Clare Bryant

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Clare Bryant
Alma mater Royal Veterinary College
University of London
Scientific career
Institutions University of Cambridge
Thesis A study of the cardiovascular pharmacology of medetomidine  (1993)

Clare Bryant FLSW is a British veterinary scientist and clinical pharmacologist who is a professor at the University of Cambridge. She specialises in innate immunity. Bryant is a Fellow of Queens' College, Cambridge and of the British Pharmacological Society.

Contents

Early life and education

Bryant was an undergraduate in biochemistry and physiology at the University of Southampton. [1] [2] She trained in veterinary medicine in London. [3] She was supported by the Wellcome Trust to complete a doctorate. [4] Her research first concentrated on anaesthesia, but soon shifted focus to concentrate on receptor pharmacology. [2] She spent four years as a Wellcome Trust postdoctoral fellow with John Vane at the William Harvey Research Institute. [1] She started her independent career at the University of Cambridge.

Research and career

Bryant studies how hosts recognise bacteria using pattern recognition receptors (PRR). [5] [6] She is interested in how these PRR are related to chronic inflammatory diseases, for example Alzheimer's disease. There are several different types of PRR, including Toll-like receptors and NOD-like receptors. She is particularly interested in the PRRs that detect Salmonella enterica . Bryant has studied how ligands on the outer-membranes of bacteria (for example, lipopolysaccharides like endotoxin) interact with PRR to recruit signalling molecules. [7]

Bryant's research demonstrated the power of Fluorescence Resonance Energy Transfer (FRET) and single-molecule fluorescence microscopy to understand the function of toll-like receptors [8] and super resolution microscopy to determine the function of NOD-like receptors [9] to work out how these PRRs form signalling. [10] When allergens are contaminated by endotoxins they can be detected by toll-like receptors. By preventing this detection, Bryant believes it may be possible to design inhibitors that suppress the onset of allergenic responses. As the proteins produced in neuroinflammatory diseases such as Alzheimer's and Parkinson's are recognised by toll-like receptors and induce inflammation, these studies may identify novel treatments for neurodegenerative conditions. [7] [11]

In 2023, Bryant was elected a Fellow of the Learned Society of Wales. [12]

Selected publications

Related Research Articles

<span class="mw-page-title-main">Kupffer cell</span>

Kupffer cells, also known as stellate macrophages and Kupffer–Browicz cells, are specialized cells localized in the liver within the lumen of the liver sinusoids and are adhesive to their endothelial cells which make up the blood vessel walls. Kupffer cells comprise the largest population of tissue-resident macrophages in the body. Gut bacteria, bacterial endotoxins, and microbial debris transported to the liver from the gastrointestinal tract via the portal vein will first come in contact with Kupffer cells, the first immune cells in the liver. It is because of this that any change to Kupffer cell functions can be connected to various liver diseases such as alcoholic liver disease, viral hepatitis, intrahepatic cholestasis, steatohepatitis, activation or rejection of the liver during liver transplantation and liver fibrosis. They form part of the mononuclear phagocyte system.

Pathogen-associated molecular patterns (PAMPs) are small molecular motifs conserved within a class of microbes, but not present in the host. They are recognized by toll-like receptors (TLRs) and other pattern recognition receptors (PRRs) in both plants and animals. This allows the innate immune system to recognize pathogens and thus, protect the host from infection.

Pattern recognition receptors (PRRs) play a crucial role in the proper function of the innate immune system. PRRs are germline-encoded host sensors, which detect molecules typical for the pathogens. They are proteins expressed, mainly, by cells of the innate immune system, such as dendritic cells, macrophages, monocytes, neutrophils and epithelial cells, to identify two classes of molecules: pathogen-associated molecular patterns (PAMPs), which are associated with microbial pathogens, and damage-associated molecular patterns (DAMPs), which are associated with components of host's cells that are released during cell damage or death. They are also called primitive pattern recognition receptors because they evolved before other parts of the immune system, particularly before adaptive immunity. PRRs also mediate the initiation of antigen-specific adaptive immune response and release of inflammatory cytokines.

<span class="mw-page-title-main">Neuroimmune system</span>

The neuroimmune system is a system of structures and processes involving the biochemical and electrophysiological interactions between the nervous system and immune system which protect neurons from pathogens. It serves to protect neurons against disease by maintaining selectively permeable barriers, mediating neuroinflammation and wound healing in damaged neurons, and mobilizing host defenses against pathogens.

<span class="mw-page-title-main">Interleukin 1 beta</span> Mammalian protein found in Homo sapiens

Interleukin-1 beta (IL-1β) also known as leukocytic pyrogen, leukocytic endogenous mediator, mononuclear cell factor, lymphocyte activating factor and other names, is a cytokine protein that in humans is encoded by the IL1B gene. There are two genes for interleukin-1 (IL-1): IL-1 alpha and IL-1 beta. IL-1β precursor is cleaved by cytosolic caspase 1 to form mature IL-1β.

<span class="mw-page-title-main">NLRP3</span> Human protein and coding gene

NLR family pyrin domain containing 3 (NLRP3), is a protein that in humans is encoded by the NLRP3 gene located on the long arm of chromosome 1.

<span class="mw-page-title-main">Toll-like receptor 2</span> One of the toll-like receptors and plays a role in the immune system

Toll-like receptor 2 also known as TLR2 is a protein that in humans is encoded by the TLR2 gene. TLR2 has also been designated as CD282. TLR2 is one of the toll-like receptors and plays a role in the immune system. TLR2 is a membrane protein, a receptor, which is expressed on the surface of certain cells and recognizes foreign substances and passes on appropriate signals to the cells of the immune system.

Pyroptosis is a highly inflammatory form of lytic programmed cell death that occurs most frequently upon infection with intracellular pathogens and is likely to form part of the antimicrobial response. This process promotes the rapid clearance of various bacterial, viral, fungal and protozoan infections by removing intracellular replication niches and enhancing the host's defensive responses. Pyroptosis can take place in immune cells and is also reported to occur in keratinocytes and some epithelial cells.

<span class="mw-page-title-main">NLRC4</span> Protein-coding gene in the species Homo sapiens

NLR family CARD domain-containing protein 4 is a protein that in humans is encoded by the NLRC4 gene.

<span class="mw-page-title-main">NOD-like receptor</span> Class of proteins

The nucleotide-binding oligomerization domain-like receptors, or NOD-like receptors (NLRs), are intracellular sensors of pathogen-associated molecular patterns (PAMPs) that enter the cell via phagocytosis or pores, and damage-associated molecular patterns (DAMPs) that are associated with cell stress. They are types of pattern recognition receptors (PRRs), and play key roles in the regulation of innate immune response. NLRs can cooperate with toll-like receptors (TLRs) and regulate inflammatory and apoptotic response.

<span class="mw-page-title-main">Inflammasome</span> Cytosolic multiprotein complex that mediates the activation of Caspase 1

Inflammasomes are cytosolic multiprotein oligomers of the innate immune system responsible for the activation of inflammatory responses. Activation and assembly of the inflammasome promotes proteolytic cleavage, maturation and secretion of pro-inflammatory cytokines interleukin 1β (IL-1β) and interleukin 18 (IL-18), as well as cleavage of gasdermin D. The N-terminal fragment resulting from this cleavage induces a pro-inflammatory form of programmed cell death distinct from apoptosis, referred to as pyroptosis, and is responsible for secretion of the mature cytokines, presumably through the formation of pores in the plasma membrane. Additionally, inflammasomes can be incorporated into larger cell death-inducing complexes called PANoptosomes, which drive another distinct form of pro-inflammatory cell death called PANoptosis.

<span class="mw-page-title-main">Pyrin domain</span>

A pyrin domain is a protein domain and a subclass of protein motif known as the death fold, the 4th and most recently discovered member of the death domain superfamily (DDF). It was originally discovered in the pyrin protein, or marenostrin, encoded by MEFV. The mutation of the MEFV gene is the cause of the disease known as Familial Mediterranean Fever. The domain is encoded in 23 human proteins and at least 31 mouse genes.

<span class="mw-page-title-main">NLRP11</span> Protein-coding gene in the species Homo sapiens

NOD-like receptor family pyrin domain containing 11 is a protein that in humans is encoded by the NLRP11 gene located on the long arm of human chromosome 19q13.42. NLRP11 belongs to the NALP subfamily, part of a large subfamily of caterpiller. It is also known as NALP11, PYPAF6, NOD17, PAN10, and CLR19.6

NLRP (Nucleotide-binding oligomerization domain, Leucine rich Repeat and Pyrin domain containing), also abbreviated as NALP, is a type of NOD-like receptor. NOD-like receptors are a type of pattern recognition receptor that are found in the cytosol of the cell, recognizing signals of antigens in the cell. NLRP proteins are part of the innate immune system and detect conserved pathogen characteristics, or pathogen-associated molecular patterns, such as such as peptidoglycan, which is found on some bacterial cells. It is thought that NLRP proteins sense danger signals linked to microbial products, initiating the processes associated with the activation of the inflammasome, including K+ efflux and caspase 1 activation. NLRPs are also known to be associated with a number of diseases. Research suggests NLRP proteins may be involved in combating retroviruses in gametes. As of now, there are at least 14 different known NLRP genes in humans, which are named NLRP1 through NLRP14. The genes translate into proteins with differing lengths of leucine-rich repeat domains.

<span class="mw-page-title-main">Luke O'Neill (scientist)</span> Irish biochemist (born 1964)

Luke Anthony John O'Neill is an Irish biochemist. He has been a professor of biochemistry in the School of Biochemistry and Immunology at Trinity College Dublin since 2009.

Hao Wu is a Chinese American biochemist and crystallographer and the Asa and Patricia Springer Professor of Structural Biology in the Department of Biological Chemistry and Molecular Pharmacology at Harvard Medical School. Her work focuses on molecular mechanisms of signal transduction in cell death and inflammation. She is the discoverer of signalosomes, which are large macromolecular complexes involved in cell death and in innate and adaptive immune pathways. She has established a new paradigm for signal transduction that involves higher-order protein assemblies. She has received the Pew Scholar Award, the Rita Allen Scholar Award, the Margaret Dayhoff Memorial Award, the NYC Mayor's Award for Excellence in Science and Technology, NIH MERIT and Pioneer Awards, and the Purdue University Distinguished Science Alumni Award. She was elected AAAS fellow in 2013 and to the National Academy of Sciences in 2015.

<span class="mw-page-title-main">Vishva Dixit</span> Kenyan molecular biologist

Vishva Mitra Dixit is a physician of Indian origin who is the current Vice President of Discovery Research at Genentech.

<span class="mw-page-title-main">Dapansutrile</span> Chemical compound

Dapansutrile (OLT1177) is an inhibitor of the NLRP3 inflammasome.

Elizabeth Sally Ward is a British physician who is Director of Translational Immunology at the Centre for Cancer Immunology in the University of Southampton. She was elected Fellow of the Royal Society in 2022.

Jonathan C. Kagan is an American immunologist and the Marian R. Neutra, Ph.D. Professor of Pediatrics at Harvard Medical School. He is also the director of Basic Research and Shwachman Chair in Gastroenterology at Boston Children's Hospital. Kagan is a world leader in defining the molecular basis of innate immunity and inflammation.

References

  1. 1 2 Bryant, Professor Clare (10 May 2011). "Professor Clare Bryant". www.infectiousdisease.cam.ac.uk. Retrieved 20 December 2021.
  2. 1 2 Leonard, Lorraine (10 May 2016). "Professor Clare Bryant". www.vet.cam.ac.uk. Retrieved 20 December 2021.
  3. ↑ "Professor Clare Bryant | Queens' College". www.queens.cam.ac.uk. Retrieved 20 December 2021.
  4. ↑ "Polypharmakos Ltd". www.polypharmakos.com. Retrieved 10 January 2022.
  5. ↑ Bryant, BBSRC Research Development Fellow C. E. (7 December 2016). "Professor Clare Bryant". www.globalfood.cam.ac.uk. Retrieved 20 December 2021.
  6. ↑ "Polypharmakos Ltd". www.polypharmakos.com. Retrieved 20 December 2021.
  7. 1 2 Bryant, Professor Clare (21 October 2012). "Professor Clare Bryant". www.immunology.cam.ac.uk. Retrieved 20 December 2021.
  8. ↑ Latty, Sarah Louise; Sakai, Jiro; Hopkins, Lee; Verstak, Brett; Paramo, Teresa; Berglund, Nils A; Cammarota, Eugenia; Cicuta, Pietro; Gay, Nicholas J; Bond, Peter J; Klenerman, David (24 January 2018). "Activation of Toll-like receptors nucleates assembly of the MyDDosome signaling hub". eLife. 7: e31377. doi: 10.7554/eLife.31377 . ISSN   2050-084X. PMC   5825206 . PMID   29368691.
  9. ↑ Man, S. M.; Hopkins, L. J.; Nugent, E.; Cox, S.; Gluck, I. M.; Tourlomousis, P.; Wright, J. A.; Cicuta, P.; Monie, T. P.; Bryant, C. E. (6 May 2014). "Inflammasome activation causes dual recruitment of NLRC4 and NLRP3 to the same macromolecular complex". Proceedings of the National Academy of Sciences. 111 (20): 7403–7408. Bibcode:2014PNAS..111.7403M. doi: 10.1073/pnas.1402911111 . ISSN   0027-8424. PMC   4034195 . PMID   24803432.
  10. ↑ Herre, Jurgen; Grönlund, Hans; Brooks, Heather; Hopkins, Lee; Waggoner, Lisa; Murton, Ben; Gangloff, Monique; Opaleye, Olaniyi; Chilvers, Edwin R.; Fitzgerald, Kate; Gay, Nick (15 August 2013). "Allergens as immunomodulatory proteins: the cat dander protein Fel d 1 enhances TLR activation by lipid ligands". Journal of Immunology. 191 (4): 1529–1535. doi:10.4049/jimmunol.1300284. ISSN   1550-6606. PMC   3836235 . PMID   23878318.
  11. ↑ "Scientist Focus: Prof Clare Bryant". Alzheimer's Research UK. Retrieved 20 December 2021.
  12. ↑ Wales, The Learned Society of. "Clare Bryant". The Learned Society of Wales. Retrieved 29 August 2023.
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