Dr Parimala Vajjhala
Dr

Parimala Vajjhala

Email: 
Phone: 
+61 7 336 54881

Availability

Dr Parimala Vajjhala is:
Available for supervision

Fields of research

Biological Sciences Microbiology

Qualifications

  • Bachelor of Science, The University of Queensland
  • Bachelor (Honours) of Science (Advanced), The University of Queensland
  • Doctor of Philosophy, The University of Queensland

Research interests

  • .

    My current research focuses on understanding the mechanisms of activation of pattern recognition receptors (PRRs) of the innate immune system and the signalling complexes that they initiate. The innate immune system plays a key role in the initial defence of a host against pathogens as well as in the activation of the adaptive immune system. In addition to being activated by pathogen-associated molecular patterns (PAMPs), some PRRs are activated by endogenous damage-associated molecular patterns (DAMPs), also known as danger-associated molecular patterns. Excessive activation of certain PRRs can lead to inflammation and cell death, which are implicated in the pathology of infectious and non-infectious diseases. Thus, a detailed understanding of the activation of PRRs and the complexes that mediate inflammation and cell death may lead to the development of novel therapies.

  • .

    I have worked on inflammasome complexes that assemble upon activation of cytosolic PRRs including AIM2, which is activated by cytosolic DNA, and NLRP3, which is activated by a wide range of PAMPs and DAMPs. Inflammasomes recruit and activate caspase-1, which cleaves pro-inflammatory cytokines to their active forms that mediate inflammation, as well as caspase-8, which mediates apoptosis. Deregulated inflammasome function is implicated in the pathogenesis of common diseases including atherosclerosis, obesity, diabetes and Alzheimer’s disease, as well as kidney and liver diseases. My work, under the guidance of Assoc. Prof. Katryn Stacey (SCMB, UQ) and Dr. Justine Hill (formerly SCMB, UQ) and also in collaboration with Prof. Hao Wu (Harvard Medical School), has given key insights into the death-fold domain interactions that mediate inflammasome assembly and into the recruitment and activation of caspases. I also contributed to the development of a novel flow cytometry based assay to quantify inflammasome assembly.

  • .

    More recently, I have worked on Toll-like receptor 4 (TLR4) activation. TLR4 is a plasma membrane PRR best known for mediating an inflammatory response to the lipopolysaccharide (LPS) of the outer membrane of Gram-negative bacteria. Although TLR4 activation induces release of proinflammatory cytokines that can be protective, dysregulated TLR4 responses can lead to life-threatening systemic inflammation. TLR4 is also activated by endogenous molecules and promotes the pathology of non-infectious diseases including atherosclerosis, obesity, diabetes, Alzheimer’s disease, rheumatoid arthritis, epilepsy and ischemia/reperfusion injury. Upon activation, the intracellular TIR domain of TLR4 recruits adaptor proteins with TIR domains including MAL and MyD88. The complexes formed initiate downstream signalling pathways. In a project, which is a collaboration with Prof. Bostjan Kobe (SCMB, UQ), Dr. Thomas Ve (Griffith University) and Assoc. Prof. Katryn Stacey (SCMB, UQ), the interaction interfaces of MAL TIR and MyD88 TIR were defined. These studies have given key insights into assembly of TLR4 signalling complexes.

Search Professor Parimala Vajjhala’s works on UQ eSpace

30 works between 2001 and 2025
All (30) Journal Article (24) Book Chapter (1) Conference Publication (4) Other Outputs (1)

21 - 30 of 30 works

2012

Journal Article

Multiple Binding Sites on the Pyrin Domain of ASC Protein Allow Self-association and Interaction with NLRP3 Protein

Vajjhala, Parimala R., Mirams, Ruth E. and Hill, Justine M. (2012). Multiple Binding Sites on the Pyrin Domain of ASC Protein Allow Self-association and Interaction with NLRP3 Protein. Journal of Biological Chemistry, 287 (50), 41732-41743. doi: 10.1074/jbc.M112.381228

Multiple Binding Sites on the Pyrin Domain of ASC Protein Allow Self-association and Interaction with NLRP3 Protein

2009

Journal Article

Three-dimensional structure of AAA ATPase Vps4: Advancing structural insights into the mechanisms of endosomal sorting and enveloped virus budding

Landsberg, Michael J., Vajjhala, Parimala Rao, Rothnagel, Rosalba, Munn, Alan Leslie and Hankamer, Ben (2009). Three-dimensional structure of AAA ATPase Vps4: Advancing structural insights into the mechanisms of endosomal sorting and enveloped virus budding. Structure, 17 (3), 427-437. doi: 10.1016/j.str.2008.12.020

Three-dimensional structure of AAA ATPase Vps4: Advancing structural insights into the mechanisms of endosomal sorting and enveloped virus budding

2008

Journal Article

The Vps4 C-terminal helix is a critical determinant for assembly and ATPase activity and has elements conserved in other members of the meiotic clade of AAA ATPases.

Vajjhala, P. R., Nguyen , C. H., Landsberg, M. J., Kistler, C., Gan, A. L., King, G. F., Hankamer, B. and Munn, A. L. (2008). The Vps4 C-terminal helix is a critical determinant for assembly and ATPase activity and has elements conserved in other members of the meiotic clade of AAA ATPases.. Febs Journal, 275 (7), 1427-1449. doi: 10.1111/j.1742-4658.2008.06300.x

The Vps4 C-terminal helix is a critical determinant for assembly and ATPase activity and has elements conserved in other members of the meiotic clade of AAA ATPases.

2007

Journal Article

Vps4 regulates a subset of protein interactions at the multivesicular endosome

Vajjhala, P. R., Catchpoole, E., Nguyen, C. H., Kistler, C. and Munn, A. L. (2007). Vps4 regulates a subset of protein interactions at the multivesicular endosome. FEBS Journal, 274 (8), 1894-1907. doi: 10.1111/j.1742-4658.2007.05736.x

Vps4 regulates a subset of protein interactions at the multivesicular endosome

2007

Journal Article

Host factors in virus budding - Insights from yeast

Vajjhala, P. R. and Munn, A. (2007). Host factors in virus budding - Insights from yeast. Microbiology Australia, May 2007, 44-47.

Host factors in virus budding - Insights from yeast

2007

Journal Article

Verprolin function in endocytosis and actin organization - Roles of the Las17p (yeast WASP)-binding domain and a novel C-terminal actin-binding domain

Thanabalu, T., Rajmohan, R., Meng, L., Ren, G., Vajjhala, P. R. and Munn, A. L. (2007). Verprolin function in endocytosis and actin organization - Roles of the Las17p (yeast WASP)-binding domain and a novel C-terminal actin-binding domain. FEBS Journal, 274 (16), 4103-4125. doi: 10.1111/j.1742-4658.2007.05936.x

Verprolin function in endocytosis and actin organization - Roles of the Las17p (yeast WASP)-binding domain and a novel C-terminal actin-binding domain

2006

Journal Article

The β domain is required for Vps4p oligomerization into a functionally active ATPase

Vajjhala, Parimala R., Wong, Julin S., To, Hui-Yi and Munn, Alan L. (2006). The β domain is required for Vps4p oligomerization into a functionally active ATPase. The Febs Journal, 273 (11), 2357-2373. doi: 10.1111/j.1742-4658.2006.05238.x

The β domain is required for Vps4p oligomerization into a functionally active ATPase

2006

Journal Article

The BAR domain proteins: Molding membranes in fission, fusion, and phagy

Ren, G., Vajjhala, P., Lee, J. S., Winsor, B. and Munn, A. L. (2006). The BAR domain proteins: Molding membranes in fission, fusion, and phagy. Microbiology And Molecular Biology Reviews, 70 (1), 37-120. doi: 10.1128/MMBR.70.1.37-120.2006

The BAR domain proteins: Molding membranes in fission, fusion, and phagy

2003

Journal Article

The Wilms' Tumour Suppressor Protein, WT1, Undergoes CRM1-independent Nucleocytoplasmic Shuttling

Vajjhala, P. R., Macmillan, E., Gonda, T. and Little, M. H. (2003). The Wilms' Tumour Suppressor Protein, WT1, Undergoes CRM1-independent Nucleocytoplasmic Shuttling. FEBS Letters, 554 (1-2), 143-148. doi: 10.1016/S0014-5793(03)01144-X

The Wilms' Tumour Suppressor Protein, WT1, Undergoes CRM1-independent Nucleocytoplasmic Shuttling

2001

Other Outputs

Expression and characterisation of proteins engineered with Farnesyl groups

Vajjhala, Parimala Rao (2001). Expression and characterisation of proteins engineered with Farnesyl groups. PhD Thesis, School of Molecular and Microbial Sciences, The University of Queensland. doi: 10.14264/105596

Expression and characterisation of proteins engineered with Farnesyl groups

Current funding

  • 2021 - 2025
    Mammalian endotoxin: Characterisation of highly inflammatory endogenous material
    NHMRC IDEAS Grants
    Open grant

Availability

Dr Parimala Vajjhala is:
Available for supervision

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Supervision history

Current supervision

  • Doctor Philosophy

    Toll-like receptor signalling mechanisms

    Associate Advisor

    Other advisors: Professor Kate Stacey

  • Doctor Philosophy

    Toll-like receptor signalling mechanisms

    Associate Advisor

    Other advisors: Professor Kate Stacey

  • Doctor Philosophy

    Molecular analysis of adapter protein interaction with Toll-like receptors

    Associate Advisor

    Other advisors: Professor Kate Stacey

  • Doctor Philosophy

    Structural and functional analysis of TIR domain enzymatic activity

    Associate Advisor

    Other advisors: Professor Kate Stacey, Professor Bostjan Kobe

Completed supervision

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