Pauline Rudd

Last updated
Pauline Rudd

Born
Pauline Mary Rudd
Education Bournemouth School for Girls
Alma mater Westfield College (BSc)
Open University (PhD)
Scientific career
Fields Glycobiology
Institutions University College Dublin
University College Cork
University of Oxford
Scripps Research
Ben-Gurion University of the Negev
Wessex Biochmeicals
Thesis The structure and function of glycoforms  (1995)
Doctoral advisor Peter Taylor [1]
Website apc.ucc.ie/pauline-rudd/ OOjs UI icon edit-ltr-progressive.svg

Pauline Rudd FRSM is a British biochemist and Professor at the Microbiome Institute, University College Cork. [2] She is a founder of Wessex Biochemicals, a Fellow of the Royal Society of Medicine and was awarded the James Gregory Medal in 2010. [3]

Contents

Early life and education

Rudd grew up in Bournemouth and attended Bournemouth School for Girls. As a child she wanted to be a physicist. Her uncle was a physicist, and Rudd joined the British Junior Astronomical Association. She was the only girl in a group of 48 boys, and said she was never allowed to look down the telescope. [4] The male dominated environment of physics made Rudd consider a career in chemistry instead. [4] When she was fourteen, she started to use washing machines and liquidisers to create rare sugars and sugar phosphates. She sold these chemicals through and co-founded Wessex Biochemicals. [4] [5] Rudd was an undergraduate chemistry student at Westfield College, then part of the University of London. [4] After earning her degree, she joined Wessex Biochemicals which employed thirty people before being acquired by Sigma-Aldrich.[ when? ] [4] She compelted her PhD in 1995 which was awarded by the Open University. [1]

Research and career

Rudd joined the glycobiology institute at the University of Oxford in 1985. At the time, it was difficult for women scientists to secure jobs as academic personnel, and Rudd joined as a glass washer. She learned how to work with glycoproteins and large sugars and eventually completed a doctorate on glycoforms at the Open University in 1995. [1] Rudd moved to the Scripps Research institute, and held a visiting position at the Ben-Gurion University of the Negev. She commercialised her work on liquid chromatography–mass spectrometry (LCMS) with Waters Corporation.[ citation needed ]

Rudd has worked to miniaturise technologies for glycol analysis. For example, she has used genome-wide association studies (GWAS) to link individual genomes to their serum glycome and individual proteins. [6] She moved to University College Dublin in 2006, where was made head of the Dublin-Oxford glycobiology laboratory research group. [7] [8] She opened the National Institute for Bioprocessing Research and Training (NIBRT), where she developed new processes for protein glycosylation in an attempt to characterise recombinant protein drugs. [9]

Awards and honours

Selected publications

Personal life

Rudd serves as an associate of the Anglican Church at the Community of St Mary the Virgin in Wantage, Oxfordshire. [14] She took a fifteen-year career break to raise her four children. [4]

Related Research Articles

Defined in the narrowest sense, glycobiology is the study of the structure, biosynthesis, and biology of saccharides that are widely distributed in nature. Sugars or saccharides are essential components of all living things and aspects of the various roles they play in biology are researched in various medical, biochemical and biotechnological fields.

Glycosylation is the reaction in which a carbohydrate, i.e. a glycosyl donor, is attached to a hydroxyl or other functional group of another molecule in order to form a glycoconjugate. In biology, glycosylation usually refers to an enzyme-catalysed reaction, whereas glycation may refer to a non-enzymatic reaction.

Glycoconjugates are the classification family for carbohydrates – referred to as glycans – which are covalently linked with chemical species such as proteins, peptides, lipids, and other compounds. Glycoconjugates are formed in processes termed glycosylation.

<span class="mw-page-title-main">Glycosyltransferase</span> Class of enzymes that catalyze the transfer of glycosyl groups to an acceptor

Glycosyltransferases are enzymes that establish natural glycosidic linkages. They catalyze the transfer of saccharide moieties from an activated nucleotide sugar to a nucleophilic glycosyl acceptor molecule, the nucleophile of which can be oxygen- carbon-, nitrogen-, or sulfur-based.

<span class="mw-page-title-main">Chi-Huey Wong</span> Taiwanese-American biochemist (born 1948)

Chi-Huey Wong is a Taiwanese-American biochemist. He is currently the Scripps Family Chair Professor at the Scripps Research Institute, California in the department of chemistry. He is a member of the United States National Academy of Sciences, as awarded the 2014 Wolf Prize in Chemistry and 2015 RSC Robert Robinson Award. Wong is also the holder of more than 100 patents and publisher of more 700 scholarly academic research papers under his name.

Richard D. Cummings is an American biochemist who is the S. Daniel Abraham Professor of Surgery at Beth Israel Deaconess Medical Center and Harvard Medical School in Boston, Massachusetts. He also the chief of the division of surgical sciences within the department of surgery. He is the director of the Harvard Medical School Center for Glycoscience, director of the National Center for Functional Glycomics, and also founder of the Glycomics Core at BIDMC. As of 2018 Cummings is also the scientific director of the Feihi Nutrition Laboratory at BIDMC. Before moving to BIDMC/HMS, Cummings was the William Patterson Timmie Professor and chair of the department of biochemistry at Emory University School of Medicine in Atlanta, Georgia from 2006 to 2015. At Emory, Cummings was a founder in 2007 of the Emory Glycomics Center.

<span class="mw-page-title-main">Nucleotide sugars metabolism</span>

In nucleotide sugar metabolism a group of biochemicals known as nucleotide sugars act as donors for sugar residues in the glycosylation reactions that produce polysaccharides. They are substrates for glycosyltransferases. The nucleotide sugars are also intermediates in nucleotide sugar interconversions that produce some of the activated sugars needed for glycosylation reactions. Since most glycosylation takes place in the endoplasmic reticulum and golgi apparatus, there are a large family of nucleotide sugar transporters that allow nucleotide sugars to move from the cytoplasm, where they are produced, into the organelles where they are consumed.

Glycoinformatics is a field of bioinformatics that pertains to the study of carbohydrates involved in protein post-translational modification. It broadly includes database, software, and algorithm development for the study of carbohydrate structures, glycoconjugates, enzymatic carbohydrate synthesis and degradation, as well as carbohydrate interactions. Conventional usage of the term does not currently include the treatment of carbohydrates from the better-known nutritive aspect.

Anne Dell is an Australian biochemist specialising in the study of glycomics and the carbohydrate structures that modify proteins. Anne's work could be used to figure out how pathogens such as HIV are able to evade termination by the immune system which could be applied toward understanding how this occurs in fetuses. Her research has also led to the development of higher sensitivity mass spectroscopy techniques which have allowed for the better studying of the structure of carbohydrates. Anne also established GlycoTRIC at Imperial College London, a research center that allows for glycobiology to be better understood in biomedical applications. She is currently Professor of Carbohydrate Biochemistry and Head of the Department of Life Sciences at Imperial College London. Dell's other contributions to the study of Glycobiology are the additions she has made to the textbook "Essentials of Glycobiology" Dell was appointed Commander of the Order of the British Empire (CBE) in the 2009 Birthday Honours.

Glycopeptides are peptides that contain carbohydrate moieties (glycans) covalently attached to the side chains of the amino acid residues that constitute the peptide.

O-linked glycosylation is the attachment of a sugar molecule to the oxygen atom of serine (Ser) or threonine (Thr) residues in a protein. O-glycosylation is a post-translational modification that occurs after the protein has been synthesised. In eukaryotes, it occurs in the endoplasmic reticulum, Golgi apparatus and occasionally in the cytoplasm; in prokaryotes, it occurs in the cytoplasm. Several different sugars can be added to the serine or threonine, and they affect the protein in different ways by changing protein stability and regulating protein activity. O-glycans, which are the sugars added to the serine or threonine, have numerous functions throughout the body, including trafficking of cells in the immune system, allowing recognition of foreign material, controlling cell metabolism and providing cartilage and tendon flexibility. Because of the many functions they have, changes in O-glycosylation are important in many diseases including cancer, diabetes and Alzheimer's. O-glycosylation occurs in all domains of life, including eukaryotes, archaea and a number of pathogenic bacteria including Burkholderia cenocepacia, Neisseria gonorrhoeae and Acinetobacter baumannii.

Phosphoglycosyl transferase C (PglC) is an enzyme belonging to a class known as monotopic phosphoglycosyl transferases (PGT). PGTs are required for the synthesis of glycoconjugates on the membrane surface of bacteria. Glycoconjugates, such as glycoproteins, are imperative for bacterial communication as well as host cell interactions between prokaryotic and eukaryotic cells lending to bacteria's pathogenicity.

Translational glycobiology or applied glycobiology is the branch of glycobiology and glycochemistry that focuses on developing new pharmaceuticals through glycomics and glycoengineering. Although research in this field presents many difficulties, translational glycobiology presents applications with therapeutic glycoconjugates, with treating various bone diseases, and developing therapeutic cancer vaccines and other targeted therapies. Some mechanisms of action include using the glycan for drug targeting, engineering protein glycosylation for better efficacy, and glycans as drugs themselves.

<span class="mw-page-title-main">Charles E. Warren</span> American glycobiologist (1962–2005)

Charles E. Warren was an assistant professor of biochemistry and molecular biology at the University of New Hampshire.

Armando J. Parodi is an Argentine glycobiologist. He did his initial education at the School of Sciences of the University of Buenos Aires. His PhD work was done under Luis Federico Leloir, a recipient of the Nobel Prize in Chemistry for his work involving the finding of sugar nucleotides and how they play a role in the making of oligosaccharides and polysaccharides. He also pursued postdoc work at the Pasteur Institute in Paris, France and Duke University in Durham, NC, USA.

<span class="mw-page-title-main">Elwira Lisowska</span> Polish biochemist and professor

Elwira Lisowska is a Polish biochemist and professor. She made significant contributions to the biochemistry of human blood groups, especially MNS and P1PK blood group systems, and to the immunochemical characterization of glycopeptide antigens.

Tracey Maureen Gloster is a chemist at the University of St Andrews UK. Her research interests are in structural biology, chemical biology, glycobiology and carbohydrate processing enzymes.

Elizabeth Fay Hounsell was a British Professor of Biological Chemistry, Birkbeck, University of London. She specialised in the role of protein glycosylation in cell regulation.

Catherine E. Costello is the William Fairfield Warren distinguished professor in the department of biochemistry, Cell Biology and Genomics, and the director of the Center for Biomedical Mass Spectrometry at the Boston University School of Medicine.

Nicki Packer FRSC is a distinguished professor of glycoproteomics in the School of Natural Sciences at Macquarie University and principal research leader at Griffith University's Institute for Glycomics. Packer is a Fellow of the Royal Society of Chemistry and in 2021 received the Distinguished Achievement in Proteomic Sciences Award from the Human Proteome Organization. Her research focuses on biological functional of glycoconjugates by linking glycomics with proteomics and bioinformatics.

References

  1. 1 2 3 Rudd, Pauline Mary (1995). The structure and function of glycoforms. open.ac.uk (PhD thesis). Open University. doi:10.21954/ou.ro.0000fb9f. OCLC   556507763. EThOS   uk.bl.ethos.295604. Open Access logo PLoS transparent.svg
  2. Pauline Rudd publications from Europe PubMed Central
  3. 1 2 "James Gregory Lectures on Science, Religion and Human Flourishing | Is there more to life than genes?". jamesgregory.org.uk. Retrieved 2022-06-11.
  4. 1 2 3 4 5 6 "The Science of Sugar: Lessons Learned with Pauline Rudd". The Medicine Maker. Retrieved 2022-06-11.
  5. "Professor Pauline M. Rudd". Jenner Symposium. Retrieved 2022-06-11.
  6. 1 2 "Pauline Rudd". The Analytical Scientist. Retrieved 2022-06-11.
  7. 1 2 3 "Fellows". International Society for Science & Religion (ISSR). Retrieved 2022-06-11.
  8. "Celtic strength: Science in Ireland". science.org. Retrieved 2022-06-11.
  9. "Agilent | Agilent Technologies, National Institute for Bioprocessing Research and Training, Advance Emerging Glycomics Research". agilent.com. 2010-06-29. Retrieved 2022-06-11.
  10. "Agilent Thought Leader Program". agilent.com. 2021-09-30. Retrieved 2022-06-11.
  11. Bulletin, Laboratory News from Lab. "Waters Selects Ireland's NIBRT and Prof. Pauline Rudd for Center of Innovation Program Honors". labbulletin.com. Retrieved 2022-06-11.
  12. "Honorary Doctors at Sahlgrenska Academy | University of Gothenburg". gu.se. Retrieved 2022-06-11.
  13. Sonnino, Sandro (2019-08-01). "The international Glycoconjugate organization awards". Glycoconjugate Journal. 36 (4): 237. doi: 10.1007/s10719-019-09877-z . ISSN   1573-4986. PMID   31267249. S2CID   195774182.
  14. Priest, Eric (2016-08-18). Reason and Wonder: Why Science And Faith Need Each Other. SPCK. ISBN   978-0-281-07525-6.