Mycobacterium tuberculosis is protected from NADPH oxidase and LC3-associated phagocytosis by the LCP protein CpsA
Open accessAbstract
Significance: Mycobacterium tuberculosis (Mtb), the causative agent of the disease tuberculosis, grows in macrophages, cells that normally kill bacteria. Recent work has defined a macrophage pathway called “LC3-associated phagocytosis” (LAP) that can eliminate other microbes. LAP is characterized by the recruitment of NADPH oxidase to phagosomes, followed by phagosomal association with LC3 and delivery of the bacteria to a degradative lysosome. Here, we show that LAP does not effectively clear Mtb. The ability of Mtb to inhibit LAP and therefore cause disease depends upon CpsA, a member of the LytR-CpsA-Psr (LCP) protein family, which has previously been implicated in cell-wall metabolism. We demonstrate that Mtb CpsA plays an unexpected role in antagonizing host innate immunity by inhibiting NADPH oxidase and LAP.
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Mtb virulence factor CpsA actively inhibits Nox2 recruitment to phagosomes, preventing Nox2-derived ROS production and LAP killing.
“Through its virulence factor CpsA, Mtb also actively inhibits Nox2 recruitment to phagosomes. By preventing Nox2-derived ROS production, Mtb effectively avoids being targeted and killed by LAP [241,256].”
From Functions of ROS in Macrophages and Antimicrobial Immunity (2021) · cites this paper as [256]
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- Authors
- Köster, S., Upadhyay, S., Chandra, P., Papavinasasundaram, K., Yang, G., Hassan, A., Grigsby, S. J., Mittal, E., Park, H. S., Jones, V., Hsu, F.-F., Jackson, M., Sassetti, C. M., & Philips, J. A.
- Affiliations
- New York University (US)
- Washington University in St. Louis (US)
- University of Massachusetts Chan Medical School (US)
- Colorado State University (US)
- Corresponding author
- Philips, Jennifer A.
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2017-09-27
- Volume
- 114
- Issue
- 41
- Pages
- E8711-E8720
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC5642705
- OpenAlex
- W2764322409
- Cited by
- 208
- References
- 69
- Citations by year
- 2026: 21 · 2025: 25 · 2024: 22 · 2023: 22 · 2022: 25 · 2021: 26 · 2020: 27 · 2019: 19 · 2018: 16 · 2017: 4 · 2012: 1
- FWCI
- 13.83
- Type
- journal article
- Language
- en
- Update notices
- correction (2017-10-30)
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- The Journal of the American Medical Association (JAMA) Network (American Medical Association) (submittedVersion)
- Funders
- HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID) (AI130454, AI064282, AI107774, AI119670)
- Stony Wold-Herbert Fund (Stony Wold-Herbert Fund, Inc.) (N/A)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
- Life Sciences › Immunology and Microbiology › Immunology › Immune responses and vaccinations
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- Mycobacterium tuberculosis, cpsA, LC3-associated phagocytosis, NADPH oxidase, macrophages, phagosome, innate immune evasion, tuberculosis pathogenesis, host-pathogen interaction
- MeSH terms
- NADPH Oxidase 2, Animals, Autophagy, Bacterial Proteins, Female, Macrophages, Male, Mice, Inbred C57BL, Microtubule-Associated Proteins, Mycobacterium tuberculosis, Phagocytosis, Phagosomes, Tuberculosis, Mice, SCID, Reactive Oxygen Species, Mice, Knockout, Mice, Nitric Oxide Synthase Type II, Host-Pathogen Interactions
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