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Faculty
Matthew D. Weitzman
Associate Professor and Pioneer Developmental Chair
Laboratory of Genetics
Matthew D. Weitzman, an associate professor in the Laboratory of Genetics, is studying the interactions between viruses and their host cells. While the virus tries to commandeer the cellular machinery to aid its own replication, the host cell responds with defense systems that create obstacles for the virus. Watching these battles unfold has contributed significantly to our understanding of fundamental cellular mechanisms and has established viruses as powerful models to study cell biology. The lab is using human DNA viruses to study DNA damage responses, DNA repair, and innate antiviral defenses such as those provided by the APOBEC proteins.
Knowledge from viral systems can also be harnessed to alter the genetic makeup of cells. Viral vectors take advantage of the innate ability of viruses to transfer genetic material into target cells. Weitzman is developing novel delivery systems based upon DNA viral vectors that can be used for gene therapy applications.
Education
- B.Sc., Genetics, University of Leeds, U.K.
- Ph.D., NERC Institute of Virology and Oxford Polytechnic, UK
- Postdoctoral fellow, National Institutes of Health, Bethesda
- Research Associate, University of Pennsylvania Medical Center
Awards and Honors
- Visiting Fellowship at NIH, 1991-1993
- Cystic Fibrosis Postdoctoral Fellowship, 1994-1995
- Associate Member, Institute for Human Gene Therapy
- Young Investigator Award, American Society for Gene Therapy, 2004
Selected Publications
- Grifman, M, Trepel, M, Speece, P, Gilbert, LB, Arap, W, Pasqualini, R and Weitzman, MD (2001). Incorporation of tumor-targeting peptides into recombinant adeno-associated virus capsids. Mol Therapy, 3, 964-975.
- Cathomen, T, Stracker, T, Gilbert, L, and Weitzman, MD (2001). A genetic screen identifies a cellular regulator of adeno-associated virus. Proc Natl Acad Sci USA, 98, 14991-14996.
- Stracker, TH, Carson, CT and Weitzman, MD (2002). Adenovirus oncoproteins inactivate the Mre11-Rad50-NBS1 DNA repair complex. Nature, 418, 348- 352.
- Carson, CT, Schwartz, RA, Stracker, TH, Lilley, CE, Lee, DV and Weitzman, MD (2003). The Mre11 complex is required for ATM activation and the G2/M checkpoint. EMBO J, 22,6610-6620.
- Porteus, MH, Cathomen, T, Weitzman, MD and Baltimore, D (2003). Efficient gene targeting mediated by AAV and DNA double-strand breaks. Mol Cell Biology, 10, 3558-3565.
- Lilley, CE, Carson, CT, Muotri, AR, Gage, FH and Weitzman, MD (2005). DNA repair proteins affect the HSV-1 lifecycle. Proc Natl Acad Sci USA, 102, 5844-5849.
- Chen, H, Lilley, CE, Yu, Q, Lee, DV, Chou, J, Narvaiza, I, Landau, NR and Weitzman, MD (2006). APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons. Curr Bio 16, 480-485.
- Lilley, CE, Schwartz, RA and Weitzman, MD (2007). Using or Abusing: Viruses and the DNA damage response. Trends in Microbiology 15, 119-126.
- Carson, CT, Orazio, NI, Lee, DV, Suh, J, Bekker-Jensen, S, Araujo, FD, Lakdawala, SS, Lilley, CE, Bartek, J, Lukas, J and Weitzman, MD (2009). Mislocalization of the MRN complex prevents ATR signaling during adenovirus infection. EMBO J 28, 652-662.
- Schwartz, RA, Carson, CT, Schubert, C and Weitzman, MD (2009). Adeno-associated virus replication induces a DNA damage response coordinated by DNA-PK. J Virol 83, 6269-6278.
- Narvaiza, I, Linfesty, DC, Greener, BN, Hakata, Y, Pintel, DJ, Logue, E, Landau, NR, and Weitzman, MD (2009). Deaminase-independent inhibition of parvoviruses by the APOBEC3A cytidine deaminase. PLoS Pathog 5, e1000439.
- Chaurushiya, MS and Weitzman, MD (2009). Viral manipulation of DNA repair and cell cycle checkpoints. DNA Repair 8, 1166-1176.
- Lilley, CE, Chaurushiya, MS and Weitzman, MD (2009). Chromatin at the intersection of viral infection and DNA damage. BIOCHIMICA ET BIOPHYSICA ACTA [Epub ahead of print]
- Lilley, CE, Chaurushiya, MS, Boutell, C, Landry, S, Suh, J, Panier, S, Everett, RD, Stewart, GS, Durocher, D and Weitzman, MD (2010). A viral E3 ligase targets RNF8 and RNF168 to control histone ubiquitination and the cellular response to DNA damage. EMBO J (in press)