Research Center for Infectious Diseases
2705, boulevard Laurier, RC-709
CANADA G1V 4G2
Tel.: 418-525-4444, extension 48647
Fax: 418-654-2715CourrielSachiko [dot] sato [at] crchul [dot] ulaval [dot] ca (418-654-2715)
Sachiko [dot] Sato [at] crchul [dot] ulaval [dot] ca (Email)
The main research field of Sachiko Sato's glycobiology laboratory is functional glycomics in the context of innate immune response to parasitic and bacterial infectious diseases. Her laboratory has been investigating the biological significance of the interaction between the -galactoside containing glycoconjugates, which are expressed on the cell surface of host phagocytic cells (macrophages and dendritic cells) and protozoa parasite Leishmania, and their host side transducers, galectins (proteins which can recognize the specific -galactoside epitopes on the glycoconjugates). The last decade research on cell communication in the context of immune response reveals that the communication often hinges on specific epitopes on glycoconjugates. While it has been known that the glycan codes are deciphered by various host lectins, leading to the transduction into subsequent immune responses, fledgling is understanding the molecular mechanisms on such decoding processes . Especially, in the case of leishmaniasis, a tropical parasitic affliction, which is listed by the World Health Organization as one of the six most important parasitic diseases worldwide, Leishmania surface glycoconjugates (lipophosphoglycans) are clearly implicated in their life cycle, the interaction between macrophages/dendrictic cells and Leishmania and host immune responses to Leishmania. However, the identities of lectins which can decipher such glycan codes have been elusive. Her laboratory has recently suggested that galectin-3, a major macrophage lectin and galectin-9 can recognize the Leishmania specific glycan epitopes, and has proposed that galectin-3 and 9 could be ones of the host lectins responsible to decipher the glycan codes, leading to Leishmania species specific host immune responses mediated by macrophages and dendritic cells. Currently, they are now investigating this hypothesis.
Isabel S, Boissinot M, Charlebois I, Fauvel CM, Shi LE, Lévesque JC, Paquin AT, Bastien M, Stewart G, Leblanc E, Sato S, Bergeron MG.
Rapid filtration separation-based sample preparation method for bacillus spores in powdery and environmental matrices. Appl Environ Microbiol. 2012 Mar;78(5):1505-12. Epub 2011 Dec 30.
St-Pierre C, Ouellet M, Giguère D, Ohtake R, Roy R, Sato S, Tremblay MJ.
Galectin-1-specific inhibitors as a new class of compounds to treat HIV-1 infection. Antimicrob Agents Chemother. 2012 Jan;56(1):154-62. Epub 2011 Nov 7.
St-Pierre C, Manya H, Ouellet M, Clark GF, Endo T, Tremblay MJ, Sato S.
Host-soluble galectin-1 promotes HIV-1 replication through a direct interaction with glycans of viral gp120 and host CD4. J Virol. 2011 Nov;85(22):11742-51. Epub 2011 Aug 31.
St-Pierre C, Ouellet M, Tremblay MJ, Sato S.
Galectin-1 and HIV-1 Infection. Methods Enzymol. 2010;480:267-94. Review.
Sato S, St-Pierre C, Bhaumik P, Nieminen J.
Galectins in innate immunity: dual functions of host soluble beta-galactoside-binding lectins as damage-associated molecular patterns (DAMPs) and as receptors for pathogen-associated molecular patterns (PAMPs). Immunol Rev. 2009 Jul;230(1):172-87. Review.
Sato S, Nakayama Y, Matsuhashi T, Seiji K, Matsunaga K, Takasawa C, Ishibashi T, Zhou YM, Ishibashi-Ueda H, Okamoto Y, Asano H, Takahashi S.
Evaluation of self-expandable, FK506-coated, covered stents in canine animal model. J Biomed Mater Res B Appl Biomater. 2009 Aug;90(2):647-52.
Gauthier S, Pelletier I, Ouellet M, Vargas A, Tremblay MJ, Sato S, Barbeau B.
Induction of galectin-1 expression by HTLV-I Tax and its impact on HTLV-I infectivity. Retrovirology. 2008 Nov 25;5:105.