Dr. Pau Biak Sang
Assistant Professor
Biotech Building, Ground Floor
University of Delhi, South Campus
Benito Juarez Road, Delhi-110021
Email: pbsang@microbio.du.ac.in
Phone: 011-24157169 (Office)
Area of research: DNA repair, Molecular Biology
Research Description:
Our lab will work on the DNA repair system in Yeast using Candida glabrata as a model. Candida glabrata is a commensal fungus that can cause infection in immunocompromised patients. C. glabrata is the second most commonly isolated Candida spp in
clinical samples of Candidiasis after C. albicans. C. glabrata has been a pathogen of interest due to its high mortality rate and natural resistance to azole antifungals. Macrophages are the first line of defense against candida infection. Unlike C. albicans, C. glabrata can be easily ingested by the macrophage, where it can survive and even replicate inside the phagosomes. Macrophages are known to generate ROS, which can damage the cellular components of the pathogen, including DNA, and kill the pathogen. We are interested in the DNA glycosylase of C. glabrata, which is not yet characterized, and their role in the pathogen is not yet studied. C. glabrata is a haploid and less pathogenic compared to C. albicans. It is easier to generate knockouts and safer to work on this organism.
The Lab is also interested in methods for rapid detection of antimicrobial resistance.
Select Publications:
Sang PB, Jaiswal RK, Lyu X, Chai W. Human CST complex restricts excessive PrimPol repriming upon UV induced replication stress by suppressing p21. Nucleic Acids Res. 2024 Apr 24;52(7):3778-3793. doi: 10.1093/nar/gkae078
Lyu X, Sang PB, Chai W. CST in maintaining genome stability: Beyond telomeres. DNA Repair (Amst). 2021 Jun;102:103104. doi: 10.1016/j.dnarep.2021.103104.
Lyu X, Lei KH, Biak Sang P, Shiva O, Chastain M, Chi P, Chai W Human CST complex protects stalled replication forks by directly blocking MRE11 degradation of nascent-strand DNA EMBO J. 2021 Jan 15;40(2):e103654
Kurthkoti K, Kumar P, Sang PB, Varshney U. Base excision repair pathways of bacteria: new promise for an old problem. Future Medicinal Chemistry. 2020 Feb 7 doi: 10.4155/fmc-2019-0267
Ahn WC, Aroli S, Kim JH, Moon JH, Lee GS, Lee MH, Sang PB, Oh BH, Varshney U, Woo EJ. Covalent binding of uracil DNA glycosylase UdgX to abasic DNA upon uracil excision. Nat Chem Biol. 2019 Jun;15(6):607-614. doi: 10.1038/s41589-019-0289-3.
Sang PB, Srinath T, Patil AG, Woo EJ, Varshney U. A unique uracil-DNA binding protein of the uracil DNA glycosylase superfamily. Nucleic Acids Res. 2015 Sep 30;43(17):8452-63
Sang PB, Varshney U. (2013) Biochemical properties of MutT2 proteins from Mycobacterium tuberculosis and M. smegmatis and their contrasting antimutator roles in Escherichia coli. J Bacteriol. 2013 Apr;195(7):1552-60.
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