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Generation, recycling and release of inflammatory peptidoglycan fragments by pathogenic and nonpathogenic Neisseria
Başlık:
Generation, recycling and release of inflammatory peptidoglycan fragments by pathogenic and nonpathogenic Neisseria
Yazar:
Chan, Jia Mun, author.
ISBN:
9780438014435
Yazar Ek Girişi:
Fiziksel Tanımlama:
1 electronic resource (249 pages)
Genel Not:
Source: Dissertation Abstracts International, Volume: 79-10(E), Section: B.
Advisors: Joseph P. Dillard Committee members: Heidi Goodrich-Blair; Federico E. Rey; John-Demian Sauer; Doug B. Weibel; Jon P. Woods.
Özet:
A limited number of Gram-negative bacteria, including the etiological agent of gonorrhea Neisseria gonorrhoeae, release peptidoglycan (PG) fragments generated in the periplasm during normal growth into the extracellular milieu. Certain types of PG fragments, such as PG monomers and some free peptides, are proinflammatory. PG fragments released by N. gonorrhoeae damage the Fallopian tube epithelium by causing death and extrusion of ciliated Fallopian tube cells, which mimics the pathophysiology of pelvic inflammatory disease. The closely related species, N. meningitidis, was recently reported to release PG fragments, albeit at different amounts compared to N. gonorrhoeae. N. meningitidis is infamous for causing highly fatal invasive meningococcal disease despite being more commonly found as an asymptomatic colonizer of the human nasopharyngeal space. N. meningitidis releases lower amounts of proinflammatory PG monomers and breaks down PG fragments more extensively compared to N. gonorrhoeae. The overarching goal of my thesis work is to understand the similarities and differences in PG fragment release by different strains and species of Neisseria. I determined that polymorphisms of a PG recycling permease, AmpG, alter the recycling efficiency and amount of PG monomers released by N. gonorrhoeae, N. meningitidis and the nonpathogenic N. lactamica. I also showed that natural polymorphisms of AmpG lead to intraspecies variations in the amount of PG monomers released by different strains of N. meningitidis and N. lactamica. Additionally, I found that PG-derived peptides released by N. meningitidis include the hNOD1 agonist L-Ala-D-Glu-mesoDAP tripeptide. The innate immune receptor hNOD1 recognizes PG fragments with a terminal mesoDAP, leading to a proinflammatory response. Abolishment of peptide release abrogates the ability of N. meningitidis to stimulate hNOD1 in an in vitro reporter cell line assay. I also characterized the release of PG fragments by multiple species of human- and animal-associated nonpathogenic Neisseria. All of the Neisseria species tested release varying amounts of PG fragments. While all species tested so far release some amount of proinflammatory PG monomers, some do not release PG dimers at all. Cumulatively, my thesis work expands our understanding of the mechanisms and consequences of PG fragment release by various species of Neisseria. .
Notlar:
School code: 0262
Konu Başlığı:
Tüzel Kişi Ek Girişi:
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Yer Numarası | Demirbaş Numarası | Shelf Location | Lokasyon / Statüsü / İade Tarihi |
---|---|---|---|
XX(682636.1) | 682636-1001 | Proquest E-Tez Koleksiyonu | Arıyor... |
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