Chemical Properties of Lipopolysaccharide‐Like Substance (LLS) Extracted from <i>Leptospira interrogans</i> Serovar <i>canicola</i> Strain Moulton

Shimizu, Tadayori; Matsusaka, Eiichiro; Nagakura, Naotaka; Takayanagi, Kazuhisa; Masuzawa, Toshiyuki; Iwamoto, Yoshihisa; Morita, Tamotsu; Mifuchi, Ichiji; Yanagihara, Yasutake

doi:10.1111/j.1348-0421.1987.tb03133.x

Cited by 26 publications

(20 citation statements)

References 28 publications

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“…We have recently applied the procedure described in this study to the isolation of the Leptospira outer membrane. The membrane material purified was found to selectively contain lipopolysaccharide-like substance, a constituent of the Leptospira outer membrane (48,57), and several proteins, including OmpL1. These findings provide additional evidence that this outer membrane isolation procedure can result in selective recovery of the outer membrane and associated protein from several spirochetes.…”

Section: Resultsmentioning

confidence: 99%

Isolation of the outer membranes from Treponema pallidum and Treponema vincentii

et al. 1994

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The outer membranes from Treponema pallidum subsp. pa~idum and Treponema vincentii were isolated by a novel method. Purified outer membranes from T. palidum and T. vincentii following sucrose gradient centrifugation banded at 7 and 31% (wt/wt) sucrose, respectively. Freeze fracture electron microscopy of purified membrane vesicles from T. pallidum and T. vincentii revealed an extremel low density of protein particles; the particle density of T. pallidum was approximately six times less than that of T. vincentii. The great majority of T. vincentii lipopolysaccharide was found in the outer membrane preparation. The T. vincentii outer membrane also contained proteins of 55 and 65 kDa. 1251-penicillin V labeling demonstrated that T. pallidum penicillin-binding proteins were found exclusively with the protoplasmic cylinders and were not detectable with purified outer membrane material, indicating the absence of inner membrane contamination. Isolated T.pallidum outer membrane was devoid of the 19-kDa 4D protein and the normally abundant 47-kDa lipoprotein known to be associated with the cytoplasmic membrane; only trace amounts of the periplasmic endoflagella were detected. Proteins associated with the T. pallidum outer membrane were identified by one-and two-dimensional electrophoretic analysis using gold staining and immunoblotting. Small amounts of strongly antigenic 17-and 45-kDa proteins were detected and shown to correspond to previously identified lipoproteins which are found principally with the cytoplasmic membrane. Less antigenic proteins of 65, 31 (acidic pl), 31 (basic pl), and 28 kDa were identified. Compared with whole-organism preparations, the 65-and the more basic 31-kDa proteins were found to be highly enriched in the outer membrane preparation, indicating that they may represent the T. pallidum rare outer membrane proteins. Reconstitution of solubilized T. paUidum outer membrane into lipid bilayer membranes revealed porin activity with two estimated channel diameters of 0.35 and 0.68 nm based on the measured single-channel conductances in 1 M KCI of 0.40 and 0.76 nS, respectively.The outer membranes of spirochetes, including that of Treponema pallidum subsp. pallidum, the agent of syphilis, are fragile compared with those of typical gram-negative bacteria (17,22,24,39,42,49). Spirochetal outer membranes bleb from the underlying protoplasmic cylinder under relatively mild conditions, including dilute detergents and hypotonic environments (24). Freeze fracture electron microscopy has revealed that the outer membranes of pathogenic spirochetes contain amounts of integral membrane protein that are 1 to 2 orders of magnitude less than those of gram-negative bacteria (45,54,55). This striking feature has been suggested to be a key factor in the pathogenicity of these organisms by contributing to their ability to evade the host immune response and to establish chronic infection (11,15,38,45,54,55).The outer membrane of T. pallidum has an extremely low content of membrane-spanning protein (45, 55), a finding...

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Section: Resultsmentioning

confidence: 99%

Isolation of the outer membranes from Treponema pallidum and Treponema vincentii

et al. 1994

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“…The likely success of identifying true UDP-GlcA decarboxylases using this pattern search is evidenced by our findings in Leptospira species. All six of the Leptospira strains with genomic sequences have Uxs types of UDP-GlcA decarboxylases, and the LPS of Leptospira species has previously been shown to contain xylose (23,35).…”

Section: Discussionmentioning

confidence: 99%

“…Xylose is rarely described as a component of bacterial glycans. Bacterial molecules shown to contain xylose include the O antigen of Pseudomonas aeruginosa serotype O7 (10,25), the core oligosaccharide of the lipopolysaccharide (LPS) of Sinorhizobium meliloti (20), the LPS core oligosaccharide of Ralstonia solanacearum (19), the LPS of Leptospira species (23,35), and an S-layer glycoprotein of Parabacteroides distasonis (15).…”

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confidence: 99%

UDP-Glucuronic Acid Decarboxylases of Bacteroides fragilis and Their Prevalence in Bacteria

et al. 2011

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Xylose is rarely described as a component of bacterial glycans. UDP-xylose is the nucleotide-activated form necessary for incorporation of xylose into glycans and is synthesized by the decarboxylation of UDP-glucuronic acid (UDP-GlcA). Enzymes with UDP-GlcA decarboxylase activity include those that lead to the formation of UDP-xylose as the end product (Uxs type) and those synthesizing UDP-xylose as an intermediate (ArnA and RsU4kpxs types). In this report, we identify and confirm the activities of two Uxs-type UDP-GlcA decarboxylases of Bacteroides fragilis, designated BfUxs1 and BfUxs2. Bfuxs1 is located in a conserved region of the B. fragilis genome, whereas Bfuxs2 is in the heterogeneous capsular polysaccharide F (PSF) biosynthesis locus. Deletion of either gene separately does not result in the loss of a detectable phenotype, but deletion of both genes abrogates PSF synthesis, strongly suggesting that they are functional paralogs and that the B. fragilis NCTC 9343 PSF repeat unit contains xylose. UDP-GlcA decarboxylases are often annotated incorrectly as NAD-dependent epimerases/dehydratases; therefore, their prevalence in bacteria is underappreciated. Using available structural and mutational data, we devised a sequence pattern to detect bacterial genes encoding UDP-GlcA decarboxylase activity. We identified 826 predicted UDP-GlcA decarboxylase enzymes in diverse bacterial species, with the ArnA and RsU4kpxs types confined largely to proteobacterial species. These data suggest that xylose, or a monosaccharide requiring a UDP-xylose intermediate, is more prevalent in bacterial glycans than previously appreciated. Genes encoding BfUxs1-like enzymes are highly conserved in Bacteroides species, indicating that these abundant intestinal microbes may synthesize a conserved xylose-containing glycan.

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“…Some lipids are stored associated with GLP (palmitovacenic, linoleic, and oleic acids) [62], while others are stored associated with LPS and LLS (hydroxylauric, palmitic, and oleic acids) [64, 65]. These reports indicate that leptospiras are able to store and associate fatty acids with their endotoxins (LPS and GLP).…”

Section: Leptospira Metabolism and Endotoxinsmentioning

confidence: 99%

Leptospiraand Inflammation

Gonçalves-de-Albuquerque

Burth

Silva

et al. 2012

Mediators of Inflammation

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Leptospirosis is an important zoonosis and has a worldwide impact on public health. This paper will discuss both the role of immunogenic and pathogenic molecules during leptospirosis infection and possible new targets for immunotherapy against leptospira components. Leptospira, possess a wide variety of mechanisms that allow them to evade the host immune system and cause infection. Many molecules contribute to the ability of Leptospira to adhere, invade, and colonize. The recent sequencing of the Leptospira genome has increased our knowledge about this pathogen. Although the virulence factors, molecular targets, mechanisms of inflammation, and signaling pathways triggered by leptospiral antigens have been studied, some questions are still unanswered. Toll-like receptors (TLRs) are the primary sensors of invading pathogens. TLRs recognize conserved microbial pattern molecules and activate signaling pathways that are pivotal to innate and adaptive immune responses. Recently, a new molecular target has emerged—the Na/K-ATPase—which may contribute to inflammatory and metabolic alteration in this syndrome. Na/K-ATPase is a target for specific fatty acids of host origin and for bacterial components such as the glycolipoprotein fraction (GLP) that may lead to inflammasome activation. We propose that in addition to TLRs, Na/K-ATPase may play a role in the innate response to leptospirosis infection.

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Chemical Properties of Lipopolysaccharide‐Like Substance (LLS) Extracted from Leptospira interrogans Serovar canicola Strain Moulton

Cited by 26 publications

References 28 publications

Isolation of the outer membranes from Treponema pallidum and Treponema vincentii

Isolation of the outer membranes from Treponema pallidum and Treponema vincentii

UDP-Glucuronic Acid Decarboxylases of Bacteroides fragilis and Their Prevalence in Bacteria

Leptospiraand Inflammation

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