Alzheimer's Disease-Like Neurodegeneration in Porphyromonas gingivalis Infected Neurons with Persistent Expression of Active Gingipains.


Journal

Journal of Alzheimer's disease : JAD
ISSN: 1875-8908
Titre abrégé: J Alzheimers Dis
Pays: Netherlands
ID NLM: 9814863

Informations de publication

Date de publication:
2020
Historique:
pubmed: 12 5 2020
medline: 14 5 2021
entrez: 12 5 2020
Statut: ppublish

Résumé

Porphyromonas gingivalis (P. gingivalis) and its gingipain virulence factors have been identified as pathogenic effectors in Alzheimer's disease (AD). In a recent study we demonstrated the presence of gingipains in over 90% of postmortem AD brains, with gingipains localizing to the cytoplasm of neurons. However, infection of neurons by P. gingivalis has not been previously reported. To demonstrate intraneuronal P. gingivalis and gingipain expression in vitro after infecting neurons derived from human inducible pluripotent stem cells (iPSC) with P. gingivalis for 24, 48, and 72 h. Infection was characterized by transmission electron microscopy, confocal microscopy, and bacterial colony forming unit assays. Gingipain expression was monitored by immunofluorescence and RT-qPCR, and protease activity monitored with activity-based probes. Neurodegenerative endpoints were assessed by immunofluorescence, western blot, and ELISA. Neurons survived the initial infection and showed time dependent, infection induced cell death. P. gingivalis was found free in the cytoplasm or in lysosomes. Infected neurons displayed an accumulation of autophagic vacuoles and multivesicular bodies. Tau protein was strongly degraded, and phosphorylation increased at T231. Over time, the density of presynaptic boutons was decreased. P. gingivalis can invade and persist in mature neurons. Infected neurons display signs of AD-like neuropathology including the accumulation of autophagic vacuoles and multivesicular bodies, cytoskeleton disruption, an increase in phospho-tau/tau ratio, and synapse loss. Infection of iPSC-derived mature neurons by P. gingivalis provides a novel model system to study the cellular mechanisms leading to AD and to investigate the potential of new therapeutic approaches.

Sections du résumé

BACKGROUND
Porphyromonas gingivalis (P. gingivalis) and its gingipain virulence factors have been identified as pathogenic effectors in Alzheimer's disease (AD). In a recent study we demonstrated the presence of gingipains in over 90% of postmortem AD brains, with gingipains localizing to the cytoplasm of neurons. However, infection of neurons by P. gingivalis has not been previously reported.
OBJECTIVE
To demonstrate intraneuronal P. gingivalis and gingipain expression in vitro after infecting neurons derived from human inducible pluripotent stem cells (iPSC) with P. gingivalis for 24, 48, and 72 h.
METHODS
Infection was characterized by transmission electron microscopy, confocal microscopy, and bacterial colony forming unit assays. Gingipain expression was monitored by immunofluorescence and RT-qPCR, and protease activity monitored with activity-based probes. Neurodegenerative endpoints were assessed by immunofluorescence, western blot, and ELISA.
RESULTS
Neurons survived the initial infection and showed time dependent, infection induced cell death. P. gingivalis was found free in the cytoplasm or in lysosomes. Infected neurons displayed an accumulation of autophagic vacuoles and multivesicular bodies. Tau protein was strongly degraded, and phosphorylation increased at T231. Over time, the density of presynaptic boutons was decreased.
CONCLUSION
P. gingivalis can invade and persist in mature neurons. Infected neurons display signs of AD-like neuropathology including the accumulation of autophagic vacuoles and multivesicular bodies, cytoskeleton disruption, an increase in phospho-tau/tau ratio, and synapse loss. Infection of iPSC-derived mature neurons by P. gingivalis provides a novel model system to study the cellular mechanisms leading to AD and to investigate the potential of new therapeutic approaches.

Identifiants

pubmed: 32390638
pii: JAD200393
doi: 10.3233/JAD-200393
pmc: PMC7369049
doi:

Substances chimiques

Gingipain Cysteine Endopeptidases 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1361-1376

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Auteurs

Ursula Haditsch (U)

Cortexyme, Inc., South San Francisco, CA, USA.

Theresa Roth (T)

Cortexyme, Inc., South San Francisco, CA, USA.

Leo Rodriguez (L)

Cortexyme, Inc., South San Francisco, CA, USA.

Sandy Hancock (S)

Laboratory for Neurotoxicity Studies, Virginia-Maryland College of Veterinary Medicine, Virginia Tech, Blacksburg, VA, USA.

Thomas Cecere (T)

Laboratory for Neurotoxicity Studies, Virginia-Maryland College of Veterinary Medicine, Virginia Tech, Blacksburg, VA, USA.

Mai Nguyen (M)

Cortexyme, Inc., South San Francisco, CA, USA.

Shirin Arastu-Kapur (S)

Cortexyme, Inc., South San Francisco, CA, USA.

Sean Broce (S)

Cortexyme, Inc., South San Francisco, CA, USA.

Debasish Raha (D)

Cortexyme, Inc., South San Francisco, CA, USA.

Casey C Lynch (CC)

Cortexyme, Inc., South San Francisco, CA, USA.

Leslie J Holsinger (LJ)

Cortexyme, Inc., South San Francisco, CA, USA.

Stephen S Dominy (SS)

Cortexyme, Inc., South San Francisco, CA, USA.

Florian Ermini (F)

Cortexyme, Inc., South San Francisco, CA, USA.

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