title: Comparison of cytokine-inducing activity in a lipoteichoic acid-related molecule isolated from a penicillin-killed group A Streptococcus and from untreated bacteria.
abstract: We previously generated a monoclonal antibody, TS-2, that neutralizes the interferon (IFN)-gamma-inducing activity of OK-432, a penicillin-killed streptococcal preparation [J. Immunother. 13 (1993) 232]. Expression of the TS-2-binding antigen was markedly higher in the cell wall of the penicillin-treated Streptococcus pyogenes (OK-432) than in the untreated bacteria (Su-BBM). We here isolated the antigens from OK-432 and Su-BBM, designated OK-PSA and Su-PSA, respectively. OK-432 markedly induced IFN-gamma and interleukin (IL)-18 as compared with Su-BBM in human peripheral blood mononuclear cells (PBMC). Furthermore, all of the Thl-type and Th1-inducing cytokines tested [IFN-gamma, tumor necrosis factor (TNF)-alpha, IL-12 and IL-18] were secreted by OK-PSA-stimulated PBMC far better than by Su-PSA-treated PBMC. In addition, the cytolytic activities of the PBMC were accelerated by the stimulation with OK-432 or OK-PSA far better than by the stimulation with Su-BBM or Su-PSA. These findings strongly suggested that OK-PSA is a highly important molecule of OK-432 and may be a useful immunotherapeutic agent for the patients with malignant diseases as a potent Th inducer. It was also shown that penicillin treatment effectively enhances OK-PSA-induced anti-cancer immunity.
authors.affiliation: Second Department of Oral and Maxillofacial Surgery, Tokushima University School of Dentistry, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Okamoto
authors.forename: T
authors.initials: T
authors.lastname: Oshikawa
authors.forename: G
authors.initials: G
authors.lastname: Ohe
authors.forename: S
authors.initials: S
authors.lastname: Furuichi
authors.forename: H
authors.initials: H
authors.lastname: Nishikawa
authors.forename: T
authors.initials: T
authors.lastname: Tano
authors.forename: T
authors.initials: T
authors.lastname: Bando
authors.forename: H
authors.initials: H
authors.lastname: Yoshida
authors.forename: S
authors.initials: S
authors.lastname: Matsubara
authors.forename: T
authors.initials: T
authors.lastname: Matsuno
authors.forename: M
authors.initials: M
authors.lastname: Saito
authors.forename: M
authors.initials: M
authors.lastname: Sato
mesh_terms: D020170:Caspase 1 / Q000378:metabolism; D002470:Cell Survival / Q000187:drug effects; D003470:Culture Media; D016207:Cytokines / Q000096:biosynthesis*; D017931:DNA Primers / Q000494:pharmacology; D006801:Humans; D066298:In Vitro Techniques; D008070:Lipopolysaccharides / Q000378:metabolism*; D016253:Microscopy, Immunoelectron; D009000:Monocytes / Q000378:metabolism; D010406:Penicillins / Q000494:pharmacology*; D010844:Picibanil / Q000494:pharmacology*; D012333:RNA, Messenger / Q000096:biosynthesis / Q000302:isolation & purification; D020133:Reverse Transcriptase Polymerase Chain Reaction; D013297:Streptococcus pyogenes / Q000737:chemistry* / Q000378:metabolism*; D013682:Teichoic Acids / Q000378:metabolism*; D018417:Th1 Cells / Q000187:drug effects / Q000378:metabolism
chemical_list: D003470:Culture Media; D016207:Cytokines; D017931:DNA Primers; D008070:Lipopolysaccharides; D010406:Penicillins; D012333:RNA, Messenger; D013682:Teichoic Acids; D010844:Picibanil; C009900:lipoteichoic acid; D020170:Caspase 1