Implication of Antigenic Conversion of Helicobacter pylori Lipopolysaccharides That Involve Interaction with Surfactant Protein D

Yokota, Shinichi; Amano, Ken‐ichi; Nishitani, Chiaki; Ariki, Shigeru; Kuroki, Yoshio; Fujii, Nobuhiro

doi:10.1128/iai.00345-12

Cited by 12 publications

(5 citation statements)

References 45 publications

(64 reference statements)

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“…SP-D has been previously shown to bind to the LPS of many diverse pathogenic Gram-negative bacteria such as Pseudomonas aeruginosa , uropathogenic E . coli , Klebsiella pneumoniae and Helicobacter pylori in a calcium-dependent manner that can be inhibited by carbohydrate [ 11 , 19 , 28 , 29 ]. Furthermore, it was determined C .…”

Section: Discussionmentioning

confidence: 99%

Surfactant Protein D Binds to Coxiella burnetii and Results in a Decrease in Interactions with Murine Alveolar Macrophages

2015

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Coxiella burnetii is a Gram-negative, obligate intracellular bacterium and the causative agent of Q fever. Infections are usually acquired after inhalation of contaminated particles, where C. burnetii infects its cellular target cells, alveolar macrophages. Respiratory pathogens encounter the C-type lectin surfactant protein D (SP-D) during the course of natural infection. SP-D is a component of the innate immune response in the lungs and other mucosal surfaces. Many Gram-negative pulmonary pathogens interact with SP-D, which can cause aggregation, bactericidal effects and aid in bacterial clearance. Here we show that SP-D binds to C. burnetii in a calcium-dependent manner with no detectable bacterial aggregation or bactericidal effects. Since SP-D interactions with bacteria often alter macrophage interactions, it was determined that SP-D treatment resulted in a significant decrease in C. burnetii interactions to a mouse alveolar macrophage model cell line MH-S indicating SP-D causes a significant decrease in phagocytosis. The ability of SP-D to modulate macrophage activation by C. burnetii was tested and it was determined that SP-D does not alter the correlates measured for macrophage activation. Taken together these studies support those demonstrating limited activation of alveolar macrophages with C. burnetii and demonstrate interactions with SP-D participate in reduction of phagocyte attachment and phagocytosis.

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Section: Discussionmentioning

confidence: 99%

Surfactant Protein D Binds to Coxiella burnetii and Results in a Decrease in Interactions with Murine Alveolar Macrophages

2015

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“…Being embedded in the bacterial outer membrane, LPS constitutes a barrier protecting H. pylori from the compounds that could be potentially toxic for the bacterium. Yokota et al (2012) proposed the division of LPS into two antigenic phenotypesweakly antigenic epitope-carrying LPS and highly antigenic epitope-carrying LPS that is most prevalently expressed in GC patients with chronic and severe inflammation [170].…”

Section: Lipopolysaccharidementioning

confidence: 99%

Helicobacter pylori Virulence Factors—Mechanisms of Bacterial Pathogenicity in the Gastric Microenvironment

Baj

Forma

Sitarz

et al. 2020

Cells

179

111

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Gastric cancer constitutes one of the most prevalent malignancies in both sexes; it is currently the fourth major cause of cancer-related deaths worldwide. The pathogenesis of gastric cancer is associated with the interaction between genetic and environmental factors, among which infection by Helicobacter pylori (H. pylori) is of major importance. The invasion, survival, colonization, and stimulation of further inflammation within the gastric mucosa are possible due to several evasive mechanisms induced by the virulence factors that are expressed by the bacterium. The knowledge concerning the mechanisms of H. pylori pathogenicity is crucial to ameliorate eradication strategies preventing the possible induction of carcinogenesis. This review highlights the current state of knowledge and the most recent findings regarding H. pylori virulence factors and their relationship with gastric premalignant lesions and further carcinogenesis.

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“…An earlier investigation on binding of surfactant protein A (SP-A) has shown the Ca þ2-independency in binding to lipid-A of bacterial LPS and was not inhibited by competing saccharides (28). However, a recent study showed the binding of surfactant protein-D (SP-D) to Helicobacter pylori LPS in a Ca þ2 dependent manner (29) and also revealed the involvement of b-linked NAGA and b-linked D-Glucose of core polysaccharide in binding with LPS that was inhibited by methyl b-D-Galactoside (30). Although the conglutinin is known to evolve from SP-D (31), we observed Ca þ2 -independency in LPS binding in the present study.…”

Section: Discussionmentioning

confidence: 96%

Prokaryotic Expression ofOvis ariesConglutinin Encoding Neck and Carbohydrate Recognition Domain and its Functional Characterization

Mohan

Saini

Ramesh

et al. 2014

Animal Biotechnology

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Conglutinin, a soluble pattern recognition receptor of innate immune system in bovines is known for its potential defensive activity against microorganisms either by direct agglutination in the presence of calcium or by acting as opsonin. In the present study, sheep (Ovis aries) conglutinin encoding neck and carbohydrate recognition domain (rSCGN) was expressed in the E coli BL21 expression host. The recombinant conglutinin revealed molecular weight of 27 kDa in SDS PAGE and also in western blotting using antibuffalo conglutinin polyclonal serum. The protein was characterized further for its functional activity in various assays. In ELISA based sugar and LPS binding assay, the rSCGN revealed its high binding activity toward N-acetyl glucosamine and E. coli LPS in the presence and the absence of calcium ions, respectively. Hemagglutination of chicken red blood cells caused by Newcastle disease virus was not inhibited in the presence of rSCGN as it lacked complete collagenous region present in the native protein. In virus neutralization test, the recombinant protein was found to reduce multiplication of bovine herpes virus-1 propagated in MDBK cells. This prokaryotically expressed 27 kDa recombinant sheep conglutinin can serve as antigen in future studies to develop sandwich ELISA for assessing the level of native conglutinin in sheep serum.

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Implication of Antigenic Conversion of Helicobacter pylori Lipopolysaccharides That Involve Interaction with Surfactant Protein D

Cited by 12 publications

References 45 publications

Surfactant Protein D Binds to Coxiella burnetii and Results in a Decrease in Interactions with Murine Alveolar Macrophages

Surfactant Protein D Binds to Coxiella burnetii and Results in a Decrease in Interactions with Murine Alveolar Macrophages

Helicobacter pylori Virulence Factors—Mechanisms of Bacterial Pathogenicity in the Gastric Microenvironment

Prokaryotic Expression ofOvis ariesConglutinin Encoding Neck and Carbohydrate Recognition Domain and its Functional Characterization

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