregation hasFormat 1901516.doc.
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- aggregation hasFormat 1901516.txt.
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- aggregation hasFormat 1901516.yaml.
- aggregation isPartOf urn:issn:0007-1188.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "The proton translocation domain of cellular vacuolar ATPase provides a target for the treatment of influenza A virus infections".
- aggregation abstract "BACKGROUND AND PURPOSE: Cellular vacuolar ATPases (v-ATPase) play an important role in endosomal acidification, a critical step in influenza A virus (IAV) host cell infection. We investigated the antiviral activity of the v-ATPase inhibitor saliphenylhalamide (SaliPhe) and compared it with several older v-ATPase inhibitors concanamycin A, bafilomycin A1, (BafA) and archazolid B targeting the subunit c of the V(0) sector. EXPERIMENTAL APPROACH: An in vitro assay was devised to quantify the anti-influenza effect of v-ATPase inhibitors by measuring green fluorescent protein fluorescence of a reporter IAV. These data were combined with cytotoxicity testing to calculate selectivity indices. Data were validated by testing v-ATPase inhibitors against wild-type IAV in vitro and in vivo in mice. KEY RESULTS: In vitro SaliPhe blocked the proliferation of pandemic and multidrug resistant viruses at concentrations up to 51-fold below its cytotoxic concentrations. At essentially non-toxic concentrations, SaliPhe protected 62.5% of mice against a lethal challenge of a mouse-adapted influenza strain, while BafA at cytotoxic concentrations showed essentially no protection against infection with IAV (SaliPhe vs. BafA P < 0.001). CONCLUSIONS AND IMPLICATIONS: Our results show that a distinct binding site of the proton translocation domain of cellular v-ATPase can be selectively targeted by a new generation v-ATPase inhibitor with reduced toxicity to treat influenza virus infections, including multi-resistant strains. Treatment strategies against influenza that target host cellular proteins are expected to be more resistant to virus mutations than drugs blocking viral proteins.".
- aggregation authorList BK780521.
- aggregation endPage "357".
- aggregation issue "2".
- aggregation startPage "344".
- aggregation volume "164".
- aggregation aggregates 2937977.
- aggregation isDescribedBy 1901516.
- aggregation similarTo j.1476-5381.2011.01346.x.
- aggregation similarTo LU-1901516.