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Center for Convergent Bioscience and Medicine
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      • Zhao, Shan
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  • Home
  • About us
    • CCBM Core Values
    • Director's Message
    • Management >
      • Internal advisory board >
        • Back, William
        • Friend, Richard
        • Higginbotham, John
        • Messina, Joseph
        • Welbourne, Theresa
      • Scientific advisory board
      • Industry Partners/New Ventures committee >
        • Blakley, Daniel
        • Chiem, Nghia
        • Rich, Collin
        • George, Dana
      • Education & Training committee
      • Seminar program committee
      • Appointments committee
      • Outreach committee >
        • Jones, Adam
        • McKenna, Chelsea
        • Pearl, Drew
    • Policies
  • The Team
    • Core Members >
      • Arora, Meenakshi
      • Bao, Yuping
      • Bonizzoni, Marco
      • Caldwell, Guy
      • Caldwell, Kimberly
      • Chtarbanova, Stanislava
      • Ciesla, Lukasz
      • Correll, Nathan
      • Crowe-White, Kristi
      • Ganugula, Raghu
      • Ghosh, Ayanjeet
      • Gong, Jiaqi (Jackey)
      • Hauser, Adam
      • Kim, Brandon
      • Kim, Yonghyun
      • Koh, Amanda
      • Kumar, M. N. V. Ravi
      • Papish, Elizabeth
      • Park, Han-A
      • Rao, Shreyas
      • Snowden, Timothy
      • Zhao, Chao
    • CCBM Research Team
    • Affiliates >
      • Bartlett, Robin
      • Clement, Prabhakar
      • Dai, Shibin
      • Dunkle, Jack
      • Fedin, Igor
      • Frantom, Patrick
      • Gleyzer, Sergei
      • Higgins, Melanie
      • Iyengar, Atulya
      • Jiang, Daqian
      • Kana, Rajesh
      • McDonough, Ian
      • Mewes, Tim
      • Soylu, Firat
      • Summers, Ryan
      • Szilvási, Tibor
      • Vrbsky, Susan
      • Zhao, Shan
  • Research
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Melanie Higgins 

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Dr. Higgins is an Assistant Professor in the Department of Biological Sciences at the University of Alabama. She completed her PhD at the University of Victoria in Canada, where she investigated host glycan degradation enzymes from Streptococcus pneumoniae and studied their roles in pathogenesis. From here, she was awarded a Postdoctoral fellowship for the University of Adelaide in Australia, where she continued her research on pneumococcal pathogenesis and characterized potential vaccine targets. She then pursued a second Postdoctoral position at the University of British Columbia in Canada, where she studied the structure-function relationships and mechanisms of bacterial enzymes involved in the biosynthesis of bioactive natural products. These experiences solidified her passion for using a multidisciplinary approach to interrogate bacterial processes that can influence human health.

Representative Publications

  1. N-Glycan Degradation Pathways in Gut- and Soil-Dwelling Actinobacteria Share Common Core Genes. M.A. Higgins, G. Tegl , S.S. MacDonald, G. Arnal, H. Brumer, S.G. Withers, K.S. Ryan. ACS Chem Biol. 16(4):701-711, 2021.
  2. Generating a Fucose Permease Deletion Mutant in Bifidobacterium longum subspecies infantis ATCC 15697. M.A. Higgins & K.S. Ryan. Anaerobe. 68:102320, 2021.
  3. An Asymmetric Reductase That Intercepts Acyclic Imino Acids Produced in Situ by a Partner Oxidase. J. Guo, M.A. Higgins, P. Daniel-Ivad, K.S. Ryan. J Am Chem Soc. 141(31):12258-12267, 2019.
  4. Convergent Biosynthetic Transformations to a Bacterial Specialized Metabolite. Y.L. Du, M.A. Higgins, G. Zhao, K.S. Ryan. Nat Chem Biol. 15(11):1043-1048, 2019.
  5. A Heme-Dependent Enzyme Forms the Nitrogen-Nitrogen Bond in Piperazate. Y.L. Du, H.Y. He, M.A. Higgins, K.S. Ryan. Nat Chem Biol. 13(8):836-838, 2017.

Research Interests

​The Higgins lab uses microbiology, biochemistry, and structural biology techniques to gain a better understanding of microbial enzymes involved in glycan degradation and natural product biosynthesis. More specifically, we are interested in how commensal bacteria degrade host glycans, such as gut-associated mucin and N-glycans. In addition, we study sugar and pseudo sugar natural product biosynthetic enzymes and use amino acid sequence analysis with genome mining approaches to identify biosynthetic gene clusters that likely produce novel compounds and contain enzymes that catalyze unique biochemical reactions. 
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