Jan Maree Tennent

Last updated

Jan Tennent
Born
Melbourne, Victoria, Australia
AwardsBoard Diversity Scholarship, Australian Government Office for Women, Australian Institute of Company Directors (2013)
Perpetual Trust Scholarship (2011)
Scientific career
FieldsBiomedical Research and Innovation
Institutions biomedvic.org.au

Jan Maree Tennent (born 1 January 1960) is an Australian scientist in the biomedical and animal health research sectors, and a member of the Australian Academy of Technology Science and Engineering. [1] [2]

Contents

Early life and education

Tennent was born in Footscray, Melbourne, Victoria on 1 January 1960. She obtained a Bachelor of Science, in microbiology from the Monash University in Melbourne in 1981. She completed her PhD in 1986 at Monash University. Her PhD thesis was entitled 'Molecular Analysis of Plasmids in Multi-resistant Staphylococci'.

Career

Tennent left Australia in 1986 to do a four-year postdoctoral fellowship with Prof Staffan Normark at Umeå University in Sweden. She researched the genetic mechanism and control of host attachment by uropathogenic Escherichia coli as part of the Normark laboratory's research. [3] [4] [5] [6] [7]

Tennet returned to Australia and joined the CSIRO as a senior research scientist. She became the program manager of the Vaccines and Immunology Group in 1997. Tennent has researched and given keynote presentations in the field of biotechnology and animal vaccines. [8]

In 2000, Tennent joined the global biotherapy organisation CSL Limited and later became a member of the CSL Animal Health executive team. Tennent joined the international pharmaceutical company Pfizer in 2004. In 2009, Tennent founded ConnectBio Pty Ltd. [9]

In 2011, Tennent was appointed as the Chief Executive Officer of Biomedical Research Victoria, a body that represents Australia's biomedical research. In 2017, Tennent was elected to the AusBiotech Board. [10]

Tennent has published 35 contributions in international peer-reviewed scientific journals (1984–2006) and eight reviews, theses and book chapters on microbial pathogenesis. [11] She served on research-related committees including the Genetic Manipulation Advisory Committee (now the Office of the Gene Technology Regulator) between 1995 and 2001.

Tennent worked at RMIT University and the University of Melbourne. In 2019, Tennent was elected Fellow of the Australian Academy of Technological Sciences and Engineering (FTSE). [12]

Related Research Articles

<span class="mw-page-title-main">Bacterial conjugation</span> Method of bacterial gene transfer

Bacterial conjugation is the transfer of genetic material between bacterial cells by direct cell-to-cell contact or by a bridge-like connection between two cells. This takes place through a pilus. It is a parasexual mode of reproduction in bacteria.

<span class="mw-page-title-main">Pilus</span> A proteinaceous hair-like appendage on the surface of bacteria

A pilus is a hair-like cell-surface appendage found on many bacteria and archaea. The terms pilus and fimbria can be used interchangeably, although some researchers reserve the term pilus for the appendage required for bacterial conjugation. All conjugative pili are primarily composed of pilin – fibrous proteins, which are oligomeric.

Pathogenicity islands (PAIs), as termed in 1990, are a distinct class of genomic islands acquired by microorganisms through horizontal gene transfer. Pathogenicity islands are found in both animal and plant pathogens. Additionally, PAIs are found in both gram-positive and gram-negative bacteria. They are transferred through horizontal gene transfer events such as transfer by a plasmid, phage, or conjugative transposon. Therefore, PAIs enables microorganisms to induce disease and also contribute to microorganisms' ability to evolve.

Bacterial adhesins are cell-surface components or appendages of bacteria that facilitate adhesion or adherence to other cells or to surfaces, usually in the host they are infecting or living in. Adhesins are a type of virulence factor.

<span class="mw-page-title-main">Filamentation</span> Type of bacteria growth

Filamentation is the anomalous growth of certain bacteria, such as Escherichia coli, in which cells continue to elongate but do not divide. The cells that result from elongation without division have multiple chromosomal copies.

<span class="mw-page-title-main">DNA adenine methylase</span> Prokaryotic enzyme

DNA adenine methylase, (Dam) (also site-specific DNA-methyltransferase (adenine-specific), EC 2.1.1.72, modification methylase, restriction-modification system) is an enzyme that adds a methyl group to the adenine of the sequence 5'-GATC-3' in newly synthesized DNA. Immediately after DNA synthesis, the daughter strand remains unmethylated for a short time. It is an orphan methyltransferase that is not part of a restriction-modification system and regulates gene expression. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">RyhB</span> 90 nucleotide RNA

RyhB RNA is a 90 nucleotide RNA that down-regulates a set of iron-storage and iron-using proteins when iron is limiting; it is itself negatively regulated by the ferric uptake repressor protein, Fur.

<span class="mw-page-title-main">Fimbrial usher protein</span>

The fimbrial usher protein is involved in biogenesis of the pilus in Gram-negative bacteria. The biogenesis of some fimbriae requires a two-component assembly and transport system which is composed of a periplasmic chaperone and a pore-forming outer membrane protein which has been termed a molecular 'usher'; this is the chaperone-usher pathway.

<span class="mw-page-title-main">Sortase</span> Group of prokaryotic enzymes

Sortase refers to a group of prokaryotic enzymes that modify surface proteins by recognizing and cleaving a carboxyl-terminal sorting signal. For most substrates of sortase enzymes, the recognition signal consists of the motif LPXTG (Leu-Pro-any-Thr-Gly), then a highly hydrophobic transmembrane sequence, followed by a cluster of basic residues such as arginine. Cleavage occurs between the Thr and Gly, with transient attachment through the Thr residue to the active site Cys residue, followed by transpeptidation that attaches the protein covalently to cell wall components. Sortases occur in almost all Gram-positive bacteria and the occasional Gram-negative bacterium or Archaea, where cell wall LPXTG-mediated decoration has not been reported. Although sortase A, the "housekeeping" sortase, typically acts on many protein targets, other forms of sortase recognize variant forms of the cleavage motif, or catalyze the assembly of pilins into pili.

Bacterial small RNAs are small RNAs produced by bacteria; they are 50- to 500-nucleotide non-coding RNA molecules, highly structured and containing several stem-loops. Numerous sRNAs have been identified using both computational analysis and laboratory-based techniques such as Northern blotting, microarrays and RNA-Seq in a number of bacterial species including Escherichia coli, the model pathogen Salmonella, the nitrogen-fixing alphaproteobacterium Sinorhizobium meliloti, marine cyanobacteria, Francisella tularensis, Streptococcus pyogenes, the pathogen Staphylococcus aureus, and the plant pathogen Xanthomonas oryzae pathovar oryzae. Bacterial sRNAs affect how genes are expressed within bacterial cells via interaction with mRNA or protein, and thus can affect a variety of bacterial functions like metabolism, virulence, environmental stress response, and structure.

Pathogenic <i>Escherichia coli</i> Strains of E. coli that can cause disease

Escherichia coli is a gram-negative, rod-shaped bacterium that is commonly found in the lower intestine of warm-blooded organisms (endotherms). Most E. coli strains are harmless, but pathogenic varieties cause serious food poisoning, septic shock, meningitis, or urinary tract infections in humans. Unlike normal flora E. coli, the pathogenic varieties produce toxins and other virulence factors that enable them to reside in parts of the body normally not inhabited by E. coli, and to damage host cells. These pathogenic traits are encoded by virulence genes carried only by the pathogens.

<span class="mw-page-title-main">Peptidase Do</span>

Peptidase Do is an enzyme. This enzyme catalyses the following chemical reaction

Chaperone-usher fimbriae (CU) are linear, unbranching, outer-membrane pili secreted by gram-negative bacteria through the chaperone-usher system rather than through type IV secretion or extracellular nucleation systems. These fimbriae are built up out of modular pilus subunits, which are transported into the periplasm in a Sec dependent manner. Chaperone-usher secreted fimbriae are important pathogenicity factors facilitating host colonisation, localisation and biofilm formation in clinically important species such as uropathogenic Escherichia coli and Pseudomonas aeruginosa.

Gabriel Waksman FMedSci, FRS, is Courtauld professor of biochemistry and molecular biology at University College London (UCL), and professor of structural and molecular biology at Birkbeck College, University of London. He is the director of the Institute of Structural and Molecular Biology (ISMB) at UCL and Birkbeck, head of the Department of Structural and Molecular Biology at UCL, and head of the Department of Biological Sciences at Birkbeck.

<span class="mw-page-title-main">FtsA</span> Bacterial protein that is related to actin

FtsA is a bacterial protein that is related to actin by overall structural similarity and in its ATP binding pocket.

The fim switch in Escherichia coli is the mechanism by which the fim gene cluster, encoding Type I Pili, is transcriptionally controlled.

<span class="mw-page-title-main">Twitching motility</span> Form of crawling bacterial motility

Twitching motility is a form of crawling bacterial motility used to move over surfaces. Twitching is mediated by the activity of hair-like filaments called type IV pili which extend from the cell's exterior, bind to surrounding solid substrates, and retract, pulling the cell forwards in a manner similar to the action of a grappling hook. The name twitching motility is derived from the characteristic jerky and irregular motions of individual cells when viewed under the microscope. It has been observed in many bacterial species, but is most well studied in Pseudomonas aeruginosa, Neisseria gonorrhoeae and Myxococcus xanthus. Active movement mediated by the twitching system has been shown to be an important component of the pathogenic mechanisms of several species.

P fimbriae are chaperone-usher type fimbrial appendages found on the surface of many Escherichia coli bacteria. The P fimbriae is considered to be one of the most important virulence factor in uropathogenic E. coli and plays an important role in upper urinary tract infections. P fimbriae mediate adherence to host cells, a key event in the pathogenesis of urinary tract infections.

<span class="mw-page-title-main">Jill R. Harper</span> American molecular biologist and policy advisor

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A. C. Matin was a Pakistani-American microbiologist, immunologist, academician and researcher. He was a professor of microbiology and immunology at Stanford University School of Medicine.

References

  1. ↑ "Professor Jan Tennent – Biomedical research leader". ATSE. Retrieved 8 November 2019.
  2. ↑ "Prof Jan Tennent FTSE – AusBiotech Ltd". www.ausbiotech.org. Retrieved 9 November 2019.
  3. ↑ Marklund, Britt-lnger; Tennent, Jan M.; Garcia, Elisa; Hamers, Anja; Baga, Monika; Lindberg, Frederik; Gaastra, Wim; Normark, Staff an (August 1992). "Horizontal gene transfer of the Escherichia coli pap and prs pili operons as a mechanism for the development of tissue-specific adhesive properties". Molecular Microbiology. 6 (16): 2225–2242. doi:10.1111/j.1365-2958.1992.tb01399.x. PMID   1357526. S2CID   34556027.
  4. ↑ Tennent, J. M.; Lindberg, F.; Normark, S. (May 1990). "Integrity of Escherichia coli P pili during biogenesis: properties and role of PapJ". Molecular Microbiology. 4 (5): 747–758. doi:10.1111/j.1365-2958.1990.tb00645.x. PMID   1975085. S2CID   27745334.
  5. ↑ Lindberg, F; Tennent, J M; Hultgren, S J; Lund, B; Normark, S (November 1989). "PapD, a periplasmic transport protein in P-pilus biogenesis". Journal of Bacteriology. 171 (11): 6052–6058. doi:10.1128/jb.171.11.6052-6058.1989. PMC   210471 . PMID   2572580.
  6. ↑ Hultgren, S. J.; Lindberg, F.; Magnusson, G.; Kihlberg, J.; Tennent, J. M.; Normark, S. (1 June 1989). "The PapG adhesin of uropathogenic Escherichia coli contains separate regions for receptor binding and for the incorporation into the pilus". Proceedings of the National Academy of Sciences. 86 (12): 4357–4361. Bibcode:1989PNAS...86.4357H. doi: 10.1073/pnas.86.12.4357 . PMC   287268 . PMID   2567514.
  7. ↑ Norgren., M.; Bága., M.; Tennent, J.M.; Normark, S. (September 1987). "Nucleotide sequence, regulation and functional analysis of the papC gene required for cell surface localization of Pap pili of uropathogenic Escherichia coli". Molecular Microbiology. 1 (2): 169–178. doi:10.1111/j.1365-2958.1987.tb00509.x. PMID   2897064. S2CID   24884461.
  8. ↑ "Jan Tennent – Melbourne Knowledge Week 2019". Jan Tennent – Melbourne Knowledge Week 2019. Retrieved 9 November 2019.
  9. ↑ "ABN Lookup". November 2014.
  10. ↑ "Prof Jan Tennent elected to AusBiotech Board – Biomedical Research Victoria". biomedvic.org.au. Archived from the original on 20 March 2018.
  11. ↑ Search Results for author Tennent J on PubMed .
  12. ↑ "Professor Jan Tennent – Biomedical research leader". Applied. Archived from the original on 24 October 2019. Retrieved 24 October 2019.
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