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Articles by Lianrui Chu
Total Records ( 2 ) for Lianrui Chu
  Yanlai Lai and Lianrui Chu
  Treponema denticola, a periodontal pathogen, has recently been shown to exhibit properties of a facultative anaerobic spirochete, in contrast to its previous recognition as an obligate anaerobic bacterium. In this study, the capacity and possible mechanism of T. denticola survival and growth under aerobic conditions were investigated. Factors detrimental to the growth of T. denticola ATCC 33405, such as oxygen concentration and hydrogen sulfide (H2S) levels as well as the enzyme activities of gamma-glutamyltransferase, cysteinylglycinase, and cystalysin associated with the cells were monitored. The results demonstrated that T. denticola grew only at deeper levels of broth (≥3 ml in a 10-ml tube), high inoculation ratios (≥20% of culture in medium), and short cultivation times (≤4 days for one passage) and in media containing L-cysteine or glutathione as the substrate for H2S production during aerobic growth. The determination of the factors showed that oxygen levels were always lower (0 to 0.6%) with significantly higher concentrations of H2S and higher activities of the three enzymes in all cultures grown aerobically. Further data revealed that H2S production from the T. denticola enzymes plus their substrates resulted in removal of dissolved O2 in the growth cultures in a dose-dependent manner. These results demonstrated that T. denticola was able to generate microanaerobic environments in growth media for its survival and growth under aerobic conditions. Furthermore, the organism can be defined as a true obligate anaerobic spirochete. These findings suggest that spirochetes may play a significant role in maintaining the anaerobic environment at diseased sites in periodontitis.
  Lianrui Chu , Yanlai Lai , Xiaoping Xu , Scott Eddy , Shuang Yang , Li Song and David Kolodrubetz
  The metabolism of glutathione by the periodontal pathogen Treponema denticola produces hydrogen sulfide, which may play a role in the host tissue destruction seen in periodontitis. H2S production in this organism has been proposed to occur via a three enzyme pathway, γ-glutamyltransferase, cysteinylglycinase (CGase), and cystalysin. In this study, we describe the purification and characterization of T. denticola CGase. Standard approaches were used to purify a 52-kDa CGase activity from T. denticola, and high pressure liquid chromatography electrospray ionization tandem mass spectrometry analysis of this molecule showed that it matches the amino acid sequence of a predicted 52-kDa protein in the T. denticola genome data base. A recombinant version of this protein was overexpressed in and purified from Escherichia coli and shown to catalyze the hydrolysis of cysteinylglycine (Cys-Gly) with the same kinetics as the native protein. Surprisingly, because sequence homology indicates that this protein is a member of a family of metalloproteases called M17 leucine aminopeptidases, the preferred substrate for the T. denticola protein is Cys-Gly (kcat/Km of 8.2 µM–1 min–1) not L-Leu-p-NA (kcat/Km of 1.1 µM–1 min–1). The activity of CGase for Cys-Gly is optimum at pH 7.3 and is enhanced by Mn2+, Co2+, or Mg2+ but not by Zn2+ or Ca2+. Importantly, in combination with the two other previously purified T. denticola enzymes, γ-glutamyltransferase and cystalysin, CGase mediates the in vitro degradation of glutathione into the expected end products, including H2S. These results prove that T. denticola contains the entire three-step pathway to produce H2S from glutathione, which may be important for pathogenesis.

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