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 FTSE (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">Pilus</span> A proteinaceous hair-like appendage on the surface of bacteria

A pilus is a hair-like appendage found on the surface of 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 contribute to microorganisms' ability to evolve.

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">DNA adenine methylase</span> Prokaryotic enzyme

DNA adenine methylase, (Dam methylase) (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">SgrS RNA</span>

SgrS is a 227 nucleotide small RNA that is activated by SgrR in Escherichia coli during glucose-phosphate stress. The nature of glucose-phosphate stress is not fully understood, but is correlated with intracellular accumulation of glucose-6-phosphate. SgrS helps cells recover from glucose-phosphate stress by base pairing with ptsG mRNA and causing its degradation in an RNase E dependent manner. Base pairing between SgrS and ptsG mRNA also requires Hfq, an RNA chaperone frequently required by small RNAs that affect their targets through base pairing. The inability of cells expressing sgrS to create new glucose transporters leads to less glucose uptake and reduced levels of glucose-6-phosphate. SgrS is an unusual small RNA in that it also encodes a 43 amino acid functional polypeptide, SgrT, which helps cells recover from glucose-phosphate stress by preventing glucose uptake. The activity of SgrT does not affect the levels of ptsG mRNA of PtsG protein. It has been proposed that SgrT exerts its effects through regulation of the glucose transporter, PtsG.

<span class="mw-page-title-main">Swarming motility</span>

Swarming motility is a rapid and coordinated translocation of a bacterial population across solid or semi-solid surfaces, and is an example of bacterial multicellularity and swarm behaviour. Swarming motility was first reported by Jorgen Henrichsen and has been mostly studied in genus Serratia, Salmonella, Aeromonas, Bacillus, Yersinia, Pseudomonas, Proteus, Vibrio and Escherichia.

<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 (bsRNA) 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.

In molecular biology, the FasX small RNA (fibronectin/fibrinogen-binding/haemolytic-activity/streptokinase-regulator-X) is a non-coding small RNA (sRNA) produced by all group A Streptococcus. FasX has also been found in species of group D and group G Streptococcus. FasX regulates expression of secreted virulence factor streptokinase (SKA), encoded by the ska gene. FasX base pairs to the 5' end of the ska mRNA, increasing the stability of the mRNA, resulting in elevated levels of streptokinase expression. FasX negatively regulates the expression of pili and fibronectin-binding proteins on the bacterial cell surface. It binds to the 5' untranslated region of genes in the FCT-region in a serotype-specific manner, reducing the stability of and inhibiting translation of the pilus biosynthesis operon mRNA by occluding the ribosome-binding site through a simple Watson-Crick base-pairing mechanism.

<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.

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

The locus of enterocyte effacement-encoded regulator (Ler) is a regulatory protein that controls bacterial pathogenicity of enteropathogenic Escherichia coli (EPEC) and enterohemorrhagic Escherichia coli (EHEC). More specifically, Ler regulates the locus of enterocyte effacement (LEE) pathogenicity island genes, which are responsible for creating intestinal attachment and effacing lesions and subsequent diarrhea: LEE1, LEE2, and LEE3. LEE1, 2, and 3 carry the information necessary for a type III secretion system. The transcript encoding the Ler protein is the open reading frame 1 on the LEE1 operon.

<span class="mw-page-title-main">Curli</span> A proteinaceous extracellular fiber produced by enteric bacteria

The Curli protein is a type of amyloid fiber produced by certain strains of enterobacteria. They are extracellular fibers located on bacteria such as E. coli and Salmonella spp. These fibers serve to promote cell community behavior through biofilm formation in the extracellular matrix. Amyloids are associated with several human neurodegenerative diseases such as Alzheimer's disease, Huntington's disease, Parkinson's disease, and prion diseases. The study of curli may help to understand human diseases thought to arise from improper amyloid fiber formation. The curli pili are generally assembled through the extracellular nucleation/precipitation pathway.

P fimbriae or P pili or Pap 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.

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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. Retrieved 24 October 2019.
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