Dr Richard Lawrence Kingston

PhD (Massey)

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Senior Lecturer


Richard Kingston is a Senior Lecturer in Structural Biology and has been on the Auckland Faculty since 2005. He obtained his PhD in Biochemistry from Massey University, and was a postdoctoral fellow at Purdue University, and the University of Oregon, before returning to New Zealand.

Research | Current

  • Structural Biology of Enveloped RNA viruses
    Research in our laboratory involves two families of enveloped RNA viruses that cause infectious disease in humans, the paramyxoviruses and the retroviruses. Working primarily in vitro, we use biophysical and structural techniques to investigate virus architecture, assembly and replication. We are particularly interested in understanding the reversible molecular interactions which underpin these processes. For the paramyxoviruses, our primary model systems are measles and mumps viruses. We also study Rous sarcoma virus, the prototypical avian retrovirus.
    Details of our research can be found on our laboratory webpage.
  • Replication machinery of measles and mumps viruses
    Measles and mumps viruses are important human pathogens, especially in developing nations. Both are members of the paramyxovirus family, and they have a similar organization and mode of replication. Within the virion, the nucleocapsid protein packages their genomic RNA into a helical complex, termed the nucleocapsid.
    In the cytoplasm of an infected cell the viral RNA polymerase uses the nucleocapsid as the template for both transcription and genome replication. We are studying the organization of the viral polymerase, a large and complicated molecular machine. We are particularly interested in the way the polymerase engages and moves along the nucleocapsid during RNA synthesis.
  • Evasion of the innate immune response by measles and mumps viruses
    The interferon (IFN) family of cytokines plays a critical role in host defense against viral infection. Secreted from infected cells, IFNs activate protective functions in neighboring cells through the JAK-STAT signal transduction pathway.
    Paramyxoviruses have evolved mechanisms to counteract the IFN response, by encoding proteins that bind to and inactivate members of the signaling cascade, a process we seek to understand in molecular detail.
  • Assembly and organization of Rous sarcoma virus
    Rous sarcoma virus (RSV) is an avian retrovirus, closely related to human immunodeficiency virus (HIV). Retroviruses cause cancer and immune disorders in many species. In all such viruses, the Gag polyprotein directs formation and release of spherical virus particles.
    During or after budding, the polyprotein is cleaved by the viral protease, releasing the structural proteins found in the infectious retrovirus. This also results in a structural rearrangement of the virion interior, termed maturation, which is essential for infectivity.
    We are investigating the role of the Gag polyprotein, and its constituent domains, in retroviral assembly, in collaboration with the laboratory of Volker Vogt (Cornell University). We aim to identify Gag polyprotein assembly intermediates critical to the formation of spherical virus particles, and to understand the organization of the mature retroviral core, the large assemblage that incorporates the genomic RNA and the replicative enzymes in the infectious virion.


  • NZ HRC Hercus Fellowship

Areas of expertise

Structural Biology

Selected publications and creative works (Research Outputs)

  • Webby, M. N., Sullivan, M. P., Yegambaram, K. M., Radjainia, M., Keown, J. R., & Kingston, R. L. (2019). A method for analyzing the composition of viral nucleoprotein complexes, produced by heterologous expression in bacteria. Virology, 527, 159-168. 10.1016/j.virol.2018.11.013
    Other University of Auckland co-authors: Matthew Sullivan
  • Doktorova, M., Heberle, F. A., Kingston, R. L., Khelashvili, G., Cuendet, M. A., Wen, Y., ... Dick, R. A. (2017). Cholesterol promotes protein binding by affecting membrane electrostatics and solvation properties. Biophysical Journal, 113 (9), 2004-2015. 10.1016/j.bpj.2017.08.055
  • Hausrath, A. C., & Kingston, R. L. (2017). Conditionally disordered proteins: Bringing the environment back into the fold. Cellular and Molecular Life Sciences, 74 (17), 3149-3162. 10.1007/s00018-017-2558-1
  • Jaballah, S. A., Bailey, G. D., Desfosses, A., Hyun, J., Mitra, A. K., & Kingston, R. L. (2017). In vitro assembly of the Rous Sarcoma Virus capsid protein into hexamer tubes at physiological temperature. Scientific Reports, 7 (1)10.1038/s41598-017-02060-0
    URL: http://hdl.handle.net/2292/36114
    Other University of Auckland co-authors: Alok Mitra
  • Sullivan, M. P., Groessl, M., Meier, S. M., Kingston, R. L., Goldstone, D. C., & Hartinger, C. G. (2017). The metalation of hen egg white lysozyme impacts protein stability as shown by ion mobility mass spectrometry, differential scanning calorimetry, and X-ray crystallography. Chemical Communications, 53 (30), 4246-4249. 10.1039/c6cc10150j
    URL: http://hdl.handle.net/2292/42770
    Other University of Auckland co-authors: Christian Hartinger, David Goldstone, Matthew Sullivan
  • Jeon, J., Qiao, X., Hung, I., Mitra, A. K., Desfosses, A., Huang, D., ... Gan, Z. (2017). Structural model of the tubular assembly of the rous sarcoma virus capsid protein. Journal of the American Chemical Society, 139 (5), 2006-2013. 10.1021/jacs.6b11939
    Other University of Auckland co-authors: Alok Mitra
  • Lo, V. L., Kingston, R. L., & Millane, R. P. (2016). Iterative projection algorithms for ab initio phasing in virus crystallography. Journal of Structural Biology, 196 (3), 407-413. 10.1016/j.jsb.2016.09.004
    URL: http://hdl.handle.net/2292/32033
  • Lo, V. L., Kingston, R. L., & Millane, R. P. (2015). Iterative projection algorithms in protein crystallography. II. Application. Acta Crystallographica Section A: Foundations and Advances, 71 (Pt 4), 451-459. 10.1107/S2053273315005574


Contact details

Primary office location

Level 4, Room 4006
New Zealand

Web links