The Pathogenic Neisseria Use a Streamlined Set of Peptidoglycan Degradation Proteins for Peptidoglycan Remodeling, Recycling, and Toxic Fragment Release Article Swipe
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· 2019
· Open Access
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· DOI: https://doi.org/10.3389/fmicb.2019.00073
Neisseria gonorrhoeae and Neisseria meningitidis release peptidoglycan (PG) fragments from the cell as the bacteria grow. For N. gonorrhoeae these PG fragments are known to cause damage to human Fallopian tube tissue in organ culture that mimics the damage seen in patients with pelvic inflammatory disease. N. meningitidis also releases pro-inflammatory PG fragments, but in smaller amounts than those from N. gonorrhoeae. It is not yet known if PG fragment release contributes to the highly inflammatory conditions of meningitis and meningococcemia caused by N. meningitidis. Examination of the mechanisms of PG degradation and recycling identified proteins required for these processes. In comparison to the model organism E. coli, the pathogenic Neisseria have far fewer PG degradation proteins, and some of these proteins show differences in subcellular localization compared to their E. coli homologs. In particular, some N. gonorrhoeae PG degradation proteins were demonstrated to be in the outer membrane while their homologs in E. coli were found free in the periplasm or in the cytoplasm. The localization of two of these proteins was demonstrated to affect PG fragment release. Another major factor for PG fragment release is the allele of ampG. Gonococcal AmpG was found to be slightly defective compared to related PG fragment permeases, thus leading to increased release of PG. A number of additional PG-related factors affect other virulence functions in Neisseria. Endopeptidases and carboxypeptidases were found to be required for type IV pilus production and resistance to hydrogen peroxide. Also, deacetylation of PG was required for virulence of N. meningitidis as well as normal cell size. Overall, we describe the processes involved in PG degradation and recycling and how certain characteristics of these proteins influence the interactions of these pathogens with their host.
Related Topics
- Type
- review
- Language
- en
- Landing Page
- https://doi.org/10.3389/fmicb.2019.00073
- https://www.frontiersin.org/articles/10.3389/fmicb.2019.00073/pdf
- OA Status
- gold
- Cited By
- 23
- References
- 112
- Related Works
- 10
- OpenAlex ID
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Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W2911453485Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.3389/fmicb.2019.00073Digital Object Identifier
- Title
-
The Pathogenic Neisseria Use a Streamlined Set of Peptidoglycan Degradation Proteins for Peptidoglycan Remodeling, Recycling, and Toxic Fragment ReleaseWork title
- Type
-
reviewOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2019Year of publication
- Publication date
-
2019-01-31Full publication date if available
- Authors
-
Ryan E. Schaub, Joseph P. DillardList of authors in order
- Landing page
-
https://doi.org/10.3389/fmicb.2019.00073Publisher landing page
- PDF URL
-
https://www.frontiersin.org/articles/10.3389/fmicb.2019.00073/pdfDirect link to full text PDF
- Open access
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YesWhether a free full text is available
- OA status
-
goldOpen access status per OpenAlex
- OA URL
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https://www.frontiersin.org/articles/10.3389/fmicb.2019.00073/pdfDirect OA link when available
- Concepts
-
Peptidoglycan, Microbiology, Neisseria meningitidis, Neisseria gonorrhoeae, Bacterial outer membrane, Biology, Neisseria, Virulence, Virulence factor, Bacterial cell structure, Cell envelope, Cell wall, Escherichia coli, Bacteria, Biochemistry, Gene, GeneticsTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
23Total citation count in OpenAlex
- Citations by year (recent)
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2025: 5, 2024: 6, 2023: 3, 2022: 5, 2021: 2Per-year citation counts (last 5 years)
- References (count)
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112Number of works referenced by this work
- Related works (count)
-
10Other works algorithmically related by OpenAlex
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