Thomas Proft

Prof. Dr. Thomas Proft

The University of Auckland
orcid

Research Focus & Metrics

Academic Career Length

33Years (1994-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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9 February 2016 in Virulence
Verified
Journal Article
Open access
CTCatherine Jia-Yun Tsai
Catherine Jia-Yun Tsai
JLJacelyn Loh
Jacelyn Loh
Thomas ProftThomas Proft
Thomas Proft
Galleria mellonella (greater wax moth or honeycomb moth) has been introduced as an alternative model to study microbial infections. G. mellonella larvae can be easily and inexpensively obtained in large numbers and are simple to use as they don't require special lab equipment. There are no ethical constraints and their short life cycle makes them ideal for large-scale studies. Although insects lack an adaptive immune response, their innate immune response shows remarkable similarities with the immune response in vertebrates. This review gives a current update of what is known about the immune system of G. mellonella and provides an extensive overview of how G. mellonella is used to study the virulence of Gram-positive and Gram-negative bacteria. In addition, the use of G. mellonella to evaluate the efficacy of antimicrobial agents and experimental phage therapy are also discussed. The review concludes with a critical assessment of the current limitatons of G. mellonella infection models.

27 October 2008 in Cellular and Molecular Life Sciences
Verified
Journal Article
Closed access
PDF file
Thomas ProftThomas Proft
Thomas Proft
EBE. N. Baker
E. N. Baker

19 September 2008 in Immunological Reviews
Verified
Journal Article
Closed access
PDF file
JFJohn D. Fraser
John D. Fraser
Thomas ProftThomas Proft
Thomas Proft

7 December 2007 in Science
Verified
Journal Article
Closed access
PDF file
HKHae Joo Kang
Hae Joo Kang
FCFasseli Coulibaly
Fasseli Coulibaly
FCFiona Clow
Fiona Clow
Thomas ProftThomas Proft
Thomas Proft
EBEdward N. Baker
Edward N. Baker
Many bacterial pathogens have long, slender pili through which they adhere to host cells. The crystal structure of the major pilin subunit from the Gram-positive human pathogen Streptococcus pyogenes at 2.2 angstroms resolution reveals an extended structure comprising two all-β domains. The molecules associate in columns through the crystal, with each carboxyl terminus adjacent to a conserved lysine of the next molecule. This lysine forms the isopeptide bonds that link the subunits in native pili, validating the relevance of the crystal assembly. Each subunit contains two lysine-asparagine isopeptide bonds generated by an intramolecular reaction, and we find evidence for similar isopeptide bonds in other cell surface proteins of Gram-positive bacteria. The present structure explains the strength and stability of such Gram-positive pili and could facilitate vaccine development.

19 August 2003 in Clinical and Experimental Immunology
Verified
Journal Article
Closed access
PDF file
Thomas ProftThomas Proft
Thomas Proft
JFJ. D. Fraser
J. D. Fraser

1 July 2013 in Virulence
Verified
Journal Article
Open access
JLJacelyn Ms Loh
Jacelyn Ms Loh
NANazneen Adenwalla
Nazneen Adenwalla
Siouxsie WilesSiouxsie Wiles
Siouxsie Wiles
Thomas ProftThomas Proft
Thomas Proft
Group A streptococcus is a strict human pathogen that can cause a wide range of diseases, such as tonsillitis, impetigo, necrotizing fasciitis, toxic shock, and acute rheumatic fever. Modeling huma...