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Michael Klemba

Michael Klemba

· Associate Professor and Director of Biochemistry Study Abroad Programs: Biochemistry and Drug Discovery of Malaria

Virginia Tech · Biochemistry

Active 1992–2026

h-index29
Citations3.9k
Papers564 last 5y
Funding$1.5M

Academic metrics are sourced from OpenAlex and public funding records; values may differ from Google Scholar.

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About

Michael Klemba is an Associate Professor in the Department of Biochemistry at Virginia Tech, where he also serves as the Director of Biochemistry Study Abroad Programs. His research focuses on understanding how the human malaria parasite Plasmodium falciparum thrives in its host red blood cell. He employs biochemical and cell biological approaches to study various aspects of the parasite's biology, including the identification of the target of antimalarial compounds such as mefloquine, fatty acid uptake and lipid metabolism, endocytosis and hemoglobin catabolism, lipid utilization, protein sorting and trafficking within the parasite, and mechanisms of action of antimalarial compounds. Dr. Klemba's work aims to elucidate the metabolic pathways and molecular mechanisms that support parasite survival and proliferation, contributing to the development of new therapeutic strategies against malaria. He has been a faculty member at Virginia Tech since 2005, progressing from Assistant Professor to Associate Professor, and has taught courses in biochemistry and molecular life sciences, mentoring undergraduate and graduate students in research.

Research topics

  • Biochemistry
  • Immunology
  • Biology
  • Cell biology
  • Pharmacology
  • Chemistry
  • Stereochemistry
  • Combinatorial chemistry

Selected publications

  • Isoprenoid Precursor Biosynthesis Is the Essential Metabolic Role of the Apicoplast during Gametocytogenesis in Plasmodium falciparum

    Eukaryotic Cell · 2014-12-02 · 55 citations

    articleOpen access

    The malaria parasite harbors a relict plastid called the apicoplast and its discovery opened a new avenue for drug discovery and development due to its unusual, nonmammalian metabolism. The apicoplast is essential during the asexual intraerythrocytic and hepatic stages of the parasite, and there is strong evidence supporting its essential metabolic role during the mosquito stages of the parasite. Supply of the isoprenoid building blocks isopentenyl diphosphate (IPP) and dimethylallyl diphosphate…

  • Comparative Proteomics and Functional Analysis Reveal a Role of Plasmodium falciparum Osmiophilic Bodies in Malaria Parasite Transmission

    Molecular & Cellular Proteomics · 2016-07-18 · 51 citations

    articleOpen access

    An essential step in the transmission of the malaria parasite to the Anopheles vector is the transformation of the mature gametocytes into gametes in the mosquito gut, where they egress from the erythrocytes and mate to produce a zygote, which matures into a motile ookinete. Osmiophilic bodies are electron dense secretory organelles of the female gametocytes which discharge their contents during gamete formation, suggestive of a role in gamete egress. Only one protein with no functional annotati…

  • Evidence for a Golgi-to-Endosome Protein Sorting Pathway in Plasmodium falciparum

    PLoS ONE · 2014-02-25 · 49 citations

    articleOpen accessSenior authorCorresponding

    During the asexual intraerythrocytic stage, the malaria parasite Plasmodium falciparum must traffic newly-synthesized proteins to a broad array of destinations within and beyond the parasite's plasma membrane. In this study, we have localized two well-conserved protein components of eukaryotic endosomes, the retromer complex and the small GTPase Rab7, to define a previously-undescribed endosomal compartment in P. falciparum. Retromer and Rab7 co-localized to a small number of punctate structures…

  • Unnatural amino acids increase activity and specificity of synthetic substrates for human and malarial cathepsin C

    Amino Acids · 2013-12-31 · 41 citations

    articleOpen access

    Mammalian cathepsin C is primarily responsible for the removal of N-terminal dipeptides and activation of several serine proteases in inflammatory or immune cells, while its malarial parasite ortholog dipeptidyl aminopeptidase 1 plays a crucial role in catabolizing the hemoglobin of its host erythrocyte. In this report, we describe the systematic substrate specificity analysis of three cathepsin C orthologs from Homo sapiens (human), Bos taurus (bovine) and Plasmodium falciparum (malaria parasit…

  • Evidence for Regulation of Hemoglobin Metabolism and Intracellular Ionic Flux by the Plasmodium falciparum Chloroquine Resistance Transporter

    Scientific Reports · 2018-09-05 · 29 citations

    articleOpen access

    Abstract Plasmodium falciparum multidrug resistance constitutes a major obstacle to the global malaria elimination campaign. Specific mutations in the Plasmodium falciparum chloroquine resistance transporter (PfCRT) mediate resistance to the 4-aminoquinoline drug chloroquine and impact parasite susceptibility to several partner agents used in current artemisinin-based combination therapies, including amodiaquine. By examining gene-edited parasites, we report that the ability of the wide-spread D…

Recent grants

Frequent coauthors

  • Daniel E. Goldberg

    40 shared
  • Puran Singh Sijwali

    Centre for Cellular and Molecular Biology

    25 shared
  • Kentaro Kato

    Tohoku University

    25 shared
  • Louis H. Miller

    National Institute of Allergy and Infectious Diseases

    25 shared
  • Julie Lehman

    San Francisco General Hospital

    25 shared
  • Karl B. Seydel

    Kamuzu University of Health Sciences

    25 shared
  • Jiří Gut

    San Francisco General Hospital

    25 shared
  • Philip J. Rosenthal

    University of California, San Francisco

    25 shared

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