John Raynes PhD
- 481
- LSHTM
- Keppel Street
- London
- WC1E 7HT
- T: (44) 020 7927 2355
- F: (44) 020 7323 5687
John Raynes obtained his first degree in Biochemistry from Bristol University and a PhD studying enzyme synthesis in barley at Birmingham University. Attracted by work in area of medical biochemistry and immunology of inflammation Dr Raynes worked first at the University of Leeds on inflammatory markers in cancer and then Manchester on connective tissue before starting at LSHTM in 1986.
Affiliation
Teaching
Immunology of Infectious Disease Course Organiser. Organiser of the core 'Immunology of Infectious Disease' unit which can be taken as a separate short course.
Research
Research interests are mainly within the area of inflammation and innate immune responses. Major topics include; the role of opsonins such as C-reactive protein, serum amyloid A protein and other acute phase proteins in host protection; the receptors on macrophages and neutrophils that such proteins interact with; the macrophage response to microbial structures; protein; protein interactions and novel mechanisms to inhibit proinflammatory cytokines; The innate immune response to Streptococcus pneumoniaeResearch areas
- Immunopathology
- Infectious disease
- Innate immunity
Disciplines
- Biochemistry
- Cell biology
- Immunology
Other interests
- Acute Phase Protein
- Inflammation
- Macrophage
- Neutrophil
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Selected publications
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The Proinflammatory Activity of Recombinant Serum Amyloid A Is Not Shared by the Endogenous Protein in the Circulation
Bjorkman, L.; Raynes, J.G.; Shah, C.; Karlsson, A.; Dahlgren, C.; Bylund, J.
Arthritis and Rheumatism, 2010; 62(6):1660-1665
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The lipidation status of acute-phase protein serum amyloid A determines cholesterol mobilization via scavenger receptor class B, type I
Marsche, G.; Frank, S.; Raynes, J.G.; Kozarsky, K.F.; Sattler, W.; Malle, E.
Biochemical Journal, 2007; 402:117-124
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CD11b Regulates Recruitment of Alveolar Macrophages but Not Pulmonary Dendritic Cells after Pneumococcal Challenge.
Kirby, A.C.; Raynes, J.G.; Kaye, P.M.;
J Infect Dis, 2006; 193(2):205-13
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Serum amyloid A is an innate immune opsonin for Gram-negative bacteria.
Shah, C.; Hari-Dass, R.; Raynes, J.G.;
Blood, 2006; 108(5):1751-7
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Serum amyloid A protein binds to outer membrane protein A of gram-negative bacteria.
Hari-Dass, R.; Shah, C.; Meyer, D.J.; Raynes, J.G.;
J Biol Chem, 2005; 280(19):18562-7
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The Role Played by Tumor Necrosis Factor during Localized and Systemic Infection with Streptococcus pneumoniae.
Kirby, A.C.; Raynes, J.G.; Kaye, P.M.;
J Infect Dis, 2005; 191(9):1538-1547
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Proteolysis of serum amyloid A and AA amyloid proteins by cysteine proteases: cathepsin B generates AA amyloid proteins and cathepsin L may prevent their formation
Rocken, C.; Menard, R.; Buhling, F.; Vockler, S.; Raynes, J.; Stix, B.; Kruger, S.; Roessner, A.; Kahne, T.
Annals of the Rheumatic Diseases, 2005; 64(6):808-815
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Fc{gamma}RIIa expression with Fc{gamma}RI results in C-reactive protein- and IgG-mediated phagocytosis
Bodman-Smith, K. B.; Gregory, R. E.; Harrison, P. T.; Raynes, J. G.
Journal of Leukocyte Biology, 2004; 75(6):1029-35
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