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  1. Article ; Online: High real-time reporting of domestic and wild animal diseases following rollout of mobile phone reporting system in Kenya.

    Njenga, M Kariuki / Kemunto, Naomi / Kahariri, Samuel / Holmstrom, Lindsey / Oyas, Harry / Biggers, Keith / Riddle, Austin / Gachohi, John / Muturi, Mathew / Mwatondo, Athman / Gakuya, Francis / Lekolool, Isaac / Sitawa, Rinah / Apamaku, Michael / Osoro, Eric / Widdowson, Marc-Alain / Munyua, Peninah

    PloS one

    2021  Volume 16, Issue 9, Page(s) e0244119

    Abstract: Background: To improve early detection of emerging infectious diseases in sub-Saharan Africa (SSA), many of them zoonotic, numerous electronic animal disease-reporting systems have been piloted but not implemented because of cost, lack of user ... ...

    Abstract Background: To improve early detection of emerging infectious diseases in sub-Saharan Africa (SSA), many of them zoonotic, numerous electronic animal disease-reporting systems have been piloted but not implemented because of cost, lack of user friendliness, and data insecurity. In Kenya, we developed and rolled out an open-source mobile phone-based domestic and wild animal disease reporting system and collected data over two years to investigate its robustness and ability to track disease trends.
    Methods: The Kenya Animal Biosurveillance System (KABS) application was built on the Java® platform, freely downloadable for android compatible mobile phones, and supported by web-based account management, form editing and data monitoring. The application was integrated into the surveillance systems of Kenya's domestic and wild animal sectors by adopting their existing data collection tools, and targeting disease syndromes prioritized by national, regional and international animal and human health agencies. Smartphone-owning government and private domestic and wild animal health officers were recruited and trained on the application, and reports received and analyzed by Kenya Directorate of Veterinary Services. The KABS application performed automatic basic analyses (frequencies, spatial distribution), which were immediately relayed to reporting officers as feedback.
    Results: Of 697 trained domestic animal officers, 662 (95%) downloaded the application, and >72% of them started reporting using the application within three months. Introduction of the application resulted in 2- to 14-fold increase in number of disease reports when compared to the previous year (relative risk = 14, CI 13.8-14.2, p<0.001), and reports were more widely distributed. Among domestic animals, food animals (cattle, sheep, goats, camels, and chicken) accounted for >90% of the reports, with respiratory, gastrointestinal and skin diseases constituting >85% of the reports. Herbivore wildlife (zebra, buffalo, elephant, giraffe, antelopes) accounted for >60% of the wildlife disease reports, followed by carnivores (lions, cheetah, hyenas, jackals, and wild dogs). Deaths, traumatic injuries, and skin diseases were most reported in wildlife.
    Conclusions: This open-source system was user friendly and secure, ideal for rolling out in other countries in SSA to improve disease reporting and enhance preparedness for epidemics of zoonotic diseases.
    MeSH term(s) Animal Diseases ; Animals ; Cattle ; Kenya ; Livestock ; Sentinel Surveillance ; Sheep
    Language English
    Publishing date 2021-09-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0244119
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Butane and propane oxidation by engineered cytochrome P450cam.

    Bell, Stephen G / Stevenson, Julie-Anne / Boyd, Helen D / Campbell, Sophie / Riddle, Austin D / Orton, Erica L / Wong, Luet-Lok

    Chemical communications (Cambridge, England)

    2002  , Issue 5, Page(s) 490–491

    Abstract: The haem monooxygenase cytochrome P450cam has been engineered to oxidise the gaseous alkanes butane and propane to butan-2-ol and propan-2-ol, respectively, by the use of bulky amino acid substitutions to reduce the volume of the substrate pocket and ... ...

    Abstract The haem monooxygenase cytochrome P450cam has been engineered to oxidise the gaseous alkanes butane and propane to butan-2-ol and propan-2-ol, respectively, by the use of bulky amino acid substitutions to reduce the volume of the substrate pocket and thus improve the enzyme-substrate fit: the F87W/Y96F/T101L/V247L mutant oxidizes butane with a turnover rate of 750 min-1 and 95% yield based on NADH consumed while the wild-type enzyme has an activity of 0.4 min-1 with 4% yield.
    MeSH term(s) Binding Sites/genetics ; Butanes/metabolism ; Butanols ; Camphor 5-Monooxygenase/genetics ; Camphor 5-Monooxygenase/metabolism ; Kinetics ; Mutagenesis, Site-Directed ; Oxidation-Reduction ; Propane/metabolism ; Propanols ; Protein Engineering ; Pseudomonas putida/enzymology
    Chemical Substances Butanes ; Butanols ; Propanols ; butane (6LV4FOR43R) ; Camphor 5-Monooxygenase (EC 1.14.15.1) ; Propane (T75W9911L6)
    Language English
    Publishing date 2002-07-01
    Publishing country England
    Document type Journal Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/b110957j
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Butane and propane oxidation by engineered cytochrome P450cam

    Bell, Stephen G / Stevenson, Julie-Anne / Boyd, Helen D / Campbell, Sophie / Riddle, Austin D / Orton, Erica L / Wong, Luet-Lok

    Chemical communications. 2002 Feb. 28, , no. 5

    2002  

    Abstract: The haem monooxygenase cytochrome P450cam has been engineered to oxidise the gaseous alkanes butane and propane to butan-2-ol and propan-2-ol, respectively, by the use of bulky amino acid substitutions to reduce the volume of the substrate pocket and ... ...

    Abstract The haem monooxygenase cytochrome P450cam has been engineered to oxidise the gaseous alkanes butane and propane to butan-2-ol and propan-2-ol, respectively, by the use of bulky amino acid substitutions to reduce the volume of the substrate pocket and thus improve the enzyme–substrate fit: the F87W/Y96F/T101L/V247L mutant oxidises butane with a turnover rate of 750 min−1 and 95% yield based on NADH consumed while the wild-type enzyme has an activity of 0.4 min−1 with 4% yield.
    Keywords NAD (coenzyme) ; amino acid substitution ; butanes ; enzyme substrates ; mutants ; oxidation ; oxygenases ; propane
    Language English
    Dates of publication 2002-0228
    Size p. 490-491.
    Publishing place The Royal Society of Chemistry
    Document type Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/b110957j
    Database NAL-Catalogue (AGRICOLA)

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