Murine interferon-gamma inducible protein-10 (IP-10) secreted by Lactococcus lactis chemo-attracts human CD3+lymphocytes
BIOTECHNOLOGY LETTERS
Authors: Villatoro-Hernandez, Julio; Yolanda Arce-Mendoza, Alma; Rosas-Taraco, Adrian G.; Cecilia Esparza-Gonzalez, Sandra; Guzman-Lopez, Santos; Elizondo-Omana, Rodrigo E.; Chavez-Reyes, Arturo; Saucedo-Cardenas, Odila; Montes de Oca Luna, Roberto
Abstract
Chemokines are members of the super family of cytokines necessary for leukocyte recruitment in tissues and lymphoid organs. The interferon-gamma inducible protein-10 (IP-10) chemo-attracts CXCR3-expressing cells, such as activated T lymphocytes and monocytes. We have genetically engineered a strain of Lactococcus lactis to secrete a biologically active murine IP-10 that interacts with human CXCR3, its homolog receptor, and chemo-attracts human CD3+ T lymphocytes.
Heterologous gene expression of bovine plasmin in Lactococcus lactis
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Authors: Arnau, J; HjerlHansen, E; Israelsen, H
Abstract
Heterologous production of bovine plasmin was studied in the industrially relevant bacterium Lactococcus lactis. Two sets of lactococcal gene expression signals were coupled to the region of the plasmin gene coding for the serine protease domain. When the promoter region of the prtP gene was used, plasmin was detected mainly intracellularly in strain BPL25 by Western blot hybridization. The intracellular presence of plasmin led to physiological stress. Expression of the plasmin gene driven by the promoter and complete signal sequence of the lactococcal usp45 gene resulted in efficient plasmin secretion in strain BPL420. Cell lysis was observed in strains producing plasmin fragments including the catalytic domain, but not in control strains, which only produced a non-catalytic region of plasmin. The plasmin produced was shown to be biologically active.