A two-component system is required for colonization of host cells by meningococcus.
In order to adapt to changing environments, bacteria have evolved two-component systems (TCSs) that are able to sense and respond to environmental stimuli. The signal perception relies on a sensor protein whose activation allows rapid adaptation through transcriptional regulation achieved by the regulatory protein. The ability to adhere to and grow on the surface of human host cells is an absolute requirement for many pathogens, including Neisseria meningitidis, in order to colonize new hosts and to disseminate inside their host. Among the four TCSs encoded in the meningococcus genome, only the PhoQ (MisS)/PhoP (MisR) system has been shown to constitute a functional signal transduction circuit. To investigate the involvement of this TCS in the adaptation process requisite for host cell colonization, we have tested the ability to grow on host cells of a mutant inactivated for the sensor of the TCS. Our results demonstrate the involvement of the TCS in the adaptation of the meningococcus to growth on host cells. We show that the expression of the PhoQ (MisS)/PhoP (MisR) TCS is cell-contact controlled. Furthermore, this TCS controls the regulation of a group of genes, the REP2 regulon, previously shown to be cell-contact regulated and to encode functions crucial for the adaptation of the bacterium to host cell colonization. Thus, we provide evidence that one of the four TCSs existing in N. meningitidis contributes to the adaptation of the pathogen to growth on host cells.
Jamet
Anne
A
Université Paris Descartes, Faculté de Médecine René Descartes, F-75006 Paris, France.|Institut National de la Santé et de la Recherche Médicale, Unité 570, F-75015 Paris, France.
Rousseau
Clotilde
C
Université Paris Descartes, Faculté de Médecine René Descartes, F-75006 Paris, France.|Institut National de la Santé et de la Recherche Médicale, Unité 570, F-75015 Paris, France.
Monfort
Jean-Benoît
JB
Université Paris Descartes, Faculté de Médecine René Descartes, F-75006 Paris, France.|Institut National de la Santé et de la Recherche Médicale, Unité 570, F-75015 Paris, France.
Frapy
Eric
E
Université Paris Descartes, Faculté de Médecine René Descartes, F-75006 Paris, France.|Institut National de la Santé et de la Recherche Médicale, Unité 570, F-75015 Paris, France.
Nassif
Xavier
X
Assistance Publique-Hôpitaux de Paris, Hôpital Necker-Enfants Malades, F-75015 Paris, France.|Université Paris Descartes, Faculté de Médecine René Descartes, F-75006 Paris, France.|Institut National de la Santé et de la Recherche Médicale, Unité 570, F-75015 Paris, France.
Martin
Patricia
P
Université Paris Descartes, Faculté de Médecine René Descartes, F-75006 Paris, France.|Institut National de la Santé et de la Recherche Médicale, Unité 570, F-75015 Paris, France.
D000222:Adaptation, Physiological / Q000235:genetics; D001422:Bacterial Adhesion / Q000235:genetics; D001426:Bacterial Proteins / Q000378:metabolism*; D001483:Base Sequence; D002460:Cell Line; D004269:DNA, Bacterial / Q000235:genetics; D015964:Gene Expression Regulation, Bacterial; D054884:Host-Pathogen Interactions; D006801:Humans; D008585:Meningitis, Meningococcal / Q000378:metabolism / Q000382:microbiology*; D008969:Molecular Sequence Data; D009345:Neisseria meningitidis / Q000235:genetics / Q000254:growth & development* / Q000378:metabolism / Q000472:pathogenicity*; D018085:Regulon; D015398:Signal Transduction; D014774:Virulence
D001426:Bacterial Proteins; D004269:DNA, Bacterial; C079792:PhoQ protein, Bacteria; C061064:PhoP protein, Bacteria