For more information, visit:

• Laboratory Medicine & Pathobiology, University of Toronto
• School of Graduate Studies, University of Toronto
• Institute of Medical Sciences, University of Toronto

Click here to see Palaniyar lab members and their projects

Brief Biography

Doctoral training

• PhD in Molecular Biology and Genetics, University of Guelph, Canada. He studied viral nucleic acid binding proteins and DNA recombination in Dr. David Evans’ laboratory (1991-1996).

Postdoctoral training

• Structure of the innate immune collectin surfactant protein A (SP-A) and lipids by electron microscopy (Dr. George Harauz’s laboratory at the University of Guelph, Canada 1996-1998)
• SP-A and SP-D structure-function transgenic mouse work studies (Dr. Frank McCormack’s laboratory, University of Cincinnati, USA, 1998-2000)
• SP-D:DNA, SP-D:antibody: decorin molecular interaction studies (Dr. Kenneth Reid’s laboratory, MRC Immunochemistry Unit, Department of Biochemistry, the University of Oxford, UK 2000-2004)

SickKids lung innate immunity research laboratory

• He returned to Canada in 2004 and established a laboratory to continue his research work on innate immunity that affects several lung diseases.

Research Interests

• Diseases of interest: infectious diseases, rare lung diseases, cystic fibrosis, allergy/asthma
• Lung innate immunity – collectins - SP-A & SP-D
• Influenza virus infection – H1N1 Swine Flu
• Link between innate and adaptive immunity – SP-D & antibodies
• DNA, neutrophil extracellular trap (NETs) and apoptotic cell clearance
• Lung inflammation and hyperresponsiveness

Dr. Palaniyar currently accepts graduate students and trainees.
For more information contact: nades.palaniyar@sickkids.ca

Research Activities

Palaniyar's lab aims i) to understand novel innate immune functions of SP-A and SP-D, and (ii) to determine the therapeutic potential of these proteins to treat infectious and inflammatory lung diseases. 

Interestingly, while adults rely on both innate and antibody-based adaptive immune systems, neonates and children depend primarily on innate immune system for their protection against invading microbial pathogens. To better understand the innate immune system in the lungs, we study SP-A and SP-D.  We consider these collections as the antibodies of the innate immune system.

SP-A and SP-D are innate immune collectins (collagenous lectins) that are secreted onto the inner airway surfaces. These proteins constitute about 90 per cent (w/w) of the proteins associated with lung surfactant lipid that covers the inner surface of the airways. These antibody-like innate immune pattern-recognition proteins recognize the carbohydrate arrays present on the inhaled microbes and particles. They form immune complexes to enhance the killing and clearance of foreign invaders from the lungs. SP-D specifically enhances the clearance of infectious agents, DNA and dying immune cells by macrophages. Our current studies suggest that SP-D may also enhance NET-mediated clearance of various infectious agents. SP-A and SP-D are destroyed by some pathogens and dysregulated during infection or in many lung diseases. We conduct research work to determine the molecular mechanisms regulated by these proteins.

Specific projects:

• SP-A and SP-D in H1N1 Swine flu infection
• SP-A and  IgM in apoptosis and apoptotic cell clearance
• SP-D and NET-mediated microbial clearance
• SP-D and alpha-2 macroglobulin in microbial infection and apoptotic cell clearance
• SP-A and SP-D in stem cell transplant patients
• SP-A and SP-D in allergy/asthma, chronic obstructive pulmonary disease (COPD), alveolar proteinosis, cystic fibrosis (CF)

Common techniques used in our lab: 

• Routine biochemical, molecular and cell biology assays
• Gene cloning and protein expression (yeast, E. coli, mamalian cells)
• Protein purification (affinity, ion exchange, size-exclusion; AKTA FPLC)
• Surface plasmon resonance or SPR (ProteON)
• Light, fluorescence, confocal and electron microscopy
• Live cell imaging, thick tissue 3D-imaging
• Tissue culture (epithelial, T-cells, macrophages, neutrophils; cell lines and primary cells)
• Ex vivo and in vivo experiments in mouse models experiments (SP-A and SP-D knockouts)
• Human amniotic fluid, blood and lung washing sample studies

Long-term Research Interests

Determining the therapeutic potential of collectins to minimize airway infection and inflammation.

Conferences

• i-CLIIP conference
• TASME conference in July 2010
• TASME conference 2008

Achievements

• American Lung Association (Ohio USA) postdoctoral fellowship (1999-2000)
• Wellcome Trust, UK/CIHR postdoctoral fellowships (2000-2004)

Publications

Palaniyar N. (2010) Antibody equivalent molecules of the innate immune system: Parallels between innate and adaptive immune proteins (Editorial). Innate Immunity (June issue; 16(3) In press)

Craig-Barnes, H.A., Doumouras, B.S., Palaniyar, N. (2010) Surfactant protein D interacts with alpha-2-macroglobulin and increases its innate immune potential. J Biol Chem.  (Mar 5. Epub ahead of print)

Thomsen T, Moeller, J.B., Schlosser, A., Sorensen, G.L., Moestrup, S.K., Palaniyar, N., Wallis, R., Mollenhauer, J., Holmskov, U. (2010) The recognition unit of FIBCD1 organizes into a non-covalently linked tetrameric structure and uses the hydrophobic funnel (S1) for acetyl-group recognition. J Biol Chem. 285(2):1229-38.

Douda, D. N., Farmakovski, N., Dell, S., Grasemann, H., Palaniyar, N. (2009) SP-D and GM-CSF increase the innate immune potential of macrophages and granuloma formation in LPI patients. Submitted to Orphanet J Rare Dis. 4:29.

Gaiha, G.D, Dong, T., Palaniyar, N., Mitchell, D.A., Reid, K.B.M., Clark, H. W (2008) Surfactant protein A binds to HIV and inhibits direct infection of CD4+ cells, but enhances DC-mediated viral transfer. J. Immunol. 181, 601-609.

Nadesalingam J, Dodds AW, Reid KB, Palaniyar N. (2005) Mannose-binding lectin recognizes peptidoglycan via the N-acetyl glucosamine moiety, and inhibits ligand-induced proinflammatory effect and promotes chemokine production by macrophages. J Immunol. 175(3):1785-94.

Nadesalingam, J., Reid, K.B.M., and Palaniyar, N. (2005) Collectin surfactant protein D binds antibodies and interlinks innate and adaptive immune systems. FEBS Lett. 579, 4449-53.

Nadesalingam, J., Dodds, A.W., Reid, K.B.M., and Palaniyar, N. (2005) Mannose-binding lectin recognizes peptidoglycan via the N-acetyl glucosamine moiety, and inhibits the ligand-induced pro-inflammatory effect and promotes chemokine production by macrophages. J. Immunol. 175, 1785-94.

Palaniyar, N., Clark, H., Nadesalingam, J., Shih, M.J., Hawgood, S., Reid, K.B.M. (2005) Innate immune collectin surfactant proteins D enhances the clearance of DNA by macrophages and minimize anti-DNA antibody generation. J. Immunol. 174, 7352-8.

Palaniyar, N., Nadesalingam, J., Clark, H., Shih, M.J., and Reid, K.B.M. (2004) Nucleic acid is a novel ligand for innate immune pattern recognition collectins surfactant proteins A and D and mannose binding lectin. J. Biol. Chem. 279, 32728-36.

Nadesalingam J, Bernal AL, Dodds AW, Willis AC, Mahoney DJ, Day AJ, Reid KB, Palaniyar N. (2003) Identification and characterization of a novel interaction between pulmonary surfactant protein D and decorin. J Biol Chem. 278(28):25678-87

Clark H, Palaniyar N, Strong P, Edmondson J, Hawgood S, Reid KB. (2002) Surfactant protein D reduces alveolar macrophage apoptosis in vivo. J Immunol. 169(6):2892-9.

Palaniyar N, Zhang L, Kuzmenko A, Ikegami M, Wan S, Wu H, Korfhagen TR, Whitsett JA, McCormack FX. (2002) The role of pulmonary collectin N-terminal domains in surfactant structure, function, and homeostasis in vivo. J Biol Chem. 26;277(30):26971-9.

Shibata Y, Zsengeller Z, Otake K, Palaniyar N, Trapnell BC. (2001) Alveolar macrophage deficiency in osteopetrotic mice deficient in macrophage colony-stimulating factor is spontaneously corrected with age and associated with matrix metalloproteinase expression and emphysema. Blood. 98(9):2845-52.

Ikegami M, Elhalwagi BM, Palaniyar N, Dienger K, Korfhagen T, Whitsett JA, McCormack FX. (2001) The collagen-like region of surfactant protein A (SP-A) is required for correction of surfactant structural and functional defects in the SP-A null mouse. J Biol Chem. 276(42):38542-8.

Pubmed Palaniyar-N to see additional publications

Intellectual Property

Recombinant surfactant protein D compositions and methods of use thereof (WO/03/035679 A2)