Infection Medicine

Dr Vasso Makrantoni

My laboratory's work focuses on how human fungal pathogens adapt and thrive under different stress conditions.

Dr Vasso Makrantoni

Academic Track Lecturer (Edinburgh-Zhejiang)

  • Infection Medicine
  • Deanery of Biomedical Sciences
  • Edinburgh Medical School

Contact details

Address

Street

The University of Edinburgh
Centre for Inflammation Research
Institute for Regeneration and Repair
Edinburgh BioQuarter
4-5 Little France Drive

City
Edinburgh
Post Code
EH16 4UU

Personal Profile

Dr Vasso Makrantoni is a Lecturer in Infection Medicine and holds a joint appointment at the Zhejiang University - University of Edinburgh Institute (ZJU-UoE). Following undergraduate studies at the Aristotle University of Thessaloniki in Greece, Vasso obtained her PhD degree from St Andrews University and then undertook postdoctoral research first at the Centre for Gene Regulation & Expression in Dundee and then at the Wellcome Centre for Cell Biology in Edinburgh. She started her own lab in Infection Medicine in 2021.

Teaching

Vasso is involved in developing and delivering undergraduate teaching at the Zhejiang University-University of Edinburgh Institute.

Research

Research in our laboratory focuses on how human fungal pathogens adapt and thrive under different stress conditions. We study this in Candida albicans, one of the most successful opportunistic human pathogens responsible for millions of infections every year.  Candida has an unusual life cycle existing as a yeast, pseudohyphae and true hyphae,  while under stress conditions its cell division  leads to aneuploidy (an incorrect number of chromosomes). This remarkable genomic plasticity allows Candida to rapidly adapt in diverse host environments and acquire antifungal drug resistance. Our main goal is to understand the molecular mechanisms that regulate aneuploidy using molecular genetics, biochemistry, live-cell imaging and whole genome sequencing. Ultimately, we envision to uncover new therapeutic strategies to combat Candida infections.

Research Themes

Current Funding Sources

Lab Members

Collaborators

Recent Publications

  1. Kuhl LM., Makrantoni V., Recknagel S., Vaze AN., Marston AL and Vader G. (2020). A dCas9/CRISPR-based targeting system identifies a central role for Ctf19 in kinetochore-derived suppression of meiotic recombination. Genetics. 216: 395-408
  2. Hsieh YYP., Makrantoni V., Robertson D., Marston AL., Murray AW. (2020). Evolutionary repair: changes in multiple functional modules allow meiotic cohesion to support mitosis.  PLoS Biol.10;18:e3000635
  3. Makrantoni V and Marston AL. (2018). Cohesin and chromosome segregation. Curr. Biol. 28, R688-R693
  4. Hinshaw S*., Makrantoni V*., Harrison SC., Marston AL. (2017). The Kinetochore Receptor for the Cohesin loading complex. Cell. 171, 72-84 (* equal contributions)
  5. Makrantoni V., Ciesiolka A., Lawless C., Fernius J., Marston AL., Lydall D., Stark MJR. (2017). A functional link between Bir1 and the S. cerevisiae Ctf19 kinetochore complex revealed through Quantitative Fitness Analysis. G3 (Bethesda).7, 3203-3215.
  6. Hinshaw S., Makrantoni V., Kerr A., Marston AL., Harrison SC. (2015). Structural evidence for Scc4-dependent localization of cohesin. eLife. doi: 10.7554/eLife.06057
  7. Makrantoni V., Corbishley SJ., Rachidi N., Morrice NA., Robinson DA., Stark MJ. (2014).  Phosphorylation of Sli15 by Ipl1 is important for proper CPC localization and chromosome stability in S. cerevisiae. PLoS ONE. 9(2): e89399
  8. Makrantoni V and Stark, MJR. (2009). Efficient chromosome bi-orientation and the tension checkpoint in S. cerevisiae both require Bir1. Mol Cell Biol. 29, 4552-62
  9. Fox, GC., Shafiq, M., Briggs, DC., Knowles, PP., Collister, M., Didmon, M., Makrantoni V., Dickinson, RJ., Hanrahan, S., Totty, N., Stark, MJR., Keyse, SM., McDonald, NQ. (2007). Redox-mediated substrate recognition by Sdp1 defines a new group of Tyr phosphatases. Nature. 447, 487-92
  10. Rudolf, J., Makrantoni V., Ingledew, J., Stark, MJR and White, MW. (2006). The DNA Repair Helicases XPD and FancJ have essential Iron-Sulphur Domains. Mol Cell. 23,1-8