Browsing by Author "Paemanee A."

Filter results by typing the first few letters
Now showing 1 - 2 of 2
  • No Thumbnail Available
    ItemMetadata only
    A 2D-proteomic analysis identifies proteins differentially regulated by two different dengue virus serotypes
    (2024-12-01) Chumchanchira C.; Ramphan S.; Paemanee A.; Roytrakul S.; Lithanatudom P.; Smith D.R.; Chumchanchira C.; Mahidol University
    The mosquito transmitted dengue virus (DENV) is a major public health problem in many tropical and sub-tropical countries around the world. Both vaccine development and drug development are complex as the species Dengue virus consist of four distinct viruses (DENV 1 to DENV 4) each of which is composed of multiple lineages and strains. To understand the interaction of DENV with the host cell machinery, several studies have undertaken in vitro proteomic analysis of different cell lines infected with DENV. Invariably, these studies have utilized DENV 2. In this study we sought to define proteins that are differentially regulated by two different DENVs, DENV 2 and DENV 4. A 2-dimensional proteomic analysis identified some 300 protein spots, of which only 11 showed differential expression by both DENVs. Of these, only six were coordinately regulated. One protein, prohibitin 1 (PHB1) was downregulated by infection with both DENVs. Overexpression of PHB1 increased DENV protein expression, level of infection and genome copy number. DENV E protein colocalized with PHB, and there was a direct interaction between DENV 2 E protein and PHB1, but not between DENV 4 E protein and PHB1. The low number of proteins showing coordinate regulation after infection by different DENVs is a cause for concern, particularly in determining new druggable targets, and suggests that studies should routinely investigate multiple DENVs.
  • No Thumbnail Available
    ItemMetadata only
    Identification of a plastic-degrading enzyme from Cryptococcus nemorosus and its use in self-degradable plastics
    (2023-01-01) Arunrattanamook N.; Mhuantong W.; Paemanee A.; Reamtong O.; Hararak B.; Champreda V.; Mahidol University
    Abstract: For decades, plastic waste management has been one of the major ecological challenges of our society. Despite the introduction of biodegradable alternatives such as polylactic acid (PLA), their beneficial environmental impact is limited by the requirement of specific compost facility as biodegradation of PLA in natural environment occurs at a very slow rate. In this work, a plastic-degrading enzyme was utilized to facilitate degradation process. Genomic and proteomic tools were employed to identify a new biodegradable plastic-degrading enzyme from Cryptococcus nemorosus TBRC2959. The new enzyme, Cr14CLE, functions optimally under mild conditions with temperature range of 30 to 40 °C and suffers no significant loss of enzymatic activity at pH ranging from 6 to 8. In addition to PLA, Cr14CLE is capable to degrade other types of biodegradable plastic such as polybutylene succinate (PBS) and polybutylene adipate terephthalate (PBAT) as well as composite bioplastic. Applications of Cr14CLE have been demonstrated through the preparation of enzyme-coated PLA film and laminated PLA film with enzyme layer. PLA films prepared by both approaches exhibited capability to self-degrade in water. Key points: • Novel plastic-degrading enzyme (Cr14CLE) was identified and characterized. • Cr14CLE can degrade multiple types of biodegradable plastics under mild conditions. • Applications of Cr14CLE on self-degradable plastic were demonstrated.