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Dr Naomi Bishop
Cell biology and molecular pathogenesis

Contact details

Room 127, Thomas Cherry Building
Department of Microbiology
Faculty of Science, Technology and Engineering
La Trobe University Victoria 3086
AUSTRALIA

Office Phone: +61 3 9479 2232
Departmental Enquiries: + 61 9479 1114
Cell Biology in Health & Disease Lab: +61 3 9479 1401
Eukaryotic Genomics Lab: + 61 3 9479 1212
Molecular & Cellular Virology Lab: +61 3 9479 1212
Fax: +61 3 9479 1222

Email: n.bishop@latrobe.edu.au

Research areas

Cell biology encompasses all aspects of the control of cell structure and function. Sequencing the human genome has revealed each cell contains more than a million components, with each person containing billions of cells, and many of these have specialized functions. Our challenge is in understanding how these components interact and mediate the various aspects of cell function.

One of the most distinguishing characteristics of eukaryotic cells is the presence of membrane-bound compartment, or organelles, in the cytoplasm. Each organelle contains a distinct set of proteins and lipids, and these give each organelle a characteristic structure and function. Proteins and lipids typically move from organelle to organelle using transport vesicles, a process described as membrane traffic. Cell function and survival relies of the accuracy and correct function of unless the transport machinery. Around one third of the human genome encodes proteins involved in these processes.

Organelles in the secretory and endocytic pathways include the plasma membrane, endosomes, lysosomes, the endoplasmic reticulum, Golgi apparatus, and autophagosomes. Importantly, malfunction of membrane traffic along these pathways is linked to certain diseases. Identifying the molecular mechanisms of transport and sorting along the endocytic pathway and the role of these processes in disease is the focus of the Cell Biology in Health and Disease Laboratory. Viruses and other pathogens are known to hijack these pathways to facilitate various aspects of their replication in eukaryotic host cells, and this is the focus of the Molecular & Cellular Pathogenesis Laboratory. Further studies on the host cell proteins we identify in the Cell Biology in Health and Disease and Molecular & Cellular Pathogenesis Laboratories are carried out in the Eukaryotic Genomics Laboratory.

Genomics is the study of genes and their function, and our research includes: (a) Functional genomics, where genes, their mRNAs and protein products are studied in detail; (b) Structural genomics, where the motifs and domains, within the gene products and their structures are examined; and (c) Comparative genomics, where the evolutionary relationship between genes and proteins of interest, are analysed across a wide range of eukaryotic species.

Recent Publications

  • Slater R. & Bishop N.E. (2006) Genetic structure and evolution of the Vps25 family, a yeast ESCRT-II component. BMC Evolutionary Biology, 6: 59.
  • Monie T.P., Greatorex J.S., Hook B.D., Bishop N., Beales L P. & A.M. Lever. (2005). Identification and visualisation of the dimerisation initiation site of the prototype lentivirus, Maedi Visna virus: a potential GACG tetraloop displays structural homology with the α- and γ-retroviruses. Biochemistry, 44: 294-302.
  • Bishop N.E. (2003) Role of ubiquitin in sorting along the endocytic pathway. Recent Research Developments in Cell Research, 1: 45-65.
  • Bishop N.E. (2003) Dynamics of endosomal sorting. International Review of Cytology, 232: 1-57.
  • Bishop N., Horman A. & Woodman P. (2002) Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates. Journal of Cell Biology, 157: 91-101.
  • Bishop N, & Woodman P. (2001) TSG101/mammalian VPS23 and mammalian VPS28 interact directly and are recruited to VPS4-induced endosomes. Journal of Biological Chemistry, 276: 11735-42.
  • Bishop N.E. (2000) Identification of an intermediate in the hepatitis A virus uncoating process. Intervirology, 43: 36-47.
  • Bishop N.E. & Anderson D. A. (2000) Uncoating of hepatitis A virus virions and provirions. Journal of Virology, 74: 3423-3426.
  • Bishop, N. & Woodman, P. (2000) ATPase-defective mammalian VPS4 localizes to aberrant endosomes and impairs cholesterol trafficking. Molecular Biology of the Cell, 11: 227-239.
  • Swanton, E., Bishop, N. & Woodman, P. (2000) Disassembly of membrane-associated NSF 20S complexes is slow relative to vesicle fusion and is Ca2+-independent. Journal of Cell Science, 113: 1783-1791.
  • Bishop N.E. (1999) Conformational changes in the hepatitis A virus capsid in response to acidic conditions. Journal of Medical Microbiology, 48: 433-450.
  • Swanton, E., Bishop, N. & Woodman, P. (1999) Human rabaptin-5 is selectively cleaved by caspase-3 during apoptosis. Journal of Biological Chemistry, 274: 37583-37590.
  • Bishop, N. (1999) Unusual aspects of hepatitis A virus replication. Recent Research Developments in Virology, 1: 183-202.
  • Bishop, N. E. (1999) Effect of low pH on the intramolecular cleavage of hepatitis A virus VP0 molecule. Acta Virologica, 43: 291-296.
  • Bishop N.E. (1998) Examination of potential inhibitors of Hepatitis A virus uncoating. Intervirology, 42: 233-288.
  • Swanton, E., Sheehan, J., Bishop, N., High, S. & Woodman, P. (1998) Formation and turnover of NSF- and SNAP-containing 'fusion' complexes occur on undocked, clathrin-coated vesicle-derived membranes. Molecular Biology of the Cell, 9: 1633-1647.
  • Bishop N.E. (1997) An update on non-clathrin coated endocytosis. Reviews in Medical Virology, 7: 199-209.
  • Bishop N.E. & Anderson, D.A. (1997) Hepatitis A virus subviral particles: purification, accumulation, and relative infectivity of virions, provirions and procapsids. Archives of Virology, 142: 2147-2160.
  • Bishop N.E. & Anderson D.A. (1997) Early interactions of hepatitis A virus with cultured cells: viral elution and the effect of pH and calcium ions. Archives of Virology, 142: 2161-2178.
  • Bishop N.E. & Lever, A.M. (1996) Characterization and modification of an infectious maedi-visna virus clone. In Retroviruses, eds. Desrosiers, R. & Skalka, A.M. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
  • Bishop N.E., Hugo D.L., Borovec, S.V. & Anderson D.A. (1994) Rapid and efficient purification of hepatitis A virus from cell culture. Journal of Virological Methods, 47: 203-216.
  • Bishop N.E. & Anderson D. A. (1993) RNA-dependent cleavage of VP0 capsid protein of hepatitis A virus. Virology, 197: 616-623.
  • Civitico G., Wang Y., Luscombe C., Bishop N., Tachedjian G., Gust I. & Locarnini S. (1990) Antiviral strategies in chronic hepatitis B virus infection: inhibition of duck hepatitis B virus in vitro using conventional antiviral agents and supercoiled-DNA active compounds. Journal of Medical Virology, 31: 90-97.
  • Bishop N., Civitico G., Wang Y., Guo K., Birch C., Gust I. & Locarnini S. (1990) Antiviral strategies in chronic hepatitis B virus infection: establishment of an in vitro system using the duck hepatitis B virus model. Journal of Medical Virology, 31: 82-89.

Content approved by: Naomi Bishop
Page maintained by: Craig Lighton
Last updated: 11 June, 2008