Comparison of peptidase, glycosidase and esterase activities of oral and non-oral Treponema species

Abstract

The enzyme profiles of 20 oral and non-oral Treponema strains were investigated using an API ZYM Complete Research kit. The test included 10 2-naphthyl derivatives of fatty acids, 20 p-nitrophenol derivatives of carbohydrates and 60 2-naphthylamide derivatives of amino acids and peptides. The oral Treponema species investigated were T. denticola, T. vincentii and T. pectinovorum. The non-oral species examined were T. phagedenis, T. hyodysenteriae and intestinal spirochaetes of human and chicken origin. Esterase activities on C5 to Clo fatty acids were common among different Treponema species. Glycosidase activities were infrequently observed in T. vincentii, T. pectinovorum and T. phagedenis Reiter strain. Arabinosidaw, lactosidase and xylssidase activity was observed in the T. hyodysenteriae strains but a-L-fucosidase activity was found only in T. denticola and T. phagedenis. More exo-and endo-peptidase activities were found in T. denticola than in other species. The enteropathogenic T. hyodysenteriae isolates had a very low proteolytic profile. Dipeptidyl prolyl amidase activity was observed in all species except in the T. phagedenis Reiter strain and the avian intestinal spirochaetes. The enzyme profiles did not discriminate between oral and non-oral Treponema species.

Identification of a Treponema denticola OppA Homologue That Binds Host Proteins Present in the Subgingival Environment

“…Neither the OppA peptide nor the gene encoding it were detected in T. pectinovorum or T. socranskii. Interestingly, metabolic requirements of T. pectinovorum and T. socranskii are somewhat distinct from those of T. denticola and T. vincentii (26,28,53,69) and neither possesses the high levels of cell surface peptidase activity characteristic of T. denticola and T. vincentii (53,64). This suggests that OppA may be important for survival of T. denticola in the subgingival environment, perhaps functioning in the acquisition of peptide nutrients.…”

Role of Treponema Denticola in Periodontal Diseases

“…Several proteases or peptidases [a trypsin-like activity, a proline aminopeptidase, a proline iminopeptidase, and an endopeptidase (FLAG-PA)] of T. denticola have been described, and their pathogenic effects have been characterized (Ohta et al, 1986;Makinen KK et al, 1992, 1996Makinen PL et al, 1994Rosen et al, 1994Rosen et al, , 1995Rosen et al, , 1999aFenno et al, 1997Fenno et al, , 1998aMakinen PL and Makinen, 1997; Mikx, 1997;Ishihara et al, 1998). Examination of the enzyme profiles of 20 treponemal strains (Mikx, 1991)-including the oral species T. denticola, T. vincentii, and T. pectinovorum-revealed more exo-and endopeptidase activities in T. denticola than in the other species studied. The presence of peptidases in the outer cell structures of the treponemes points to the importance of these enzymes for the nutrition of the bacteria, and the possible peptidolytic processing of host tissue proteins and peptides to gradually smaller molecules by the bacteria.…”

The Microbial Aetiology of Periodontal Diseases

“…Glycosidase activity was sometimes observed with T. denticola (Mikx, 1991) but not with T. vincentii nor T. pectinovorum (Fiehn, 1986b;Mikx, 1991). P. gingivalis and oral spirochaetes show esterase activity (Lamont & Jenkinson, 1998;Mikx, 1991). In conjunction with phospholipase, esterases may play a role in tissue destruction.…”

“…Bacterial glycosidases may expose host cell-surface sugars which bind to haemagglutinins identified in T. forsythia (Murakami et al, 2002). Glycosidase activity was sometimes observed with T. denticola (Mikx, 1991) but not with T. vincentii nor T. pectinovorum (Fiehn, 1986b;Mikx, 1991). P. gingivalis and oral spirochaetes show esterase activity (Lamont & Jenkinson, 1998;Mikx, 1991).…”

“…Outer sheath (S-layer), outer sheath vesicles (OSV) Grenier, 1991Batista de silva et al, 2004Kaplan et al, 2009;Kolenbrander et al, 1995, Rosen et al, 2008, Yao et al, 1996Kuchn & Kesty, 2005 Impairment of host defences Methyl mercaptan Lipoproteins Suppression of -defensin production Internalisation by epithelial cells Johnson et al, 1992;Lancero et al, 1996Dashper et al, 2011Shin et al, 2010Colombo et al, 2007 Tissue invasion / bone resorption Motility Metabolic end products Phosphatases Trypsin-like protease Tissue degrading enzymes Li et al, 1999;Kataoka et al, 1997Chu et al, 2002Fiehn, 1989;Fukamachi et al, 2005;Kuramitsu et al, 2007;Yoshimura et al, 2000Ishihara et al, 1995Laughon et al, 1982;Loesche et al, 1987;Ohta et al, 1986Fiehn 1986bMikx, 1991;Uitto et al, 1986 Table 5. Virulence factors of T. denticola.…”