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Cyclic di-GMP Signaling Regulates Invasion by Ehrlichia chaffeensis of Human Monocytes
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| Zeitschriftentitel: | Journal of Bacteriology |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | Journal of Bacteriology, 192, 2010, 16, S. 4122-4133 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society for Microbiology
|
| Schlagwörter: |
| author_facet |
Kumagai, Yumi Matsuo, Junji Hayakawa, Yoshihiro Rikihisa, Yasuko Kumagai, Yumi Matsuo, Junji Hayakawa, Yoshihiro Rikihisa, Yasuko |
|---|---|
| author |
Kumagai, Yumi Matsuo, Junji Hayakawa, Yoshihiro Rikihisa, Yasuko |
| spellingShingle |
Kumagai, Yumi Matsuo, Junji Hayakawa, Yoshihiro Rikihisa, Yasuko Journal of Bacteriology Cyclic di-GMP Signaling Regulates Invasion by Ehrlichia chaffeensis of Human Monocytes Molecular Biology Microbiology |
| author_sort |
kumagai, yumi |
| spelling |
Kumagai, Yumi Matsuo, Junji Hayakawa, Yoshihiro Rikihisa, Yasuko 0021-9193 1098-5530 American Society for Microbiology Molecular Biology Microbiology http://dx.doi.org/10.1128/jb.00132-10 <jats:title>ABSTRACT</jats:title> <jats:p> Cyclic di-GMP (c-di-GMP) is a bacterial second messenger produced by GGDEF domain-containing proteins. The genome of <jats:italic>Ehrlichia chaffeensis</jats:italic> , an obligatory intracellular bacterium that causes human monocytic ehrlichiosis, encodes a single protein that contains a GGDEF domain, called PleD. In this study, we investigated the effects of c-di-GMP signaling on <jats:italic>E. chaffeensis</jats:italic> infection of the human monocytic cell line THP-1. Recombinant <jats:italic>E. chaffeensis</jats:italic> PleD showed diguanylate cyclase activity as it generated c-di-GMP <jats:italic>in vitro</jats:italic> . Because c-di-GMP is not cell permeable, the c-di-GMP hydrophobic analog 2′- <jats:italic>O</jats:italic> -di( <jats:italic>tert</jats:italic> -butyldimethylsilyl)-c-di-GMP (CDGA) was used to examine intracellular c-di-GMP signaling. CDGA activity was first tested with <jats:italic>Salmonella enterica</jats:italic> serovar Typhimurium. CDGA inhibited well-defined c-di-GMP-regulated phenomena, including cellulose synthesis, clumping, and upregulation of <jats:italic>csgD</jats:italic> and <jats:italic>adrA</jats:italic> mRNA, indicating that CDGA acts as an antagonist in c-di-GMP signaling. [ <jats:sup>32</jats:sup> P]c-di-GMP bound several <jats:italic>E. chaffeensis</jats:italic> native proteins and two <jats:italic>E. chaffeensis</jats:italic> recombinant I-site proteins, and this binding was blocked by CDGA. Although pretreatment of <jats:italic>E. chaffeensis</jats:italic> with CDGA did not reduce bacterial binding to THP-1 cells, bacterial internalization was reduced. CDGA facilitated protease-dependent degradation of particular, but not all, bacterial surface-exposed proteins, including TRP120, which is associated with bacterial internalization. Indeed, the serine protease HtrA was detected on the surface of <jats:italic>E. chaffeensis</jats:italic> , and TRP120 was degraded by treatment of <jats:italic>E. chaffeensis</jats:italic> with recombinant <jats:italic>E. chaffeensis</jats:italic> HtrA. Furthermore, anti-HtrA inhibited CDGA-induced TRP120 degradation. Our results suggest that <jats:italic>E. chaffeensis</jats:italic> invasion is regulated by c-di-GMP signaling, which stabilizes some bacterial surface-exposed proteins against proteases. </jats:p> Cyclic di-GMP Signaling Regulates Invasion by <i>Ehrlichia chaffeensis</i> of Human Monocytes Journal of Bacteriology |
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American Society for Microbiology, 2010 |
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American Society for Microbiology, 2010 |
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2010 |
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American Society for Microbiology |
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Journal of Bacteriology |
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| title |
Cyclic di-GMP Signaling Regulates Invasion by Ehrlichia chaffeensis of Human Monocytes |
| title_unstemmed |
Cyclic di-GMP Signaling Regulates Invasion by Ehrlichia chaffeensis of Human Monocytes |
| title_full |
Cyclic di-GMP Signaling Regulates Invasion by Ehrlichia chaffeensis of Human Monocytes |
| title_fullStr |
Cyclic di-GMP Signaling Regulates Invasion by Ehrlichia chaffeensis of Human Monocytes |
| title_full_unstemmed |
Cyclic di-GMP Signaling Regulates Invasion by Ehrlichia chaffeensis of Human Monocytes |
| title_short |
Cyclic di-GMP Signaling Regulates Invasion by Ehrlichia chaffeensis of Human Monocytes |
| title_sort |
cyclic di-gmp signaling regulates invasion by
<i>ehrlichia chaffeensis</i>
of human monocytes |
| topic |
Molecular Biology Microbiology |
| url |
http://dx.doi.org/10.1128/jb.00132-10 |
| publishDate |
2010 |
| physical |
4122-4133 |
| description |
<jats:title>ABSTRACT</jats:title>
<jats:p>
Cyclic di-GMP (c-di-GMP) is a bacterial second messenger produced by GGDEF domain-containing proteins. The genome of
<jats:italic>Ehrlichia chaffeensis</jats:italic>
, an obligatory intracellular bacterium that causes human monocytic ehrlichiosis, encodes a single protein that contains a GGDEF domain, called PleD. In this study, we investigated the effects of c-di-GMP signaling on
<jats:italic>E. chaffeensis</jats:italic>
infection of the human monocytic cell line THP-1. Recombinant
<jats:italic>E. chaffeensis</jats:italic>
PleD showed diguanylate cyclase activity as it generated c-di-GMP
<jats:italic>in vitro</jats:italic>
. Because c-di-GMP is not cell permeable, the c-di-GMP hydrophobic analog 2′-
<jats:italic>O</jats:italic>
-di(
<jats:italic>tert</jats:italic>
-butyldimethylsilyl)-c-di-GMP (CDGA) was used to examine intracellular c-di-GMP signaling. CDGA activity was first tested with
<jats:italic>Salmonella enterica</jats:italic>
serovar Typhimurium. CDGA inhibited well-defined c-di-GMP-regulated phenomena, including cellulose synthesis, clumping, and upregulation of
<jats:italic>csgD</jats:italic>
and
<jats:italic>adrA</jats:italic>
mRNA, indicating that CDGA acts as an antagonist in c-di-GMP signaling. [
<jats:sup>32</jats:sup>
P]c-di-GMP bound several
<jats:italic>E. chaffeensis</jats:italic>
native proteins and two
<jats:italic>E. chaffeensis</jats:italic>
recombinant I-site proteins, and this binding was blocked by CDGA. Although pretreatment of
<jats:italic>E. chaffeensis</jats:italic>
with CDGA did not reduce bacterial binding to THP-1 cells, bacterial internalization was reduced. CDGA facilitated protease-dependent degradation of particular, but not all, bacterial surface-exposed proteins, including TRP120, which is associated with bacterial internalization. Indeed, the serine protease HtrA was detected on the surface of
<jats:italic>E. chaffeensis</jats:italic>
, and TRP120 was degraded by treatment of
<jats:italic>E. chaffeensis</jats:italic>
with recombinant
<jats:italic>E. chaffeensis</jats:italic>
HtrA. Furthermore, anti-HtrA inhibited CDGA-induced TRP120 degradation. Our results suggest that
<jats:italic>E. chaffeensis</jats:italic>
invasion is regulated by c-di-GMP signaling, which stabilizes some bacterial surface-exposed proteins against proteases.
</jats:p> |
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| author | Kumagai, Yumi, Matsuo, Junji, Hayakawa, Yoshihiro, Rikihisa, Yasuko |
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| description | <jats:title>ABSTRACT</jats:title> <jats:p> Cyclic di-GMP (c-di-GMP) is a bacterial second messenger produced by GGDEF domain-containing proteins. The genome of <jats:italic>Ehrlichia chaffeensis</jats:italic> , an obligatory intracellular bacterium that causes human monocytic ehrlichiosis, encodes a single protein that contains a GGDEF domain, called PleD. In this study, we investigated the effects of c-di-GMP signaling on <jats:italic>E. chaffeensis</jats:italic> infection of the human monocytic cell line THP-1. Recombinant <jats:italic>E. chaffeensis</jats:italic> PleD showed diguanylate cyclase activity as it generated c-di-GMP <jats:italic>in vitro</jats:italic> . Because c-di-GMP is not cell permeable, the c-di-GMP hydrophobic analog 2′- <jats:italic>O</jats:italic> -di( <jats:italic>tert</jats:italic> -butyldimethylsilyl)-c-di-GMP (CDGA) was used to examine intracellular c-di-GMP signaling. CDGA activity was first tested with <jats:italic>Salmonella enterica</jats:italic> serovar Typhimurium. CDGA inhibited well-defined c-di-GMP-regulated phenomena, including cellulose synthesis, clumping, and upregulation of <jats:italic>csgD</jats:italic> and <jats:italic>adrA</jats:italic> mRNA, indicating that CDGA acts as an antagonist in c-di-GMP signaling. [ <jats:sup>32</jats:sup> P]c-di-GMP bound several <jats:italic>E. chaffeensis</jats:italic> native proteins and two <jats:italic>E. chaffeensis</jats:italic> recombinant I-site proteins, and this binding was blocked by CDGA. Although pretreatment of <jats:italic>E. chaffeensis</jats:italic> with CDGA did not reduce bacterial binding to THP-1 cells, bacterial internalization was reduced. CDGA facilitated protease-dependent degradation of particular, but not all, bacterial surface-exposed proteins, including TRP120, which is associated with bacterial internalization. Indeed, the serine protease HtrA was detected on the surface of <jats:italic>E. chaffeensis</jats:italic> , and TRP120 was degraded by treatment of <jats:italic>E. chaffeensis</jats:italic> with recombinant <jats:italic>E. chaffeensis</jats:italic> HtrA. Furthermore, anti-HtrA inhibited CDGA-induced TRP120 degradation. Our results suggest that <jats:italic>E. chaffeensis</jats:italic> invasion is regulated by c-di-GMP signaling, which stabilizes some bacterial surface-exposed proteins against proteases. </jats:p> |
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| spelling | Kumagai, Yumi Matsuo, Junji Hayakawa, Yoshihiro Rikihisa, Yasuko 0021-9193 1098-5530 American Society for Microbiology Molecular Biology Microbiology http://dx.doi.org/10.1128/jb.00132-10 <jats:title>ABSTRACT</jats:title> <jats:p> Cyclic di-GMP (c-di-GMP) is a bacterial second messenger produced by GGDEF domain-containing proteins. The genome of <jats:italic>Ehrlichia chaffeensis</jats:italic> , an obligatory intracellular bacterium that causes human monocytic ehrlichiosis, encodes a single protein that contains a GGDEF domain, called PleD. In this study, we investigated the effects of c-di-GMP signaling on <jats:italic>E. chaffeensis</jats:italic> infection of the human monocytic cell line THP-1. Recombinant <jats:italic>E. chaffeensis</jats:italic> PleD showed diguanylate cyclase activity as it generated c-di-GMP <jats:italic>in vitro</jats:italic> . Because c-di-GMP is not cell permeable, the c-di-GMP hydrophobic analog 2′- <jats:italic>O</jats:italic> -di( <jats:italic>tert</jats:italic> -butyldimethylsilyl)-c-di-GMP (CDGA) was used to examine intracellular c-di-GMP signaling. CDGA activity was first tested with <jats:italic>Salmonella enterica</jats:italic> serovar Typhimurium. CDGA inhibited well-defined c-di-GMP-regulated phenomena, including cellulose synthesis, clumping, and upregulation of <jats:italic>csgD</jats:italic> and <jats:italic>adrA</jats:italic> mRNA, indicating that CDGA acts as an antagonist in c-di-GMP signaling. [ <jats:sup>32</jats:sup> P]c-di-GMP bound several <jats:italic>E. chaffeensis</jats:italic> native proteins and two <jats:italic>E. chaffeensis</jats:italic> recombinant I-site proteins, and this binding was blocked by CDGA. Although pretreatment of <jats:italic>E. chaffeensis</jats:italic> with CDGA did not reduce bacterial binding to THP-1 cells, bacterial internalization was reduced. CDGA facilitated protease-dependent degradation of particular, but not all, bacterial surface-exposed proteins, including TRP120, which is associated with bacterial internalization. Indeed, the serine protease HtrA was detected on the surface of <jats:italic>E. chaffeensis</jats:italic> , and TRP120 was degraded by treatment of <jats:italic>E. chaffeensis</jats:italic> with recombinant <jats:italic>E. chaffeensis</jats:italic> HtrA. Furthermore, anti-HtrA inhibited CDGA-induced TRP120 degradation. Our results suggest that <jats:italic>E. chaffeensis</jats:italic> invasion is regulated by c-di-GMP signaling, which stabilizes some bacterial surface-exposed proteins against proteases. </jats:p> Cyclic di-GMP Signaling Regulates Invasion by <i>Ehrlichia chaffeensis</i> of Human Monocytes Journal of Bacteriology |
| spellingShingle | Kumagai, Yumi, Matsuo, Junji, Hayakawa, Yoshihiro, Rikihisa, Yasuko, Journal of Bacteriology, Cyclic di-GMP Signaling Regulates Invasion by Ehrlichia chaffeensis of Human Monocytes, Molecular Biology, Microbiology |
| title | Cyclic di-GMP Signaling Regulates Invasion by Ehrlichia chaffeensis of Human Monocytes |
| title_full | Cyclic di-GMP Signaling Regulates Invasion by Ehrlichia chaffeensis of Human Monocytes |
| title_fullStr | Cyclic di-GMP Signaling Regulates Invasion by Ehrlichia chaffeensis of Human Monocytes |
| title_full_unstemmed | Cyclic di-GMP Signaling Regulates Invasion by Ehrlichia chaffeensis of Human Monocytes |
| title_short | Cyclic di-GMP Signaling Regulates Invasion by Ehrlichia chaffeensis of Human Monocytes |
| title_sort | cyclic di-gmp signaling regulates invasion by <i>ehrlichia chaffeensis</i> of human monocytes |
| title_unstemmed | Cyclic di-GMP Signaling Regulates Invasion by Ehrlichia chaffeensis of Human Monocytes |
| topic | Molecular Biology, Microbiology |
| url | http://dx.doi.org/10.1128/jb.00132-10 |