• Helicobacter pylori
• antibiotic‐free strategies
• bioengineering
• gold nanoparticles
• lipids
• self‐assembled monolayers

• 951723 European Union's Horizon 2020
• 02/C05-i01.01/2022.PC644937233-00000047 Health from Portugal
• FCT-Fundação para a Ci ência e Tecnologia

• Antibacterial target
• Membrane
• Phospholipid
• Phospholipid biosynthesis
• Phospholipid ligands

• Anti-Bacterial Agents/pharmacology
• Anti-Bacterial Agents/chemistry
• Anti-Bacterial Agents/chemical synthesis
• Phospholipids/chemistry
• Phospholipids/metabolism
• Bacteria/drug effects
• Bacteria/metabolism
• Drug Discovery
• Humans
• Animals
• Structure-Activity Relationship
• Bacterial Infections/drug therapy
• Bacterial Infections/metabolism
• Bacterial Infections/microbiology

• Anti-infection
• Helicobacter pylori
• Huangjiu
• Jatrorrhizine
• Phellodendron chinense C.K.Schneid

• Helicobacter pylori/drug effects
• Phellodendron/chemistry
• Anti-Bacterial Agents/pharmacology
• Plant Extracts/pharmacology
• Plant Extracts/chemistry
• Berberine/pharmacology
• Microbial Sensitivity Tests
• Urease/metabolism
• Humans
• Helicobacter Infections/drug therapy
• Helicobacter Infections/microbiology

• Humans
• Hyperlipidemias/drug therapy
• Hyperlipidemias/complications
• Hypolipidemic Agents/therapeutic use
• Male
• Female
• Middle Aged
• Incidence
• Peptic Ulcer/prevention & control
• Peptic Ulcer/complications
• Aged
• Cohort Studies
• Adult
• Taiwan/epidemiology

• Casual effect
• Mendelian randomization
• Peptic ulcer
• Ratio of cholesterol to total lipids in medium VLDL
• Single nucleotide polymorphism

• Helicobacter pylori
• Macrophages
• gastric cancer
• gastritis

• Parkinson's disease
• fluorescent biomarker
• glucosyl-sterols
• lysosome
• neurodegenerative disease

• Fluorescent Dyes/chemistry
• Neurodegenerative Diseases/metabolism
• Neurons/metabolism
• Lysosomes/metabolism
• Lysosomes/chemistry
• Sterols/chemistry
• Humans
• Animals

• Università Ca' Foscari Venezia
• Dipartimento di Biologia, Università degli Studi di Padova

• Helicobacter pylori
• gastritis
• immunocompetent cells
• trained immunity

• Humans
• Helicobacter Infections/immunology
• Helicobacter Infections/microbiology
• Helicobacter pylori/immunology
• Immunity, Innate
• Immune Tolerance
• Animals
• Gastric Mucosa/immunology
• Gastric Mucosa/microbiology
• Gastric Mucosa/pathology
• Gastritis/immunology
• Gastritis/microbiology
• Immunologic Memory
• Trained Immunity

• Helicobacter pylori
• Adhesion
• Biosynthesis
• Cholesterol
• Membrane
• Phospholipids

• Helicobacter pylori/metabolism
• Helicobacter pylori/physiology
• Mice
• Animals
• Humans
• Membrane Lipids/metabolism
• Cell Line, Tumor
• Helicobacter Infections/drug therapy
• Helicobacter Infections/microbiology
• Helicobacter Infections/metabolism
• Cholesterol Esters/metabolism
• Cholesterol/analogs & derivatives

• AS-GC-110-MD04 Academia Sinica
• 111-2113-M-001-036 National Science and Technology Council

• Helicobacter pylori
• Clarithromycin/pharmacology
• Virulence
• Metabolic Reprogramming
• Anti-Infective Agents

• Malaysian Ministry of Higher Education, Malaysia

• H. pylori phospholipase A
• Host-pathogen interaction
• TNFR1 signaling
• innate immunity
• membrane fluidity

• Helicobacter pylori
• Receptors, Tumor Necrosis Factor, Type I/metabolism
• Receptors, Tumor Necrosis Factor, Type I/genetics
• Macrophages/immunology
• Macrophages/microbiology
• Macrophages/metabolism
• Animals
• Mice
• Helicobacter Infections/microbiology
• Helicobacter Infections/immunology
• Helicobacter Infections/metabolism
• p38 Mitogen-Activated Protein Kinases/metabolism
• Signal Transduction
• Mice, Inbred C57BL
• Humans
• Bacterial Proteins/metabolism
• Bacterial Proteins/genetics
• MAP Kinase Signaling System
• Apoptosis

• O antigen
• Shigella flexneri
• fatty acids
• lipid droplets
• lipid homeostasis
• lipopolysaccharide

• Humans
• Bacterial Proteins/metabolism
• Shigella flexneri/metabolism
• Fatty Acids/metabolism
• Lipids

• 1159752 DHAC | National Health and Medical Research Council (NHMRC)
• 1143974 DHAC | National Health and Medical Research Council (NHMRC)
• DP160103903 Department of Education and Training | Australian Research Council (ARC)

• Humans
• Anti-Bacterial Agents/chemistry
• Cholecalciferol/pharmacology
• Helicobacter Infections/drug therapy
• Helicobacter Infections/microbiology
• Helicobacter pylori
• Indenes/chemistry
• Indenes/pharmacology
• Microbial Sensitivity Tests
• Phosphatidylethanolamines

• lipid
• bacterial and viral infections
• lipid droplets
• lipid metabolism
• phospholipids

• Fatty Acids/metabolism
• Lipid Metabolism
• Phospholipids
• Triglycerides
• Biology

• h. pylori
• mortality
• morbidity
• dyslipidemia
• gastric cancer

• Humans
• Helicobacter pylori
• Gastritis/complications
• Gastritis, Atrophic
• Peptic Ulcer
• Stomach Neoplasms/complications
• Helicobacter Infections/complications
• Helicobacter Infections/epidemiology

• ADP-heptose
• ALPK1-TIFA
• Bacterial heptose metabolites
• CagT4SS
• Gastric epithelial cells
• Helicobacter pylori
• Infection
• Innate immunity
• Myeloid cells

• CARC domain
• CRAC domain
• Catalase
• Cholesterol
• Helicobacter pylori
• KatA

• Humans
• Bacterial Proteins/genetics
• Bacterial Proteins/metabolism
• Catalase/genetics
• Catalase/metabolism
• Cholesterol/metabolism
• Helicobacter Infections/microbiology
• Helicobacter pylori/genetics
• Helicobacter pylori/metabolism
• Biological Transport

• Helicobacter pylori
• CD1d
• Mincle
• cholesteryl glycoside
• invariant NKT cell

• H. pylori
• Immune evasion
• Immune response
• Persistence

• Humans
• Helicobacter pylori
• Persistent Infection
• Stomach Neoplasms
• Biology

The human gastric epithelium forms highly organized gland structures with different subtypes of cells. The carcinogenic bacterium Helicobacter pylori can attach to gastric cells and subsequently translocate its virulence factor CagA, but the possible host cell tropism of H. pylori is currently unknown. Here, we report that H. pylori preferentially attaches to differentiated cells in the pit region of gastric units. Single-cell RNA-seq shows that organoid-derived monolayers recapitulate the pit region, while organoids capture the gland region of the gastric units. Using these models, we show that H. pylori preferentially attaches to highly differentiated pit cells, marked by high levels of GKN1, GKN2 and PSCA. Directed differentiation of host cells enable enrichment of the target cell population and confirm H. pylori preferential attachment and CagA translocation into these cells. Attachment is independent of MUC5AC or PSCA expression, and instead relies on bacterial TlpB-dependent chemotaxis towards host cell-released urea, which scales with host cell size.

The carcinogenic bacterium Helicobacter pylori infects gastric cells. Here, the authors show that H. pylori preferentially infects differentiated cells in the pit region of gastric units, and this relies on bacterial chemotaxis towards host cell-released urea, which scales with host cell size.

Helicobacter pylori (H. pylori) is an important pathogen that can cause gastric cancer. Multiple adhesion molecules mediated H. pylori adherence to cells is the initial step in the infection of host cells. H. pylori cholesterol-α-glucosyltransferase (CGT) recognizes and extracts cholesterol from cell membranes to destroy lipid raft structure, further promotes H. pylori adhesion to gastric epithelial cells. O-Glycan, a substance secreted by the deep gastric mucosa, can competitively inhibit CGT activity and may serve as an important factor to prevent H. pylori colonization in the deep gastric mucosa. However, the inhibitory and injury-protection effects of O-Glycan against H. pylori infection has not been well investigated. In this study, we found that O-Glycan significantly inhibited the relative urease content in the coinfection system. In the presence of O-glycan, the injury of GES-1 cells in H. pylori persistent infection model was attenuated and the cell viability was increased. We use fluorescein isothiocyanate-conjugated cholera toxin subunit B (FITC-CTX-B) to detect lipid rafts on gastric epithelial cells and observed that O-glycan can protect H. pylori from damaging lipid raft structures on cell membranes. In addition, transcriptome data showed that O-glycan treatment significantly reduced the activation of inflammatory cancer transformation pathway caused by H. pylori infection. Our results suggest that O-Glycan is able to inhibit H. pylori persistent infection of gastric epithelial cells, reduce the damage caused by H. pylori, and could serve as a potential medicine to treat patients infected with H. pylori.

• Helicobacter pylori
• O-Glycan
• cholesterol-α-glucosyltransferase
• gastric cancer

Helicobacter pylori is a pathogen that colonizes the stomach and causes chronic gastritis. Helicobacter pylori can colonize deep inside gastric glands, triggering increased R‐spondin 3 (Rspo3) signaling. This causes an expansion of the “gland base module,” which consists of self‐renewing stem cells and antimicrobial secretory cells and results in gland hyperplasia. The contribution of Rspo3 receptors Lgr4 and Lgr5 is not well explored. Here, we identified that Lgr4 regulates Lgr5 expression and is required for H. pylori‐induced hyperplasia and inflammation, while Lgr5 alone is not. Using conditional knockout mice, we reveal that R‐spondin signaling via Lgr4 drives proliferation of stem cells and also induces NF‐κB activity in the proliferative stem cells. Upon exposure to H. pylori, the Lgr4‐driven NF‐κB activation is responsible for the expansion of the gland base module and simultaneously enables chemokine expression in stem cells, resulting in gland hyperplasia and neutrophil recruitment. This demonstrates a connection between R‐spondin‐Lgr and NF‐κB signaling that links epithelial stem cell behavior and inflammatory responses to gland‐invading H. pylori.

• Helicobacter pylori
• Lgr4
• Lgr5
• NF-κB
• R-spondin 3

Helicobacter pylori (H. pylori), creating a global infection rate over 50%, presents great challenges in clinical therapies due to its complex pathological microenvironment in vivo. To improve the eradication efficacy, herein we fabricated a pharmaceutical vesicle RHL/Cl-Ch-cal where cholesterol-PEG, calcitriol and first-line antibiotic clarithromycin were co-loaded in the rhamnolipid-composed outer lipid layer. RHL/Cl-Ch-cal could quickly penetrate through gastric mucus layer to reach H. pylori infection sites, and then effectively destroyed the architecture of H. pylori biofilms, killed dispersed H. pylori and inhibited the re-adhesion of residual bacteria (called biofilms eradication tetralogy). Moreover, RHL/Cl-Ch-cal activated the host immune response to H. pylori by replenishing cholesterol to repair lipid raft on the cell membrane of host epithelial cells. Finally, RHL/Cl-Ch-cal killed the intracellular H. pylori through recovering the lysosomal acidification and assisting degradation. In experiments, RHL/Cl-Ch-cal demonstrated prominent anti-H. pylori efficacy in the classical H. pylori-infected mice model. Therefore, the study provides a “comprehensive attack” strategy for anti-H. pylori therapies including biofilms eradication tetralogy, immune activation and intracellular bacteria killing.

Microbial infections are sensed by the host immune system by recognizing signature molecules called Pathogen-Associated Molecular Patterns—PAMPs. The binding of these biomolecules to innate immune receptors, called Pattern Recognition Receptors (PRRs), alerts the host cell, activating microbicidal and pro-inflammatory responses. The outcome of the inflammatory cascade depends on the subtle balance between the bacterial burn and the host immune response. The role of PRRs is to promote the clearance of the pathogen and to limit the infection by bumping inflammatory response. However, many bacteria, including Helicobacter pylori, evolved to escape PRRs’ recognition through different camouflages in their molecular pattern. This review examines all the different types of H. pylori PAMPs, their roles during the infection, and the mechanisms they evolved to escape the host recognition.

• ADP-heptose
• LPS
• OMV
• PAMP

Helicobacter pylori colonizes half of the global population and causes gastritis, peptic ulcer disease or gastric cancer. In this study, we were interested in human annexin (ANX), which comprises a protein family with diverse and partly unknown physiological functions, but with a potential role in microbial infections and possible involvement in gastric cancer. We demonstrate here for the first time that H. pylori is able to specifically bind ANXs. Binding studies with purified H. pylori LPS and specific H. pylori LPS mutant strains indicated binding of ANXA5 to lipid A, which was dependent on the lipid A phosphorylation status. Remarkably, ANXA5 binding almost completely inhibited LPS-mediated Toll-like receptor 4- (TLR4) signaling in a TLR4-specific reporter cell line. Furthermore, the interaction is relevant for gastric colonization, as a mouse-adapted H. pylori increased its ANXA5 binding capacity after gastric passage and its ANXA5 incubation in vitro interfered with TLR4 signaling. Moreover, both ANXA2 and ANXA5 levels were upregulated in H. pylori-infected human gastric tissue, and H. pylori can be found in close association with ANXs in the human stomach. Furthermore, an inhibitory effect of ANXA5 binding for CagA translocation could be confirmed. Taken together, our results highlight an adaptive ability of H. pylori to interact with the host cell factor ANX potentially dampening innate immune recognition.

H. pylori is very well adapted to its natural habitat, the human gastric mucosa. For this purpose, the bacterium has evolved a number of highly specific virulence factors, such as the cag-type IV secretion system, vacuolating cytotoxin A (VacA) or secreted gamma-glutamyl transpeptidase. An important function of these bacterial factors is to manipulate the host immune response to enable a chronic H. pylori infection. The present work identifies a new player in this process. Here, we have discovered that H. pylori, as well as several other bacterial species, can bind human annexins (ANX), suggesting a more widespread phenomenon. We show that H. pylori specifically binds ANXA5 via lipid A. The interaction is strictly dependent on calcium and modulated by the phosphorylation status of lipid A. Notably, ANXA5 binding strongly inhibits LPS-mediated Toll-like receptor 4 (TLR4) signal transduction, suggesting that H. pylori exploits ANXs binding to avoid its recognition by this important receptor of the innate immune system. The study thus provides novel molecular and mechanistic insights into a further strategy of H. pylori to successfully evade recognition by the host.

• Animals
• Annexins/metabolism
• Gastric Mucosa
• Helicobacter Infections/metabolism
• Helicobacter pylori/metabolism
• Humans
• Lipid A
• Lipopolysaccharides/metabolism
• Mice
• Stomach Neoplasms/metabolism
• Toll-Like Receptor 4/genetics
• Toll-Like Receptor 4/metabolism

• Deutsche Forschungsgemeinschaft
• LMU Munich FöFoLe Program

• meta analyses
• microorganism
• neurodegenerative disorders
• observational studies
• umbrella review

• Cholesterol
• Gastric cancer
• Lipid
• Menopause

During autophagy defense against invading microbes, certain lipid types are indispensable for generating specialized membrane-bound organelles. The lipid composition of autophagosomes remains obscure, as does the issue of how specific lipids and lipid-associated enzymes participate in autophagosome formation and maturation. Helicobacter pylori is auxotrophic for cholesterol and converts cholesterol to cholesteryl glucoside derivatives, including cholesteryl 6ʹ-O-acyl-α-d-glucoside (CAG). We investigated how CAG and its biosynthetic acyltransferase assist H. pylori to escape host-cell autophagy.

We applied a metabolite-tagging method to obtain fluorophore-containing cholesteryl glucosides that were utilized to understand their intracellular locations. H. pylori 26695 and a cholesteryl glucosyltransferase (CGT)-deletion mutant (ΔCGT) were used as the standard strain and the negative control that contains no cholesterol-derived metabolites, respectively. Bacterial internalization and several autophagy-related assays were conducted to unravel the possible mechanism that H. pylori develops to hijack the host-cell autophagy response. Subcellular fractions of H. pylori-infected AGS cells were obtained and measured for the acyltransferase activity.

The imaging studies of fluorophore-labeled cholesteryl glucosides pinpointed their intracellular localization in AGS cells. The result indicated that CAG enhances the internalization of H. pylori in AGS cells. Particularly, CAG, instead of CG and CPG, is able to augment the autophagy response induced by H. pylori. How CAG participates in the autophagy process is multifaceted. CAG was found to intervene in the degradation of autophagosomes and reduce lysosomal biogenesis, supporting the idea that intracellular H. pylori is harbored by autophago-lysosomes in favor of the bacterial survival. Furthermore, we performed the enzyme activity assay of subcellular fractions of H. pylori-infected AGS cells. The analysis showed that the acyltransferase is mainly distributed in autophago-lysosomal compartments.

Our results support the idea that the acyltransferase is mainly distributed in the subcellular compartment consisting of autophagosomes, late endosomes, and lysosomes, in which the acidic environment is beneficial for the maximal acyltransferase activity. The resulting elevated level of CAG can facilitate bacterial internalization, interfere with the autophagy flux, and causes reduced lysosomal biogenesis.

The online version contains supplementary material available at 10.1186/s12929-021-00768-w.

• Autophagosomes
• Autophagy
• Autophagy flux
• Bacterial internalization
• Cholesteryl glucosides
• H. pylori
• Lipid-raft clustering
• Lysosome biogenesis
• Lysosomes

Helicobacter pylori infection is associated with several gastrointestinal diseases, including gastritis, peptic ulcers, and gastric cancer. Infection of cells with H. pylori is dependent on lipid rafts, which are cholesterol-rich microdomains located in the cell membrane. H. pylori cholesterol-α-glucosyltransferase (CGT) catalyzes the conversion of membrane cholesterol to cholesteryl glucosides, which can be incorporated into the bacterial cell wall, facilitating evasion from immune defense and colonization in the host. However, the detailed mechanisms underlying this process remain to be explored. In this study, we discovered for the first time that H. pylori CGT could promote adherence to gastric epithelial cells in a cholesterol-dependent manner. Externalization of cell membrane phosphatidylserine (PS) is crucial for enhancement of binding of H. pylori to cells by CGT and for cytotoxin-associated gene A (CagA)-induced pathogenesis. Furthermore, exogenous cholesterol interferes with the actions of H. pylori CGT to catalyze cellular cholesterol, which impedes bacterial binding to cells and attenuates subsequent inflammation, indicating that the initial attachment of H. pylori to cells is closely dependent on host cholesterol. These results provide evidence that CGT contributes to H. pylori infectivity and it may serve as a key target for the treatment of H. pylori-associated diseases.

• Helicobacter pylori
• cholesterol glucosylation
• inflammation
• phosphatidylserine

• Helicobacter pylori
• cholesterol
• gastric cancer
• reactive oxygen species
• statin

• 109-2320-B-182-025-MY3, 109-2320-B-182-029-MY3, and 109-2622-B-182-002 Ministry of Science and Technology, Taiwan
• CMRPD1I0061-3, CMRPD1J0021-3, CMRPD1K0361, and BMRPE90 Chang Gung Memorial Hospital, Linkou

• Borrelia burgdorferi/genetics
• Borrelia burgdorferi/metabolism
• Galactosyltransferases/metabolism
• Galactosyltransferases/genetics
• Lyme Disease/microbiology
• Glycolipids/metabolism
• Cholesterol/metabolism
• Amino Acid Sequence
• Bacterial Proteins/metabolism
• Bacterial Proteins/genetics
• Humans

• R01 AI141656 NIAID NIH HHS
• National Institute of Allergy and Infectious Diseases

• BRCA1
• BRCAness
• CagA
• DNA double-strand break
• Helicobacter pylori
• PAR1b
• gastric cancer
• genome instability
• homologous recombination
• replication fork instability

• Adult
• Aged
• Aged, 80 and over
• Animals
• Antigens, Bacterial/metabolism
• BRCA1 Protein/metabolism
• Bacterial Proteins/metabolism
• Carcinogenesis/metabolism
• Cell Line
• DNA Breaks, Double-Stranded
• Epithelial Cells/metabolism
• Epithelial Cells/microbiology
• Female
• Gene Expression Regulation, Neoplastic
• Genomic Instability
• Helicobacter Infections/microbiology
• Helicobacter pylori/metabolism
• Helicobacter pylori/pathogenicity
• Host-Pathogen Interactions
• Humans
• Male
• Mice
• Mice, Inbred C57BL
• Mice, Transgenic
• Middle Aged
• Phosphorylation
• Protein Serine-Threonine Kinases/metabolism
• Protein Tyrosine Phosphatase, Non-Receptor Type 11/metabolism
• Serine-Threonine Kinase 3
• Signal Transduction
• Stomach/microbiology
• Stomach Neoplasms/microbiology
• Tumor Suppressor Protein p53/metabolism

• IFNβ1
• breast cancer
• chemotherapy
• fibroblasts
• tumour microenvironment

• Breast Neoplasms/drug therapy
• Breast Neoplasms/metabolism
• Breast Neoplasms/pathology
• Cell Proliferation/drug effects
• Cells, Cultured
• Coculture Techniques
• Female
• Fibroblasts/drug effects
• Fibroblasts/metabolism
• Fibroblasts/pathology
• HEK293 Cells
• Humans
• Interferon-beta/metabolism
• Interferon-beta/pharmacology
• MCF-7 Cells
• Neoplasm Recurrence, Local/chemically induced
• Neoplasm Recurrence, Local/etiology
• Neoplasm Recurrence, Local/metabolism
• Paracrine Communication/drug effects
• Paracrine Communication/physiology
• Stromal Cells/drug effects
• Stromal Cells/metabolism
• Stromal Cells/pathology
• Tumor Microenvironment/drug effects

• Gastric Inflammation
• Immune Regulation
• Mucosal Metaplasia
• T Cell

• Animals
• Antibodies/pharmacology
• B7-H1 Antigen/metabolism
• Bone Marrow Cells/drug effects
• Bone Marrow Cells/metabolism
• Bone Marrow Transplantation
• CD11 Antigens/metabolism
• CD8-Positive T-Lymphocytes/drug effects
• CD8-Positive T-Lymphocytes/immunology
• Dendritic Cells/metabolism
• Gastric Mucosa/drug effects
• Gastric Mucosa/pathology
• Gastritis/metabolism
• Gastritis/microbiology
• Gastritis/pathology
• Helicobacter Infections/microbiology
• Helicobacter Infections/pathology
• Helicobacter pylori/drug effects
• Helicobacter pylori/physiology
• Inflammation/pathology
• Male
• Metaplasia
• Mice, Inbred C57BL
• T-Lymphocytes/immunology
• fms-Like Tyrosine Kinase 3/deficiency
• fms-Like Tyrosine Kinase 3/metabolism
• Mice

Plasma membrane integrity is essential for cellular homeostasis. In vivo, cells experience plasma membrane damage from a multitude of stressors in the extra- and intra-cellular environment. To avoid lethal consequences, cells are equipped with repair pathways to restore membrane integrity. Here, we assess plasma membrane damage and repair from a whole-body perspective. We highlight the role of tissue-specific stressors in health and disease and examine membrane repair pathways across diverse cell types. Furthermore, we outline the impact of genetic and environmental factors on plasma membrane integrity and how these contribute to disease pathogenesis in different tissues.

• Cell biology
• Disease
• Lipid peroxidation
• Membrane damage
• Membrane repair
• Plasma membrane
• Pore formation
• Tissue injury
• Vesicle trafficking

The 2,6-di-O-methyl-β-cyclodextrin (dMβCD) is an amphiphilic annular compound consisting of seven dimethyl-glucose molecules. This compound is well known as a solubilizer of lipophilic compounds. Especially, dMβCD extracts cholesterol from the plasma membrane of mammalian cells and releases the cholesterol to the aqueous solution. The experimental use of dMβCD, therefore, serves to investigate the role of cholesterol in the mammalian cell membrane. It is, however, unclear as to how dMβCD extracts cholesterol incorporated into the glycerophospholipid biomembrane. Meanwhile, dMβCD acts as a beneficial compound for Helicobacter pylori and is used as the standard component for supporting the growth of this bacterium in the serum-free culture. However, the detailed mechanism of dMβCD for supporting the growth of H. pylori is still to be clarified. H. pylori is a Gram-negative microaerophilic bacillus recognized as a pathogen concerned with gastrointestinal diseases in human. Previous studies by our group have successfully obtained the H. pylori strains culturable without dMβCD and demonstrated the distinct effects of dMβCD on the interaction between H. pylori and exogenous steroidal compounds. For instance, dMβCD promotes and inhibits the absorption of cholesterol and several steroidal compounds respectively into the biomembranes of H. pylori. In this study we summarized behaviors of dMβCD toward steroidal compounds relevant to H. pylori.

• Cholesterol
• Dimethyl-β-cyclodextrin
• Helicobacter pylor
• Phosphatidylethanolamine
• Steroid hormone

• H. pylori
• Helicobacter pylori
• antibiotic resistance
• antibiotic susceptibility
• cholesterol glucosylation
• cholesteryl glucosides
• drug development
• immune evasion
• lipid raft

• Androgens
• DHEA
• Dehydroepiandrosterone
• Estradiol
• Estrogens
• Gastric cancer
• Testosterone

Steryl glycosides (SGs) are sterols glycosylated at their 3β-hydroxy group. They are widely distributed in plants, algae, and fungi, but are relatively rare in bacteria and animals. Glycosylation of sterols, resulting in important components of the cell membrane SGs, alters their biophysical properties and confers resistance against stress by freezing or heat shock to cells. Besides, many biological functions in animals have been suggested from the observations of SG administration. Recently, cholesteryl glucosides synthesized via the transglycosidation by glucocerebrosidases (GBAs) were found in the central nervous system of animals. Identification of patients with congenital mutations in GBA genes or availability of respective animal models will enable investigation of the function of such endogenously synthesized cholesteryl glycosides by genetic approaches. In addition, mechanisms of the host immune responses against pathogenic bacterial SGs have partially been resolved. This review is focused on the biological functions of SGs in mammals taking into consideration their therapeutic applications in the future.

• NKT cell
• cholesterol
• glycolipid
• immune modulation
• lipid metabolism