Abstract:
:We previously described a cell surface anionic polysaccharide (APS) in Porphyromonas gingivalis that is required for cell integrity and serum resistance. APS is a phosphorylated branched mannan that shares a common epitope with posttranslational additions to some of the Arg-gingipains. This study aimed to determine the mechanism of anchoring of APS to the surface of P. gingivalis. APS was purified on concanavalin A affinity columns to minimize the loss of the anchoring system that occurred during chemical extraction. (1)H nuclear magnetic resonance spectroscopy of the lectin-purified APS confirmed the previous structure but also revealed additional signals that suggested the presence of a lipid A. This was confirmed by fatty acid analysis of the APS and matrix-assisted laser desorption ionization-time of flight mass spectrometry of the lipid A released by treatment with sodium acetate buffer (pH 4.5). Hence, P. gingivalis synthesizes two distinct lipopolysaccharide (LPS) macromolecules containing different glycan repeating units: O-LPS (with O-antigen tetrasaccharide repeating units) and A-LPS (with APS repeating units). Nonphosphorylated penta-acylated and nonphosphorylated tetra-acylated species were detected in lipid A from P. gingivalis total LPS and in lipid A from A-LPS. These lipid A species were unique to lipid A derived from A-LPS. Biological assays demonstrated a reduced proinflammatory activity of A-LPS compared to that of total LPS. Inactivation of a putative O-antigen ligase (waaL) at PG1051, which is required for the final step of LPS biosynthesis, abolished the linkage of both the O antigen and APS to the lipid A core of O-LPS and A-LPS, respectively, suggesting that WaaL in P. gingivalis has dual specificity for both O-antigen and APS repeating units.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Rangarajan M,Aduse-Opoku J,Paramonov N,Hashim A,Bostanci N,Fraser OP,Tarelli E,Curtis MAdoi
10.1128/JB.01868-07subject
Has Abstractpub_date
2008-04-01 00:00:00pages
2920-32issue
8eissn
0021-9193issn
1098-5530pii
JB.01868-07journal_volume
190pub_type
杂志文章abstract::Partially purified inactive glucose dehydrogenase obtained from spores which were heated at 87 or 90 C for 30 min is converted to an active from by the addition of ethylenediaminetetraacetic acid, dipicolinic acid, or some salts. The molecular weight of the inactive glucose dehydrogenase in the heated spores is about ...
journal_title:Journal of bacteriology
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journal_title:Journal of bacteriology
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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journal_title:Journal of bacteriology
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journal_title:Journal of bacteriology
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更新日期:1964-08-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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journal_title:Journal of bacteriology
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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