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Monash University > Medicine, Nursing and Health Sciences > Department of Biochemistry and Molecular Biology > Staff >

Viral Immune Evasion Laboratory

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Dr Natalie Borg

NHMRC Career Development Fellow

natalie borg

Tel:     +61 3 990 29369
Fax:    +61 3 990 29500
Office: Building 77, Room 247

Email: natalie.borg@monash.edu

Research Group Members:
Luke Cossins    (Research Assistant)
Leigh Yang        (PhD student co-supervised with Stephen Bottomley)
Steven Heaton  (PhD student)

The Role of Proteins Involved in Anti-Viral Immunity

Proteins are an essential component of all living organisms and so they must function correctly to prevent disease. As the function of a protein is directly related to its shape, the Borg laboratory uses a combined functional/structural approach to understand the functional biology and structure of proteins important in human health. This predominantly involves proteins involved in anti-viral immunity.

Techniques used within the laboratory include molecular biology, recombinant protein expression using insect and bacterial cells, protein purification using a Fast Protein Liquid Chromatography system, X-ray crystallography and protein-protein interaction analysis (eg. surface plasmon resonance, enzyme assays). Cellular assays are also used to characterize gene expression, regulation and localization and to study our innate immune response to viral infection.

Predominant Research Area

Our immune system has a first line of defense that is critical in detecting viral infections and triggering an anti-viral immune response. The RIG-like helicases (RLH) are one of two families of receptors involved in anti-viral immunity. These receptors recognize RNA ligands from prominent viruses like influenza, measles, mumps and hepatitis C, become activated and launch a complex signaling cascade that involves numerous protein molecules. The end result of this process is the release of NF-κB and the synthesis and secretion of type I interferons, which are key mediators in anti-viral immunity. In order to avoid harming the host, this immune response must be a tightly controlled, dynamic process that is initiated and regulated upon viral infection and terminated when not required. This remarkable feat is partly achieved by the balance between the addition and removal of ubiquitin-like proteins to particular proteins throughout the signaling cascade. These modifications essentially act as ‘on/off' switches that can initiate, regulate and terminate immune signaling. Their importance in regulating the immune system is reflected by the ability of viruses to manipulate these signals so as to avoid detection and enhance their own survival.

We are interested in the study of viral or host proteins that are involved in the regulation of the anti-viral immune response. This information will enable us to better understand anti-viral immunity which is crucial to the treatment and prevention of viral infection.

Opportunities in the Borg Lab

Potential honours and PhD students are welcome to drop by and chat at any time.

Link

L'Oréal Australia For Women in Science Award

 

Selected Publications

Paxman, J.J., Borg, N.A., Horne, J., Thompson, P.E., Chin, Y., Sharma, P., Simpson, J.S., Wielens, J., Piek, S., Kahler, C., Sakellaris, H., Pearce, M., Bottomley, S.P., Rossjohn, J., Scanlon, M.J. (2009). The structure of the bacterial oxidoreductase enzyme DsbA in complex with a peptide reveals a basis for substrate specificity in the catalytic cycle of DsbA enzymes. J. Biol. Chem. 284(26), 17835-17845

Borg, N.A*., Wun, K.S*., Kjer-Nielsen, L., Beddoe, T., Koh, R., Richardson, S.K., Thakur, M., Howell, A.R., Scott-Browne, J.P., Gapin, L., Godfrey, D.I., McCluskey, J., Rossjohn, J. (2008). A minimal binding footprint on CD1d-glycolipid is a basis for selection of the unique human NKT TCR. J. Exp Med. 205(4), 939-949.

Borg, N.A., Wun, K.S., Kjer-Nielsen, L., Wilce, M.C.J., Pellici, D.G., Koh, R., Besra, G.S., Bharadwaj, M., Godfrey, D.I., McCluskey, J., Rossjohn, J.  (2007).  CD1d-lipid antigen recognition by the semi-invariant NKT cell receptor.  Nature. 448 (7149), 44-49.

Borg, N.A*., Kjer-Nielsen, L*., Pellicci, D.G., Beddoe, T., Kostenko, L., Clements, C.S., Williamson, N.A., Smyth, M.J.,  Besra, G.S., Reid, H.H., Bharadwaj, M., Godfrey, D.I., Rossjohn, J., McCluskey, J. (2006). A structural basis for selection and cross-species reactivity of the semi-invariant NKT cell receptor in CD1d-mediated antigen recognition.  J. Exp. Med. 203 (3), 661-673.

Borg, N.A*., Ely, L.K*., Beddoe, T., MacDonald, W.A., Reid, H.H., Clements, C.S., Purcell, A.W., Kjer-Nielsen, L., Miles, J.J., Burrows, S.R., McCluskey, J. and Rossjohn, J. (2005).  The CDR3 regions of an immunodominant ab T cell receptor dictate the ‘energetic landscape’ of peptide-MHC recognition.  Nat. Immunol. 6 (2), 171-180.

Book Chapter

Borg, N.A., Kjer-Nielsen, L., McCluskey, J., Rossjohn, J. A structurally sound insight into natural killer T cell receptor recognition of CD1d. In Advances in Experimental Medicine and Biology, Vol. 598. Chapter 3.  Lambris, J.D. (Ed.).  2007, XVI, 438 p.98.

 

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