Prognosis and Treatment Effectiveness of Austrian Syndrome: A Case Report and Systematic Review.

Austrian syndrome is a rare triad of meningitis, pneumonia, and endocarditis caused by . It is associated with high morbidity and mortality rates. Most reports describe pneumonia as the initial illness, followed by multi-organ involvement.

Dual red imaging: a novel endoscopic imaging technology visualizing thick blood vessels in the gastrointestinal wall.

 Dual red imaging (DRI), a novel image-enhanced endoscopy (IEE) technology, has the potential to improve the visibility of blood vessels in deeper tissue using 600 nm and 630 nm wavelength lights in the red band.  To confirm the feasibility of DRI in visualization of vessels in deeper tissue and identify pathologically the features of blood vessels visualized by DRI.  Study 1: visibility of blood vessels was assessed by five observers in 137 pairs of DRI and white light imaging (WLI) images.

Dewaxed Brown Rice Feed Improves Fatty Liver in Obese and Diabetic Model Mice.

Background/aim: Dewaxed brown rice has macrophage activation ability via TLR4 and contains a high amount of lipopolysaccharides (LPS). It is expected that dewaxed brown rice can help prevent lifestyle diseases. In this study, the anti-obesity effect of dewaxed brown rice was investigated using obese and diabetic model mice.

Improvement Effect of Dewaxed Brown Rice on Constipation in Antibiotic-treated Mice.

Background/aim: A decrease in gastrointestinal motility causing weakened lipopolysaccharide (LPS) - toll-like receptor (TLR)4 signaling along with a decline in the number of enteric bacteria is known to be a cause of constipation due to the administration of antibiotics. A new type of brown rice with its wax layer removed, resulting in quick-cooking and tasty product, contains 100-times more LPS than polished white rice. In this study, the improvement effect on constipation due to intake of dewaxed brown rice was examined.

Dewaxed Brown Rice Contains a Significant Amount of Lipopolysaccharide Pointing to Macrophage Activation via TLRs.

Background/aim: Oral ingestion of lipopolysaccharide (LPS) has been shown to be effective in diseases' prevention. Brown rice contains large amounts of LPS not actively consumed because of bad taste. Recently, a new type of brown rice with its wax layer removed has been produced.

Microparticles as Biomarkers of Blood Coagulation in Cancer.

Cancer is associated with hypercoagulopathy and increased risk of thrombosis. This negatively influences patient morbidity and mortality. Cancer is also frequently complicated by the development of venous thromboembolism (VTE).

A novel method for enhancement of peptide vaccination utilizing T-cell epitopes from conventional vaccines.

Peptide vaccines have two fundamental weak points, namely low antigenicity and MHC-restriction. In our previous study, we proposed the design of vaccine peptide to overcome these weakpoints. The vaccine was constructed in the following order, N-terminal, Arg-Gly-Asp (RGD), T-cell epitope peptide, di-lysine linker (KK) to B-cell epitope peptide.

Influence of a fluoride mouthrinse on mutans streptococci in schoolchildren.

This study aimed to determine whether the long-term use of a fluoride mouthrinse affects the salivary levels of mutans streptococci. Two hundred and fifteen schoolchildren (aged 9-10 years) participated. One hundred and forty-nine of these children had used a fluoride mouthrinse since 5 years of age at nursery school, and the remaining 66 children had not.

Production of Fab fragment corresponding to surface protein antigen of Streptococcus mutans serotype c-derived peptide by Escherichia coli and cultured tobacco cells.

The cDNA of a mouse Fab fragment was cloned from a hybridoma cell line that produces a mouse monoclonal antibody, KH5, that reacts with the peptide fragment of the surface protein antigen of Streptococcus mutans serotype c (PAc). After transfection with cDNA, recombinant Fab fragments were produced by Escherichia coli (T15 Fab) and cultured tobacco cells (X253 and X262 Fabs). The antipeptide activities of T15 and X253 were similar to that of KH5.

Amelioration of acute graft-versus-host disease by NKG2A engagement on donor T cells.

Acute graft-versus-host disease (aGVHD) remains a major complication of allogeneic bone marrow transplantation, which is caused by donor T cells specific for host alloantigens. In a murine model, we found that donor T cells expressed a natural killer cell inhibitory receptor, CD94/NKG2A, during the course of aGVHD. Administration of an anti-NKG2A mAb markedly inhibited the expansion of donor T cells and ameliorated the aGVHD pathologies.

An ingenious design for peptide vaccines.

For humoral immunization, it may be possible to make effective and safe peptide vaccines for various diseases by selection of proper B-cell epitopes. However, a lack of T-cell epitopes on short peptides, such as those associated with major histocompatibility complex (MHC)-restriction, is a major problem for peptide vaccine development. We propose a solution for the design of peptide vaccines that involves induction of broadly reactive T-cell epitopes via agretopes.

RGD motif enhances immunogenicity and adjuvanicity of peptide antigens following intranasal immunization.

The use of peptides for various aspects of medical science has been a significant advance. Peptide-based vaccines are promising, but weak immunogenic potency is impeding the clinical application. We have remarkably enhanced the immunogenicity of peptide antigens by addition of motifs that bind to cell attachment proteins, such as arginine-glysine-aspartate (RGD), to the amino acid sequence.

Involvement of leucine residues at positions 107, 112, and 115 in a leucine-rich repeat motif of human Toll-like receptor 2 in the recognition of diacylated lipoproteins and lipopeptides and Staphylococcus aureus peptidoglycans.

S-(2,3-bispalmitoyloxypropyl)Cys-Gly-Asp-Pro-Lys-His-Pro-Lys-Ser-Phe (FSL-1) derived from Mycoplasma salivarium stimulated NF-kappaB reporter activity in human embryonic kidney 293 (HEK293) cells transfected with Toll-like receptor 2 (TLR2) or cotransfected with TLR2 and TLR6, but not in HEK293 cells transfected with TLR6, in a dose-dependent manner. The activity was significantly higher in HEK293 cells transfected with both TLR2 and TLR6 than in HEK293 cells transfected with only TLR2. The deletion mutant TLR2(DeltaS40-I64) (a TLR2 mutant with a deletion of the region of Ser(40) to Ile(64)) failed to activate NF-kappaB in response to FSL-1.

The effect of amino acid spacers on the antigenicity of dimeric peptide--inducing cross-reacting antibodies to a cell surface protein antigen of Streptococcus mutans.

In the course of developing a synthetic peptide vaccine for dental caries, we identified a unique 13-mer peptide named PAc(365-377), TYEAALKQYEADL, as a minimum peptide inducing cross-inhibiting antibodies to a cell surface protein antigen (PAc) of Streptococcus mutans. However, the peptide could hardly induce the production of antibody in the absence of adjuvant. Thus using this peptide as a unit peptide, tandem constructs of dimeric unit peptide with or without spacer amino acid residues were synthesized, and their antigenicities were examined in B10.

The immunogenicity of various peptide antigens inducing cross-reacting antibodies to a cell surface protein antigen of Streptococcus mutans.

A cell surface protein antigen (PAc) of Streptococcus mutans may be involved in the binding of bacteria to the tooth surface, and has long been focused upon as a candidate for a preventive vaccine of dental caries. Previously the peptide PAc (365-377) was shown to raise an antibody in B10.D2 mice which inhibited the binding of salivary components to the PAc molecule.

Inhibitory effect of a self-derived peptide on glucosyltransferase of Streptococcus mutans. Possible novel anticaries measures.

Glucosyltransferase (GTF) plays an important role in the development of dental caries. We examined the possible presence of self-inhibitory segments within the enzyme molecule for the purpose of developing anticaries measures through GTF inhibition. Twenty-two synthetic peptides derived from various regions presumably responsible for insoluble-glucan synthesis were studied with respect to their effects on catalytic activity.

Identification of Streptococcus mutans PAc peptide motif binding with human MHC class II molecules (DRB1*0802, *1101, *1401 and *1405).

A surface protein antigen (PAc) of Streptococcus mutans, in particular the A-region of this PAc molecule, has been noted as a possible target in research for an effective dental caries vaccine. To identify the antigenic peptide binding to major histocompatibility complex (MHC) class II (HLA-DR) molecules in the A-region, we prepared a panel of overlapping synthetic peptides in the second unit of the A-region, and established that a simple enzyme-linked immunosorbent assay (ELISA) binding assay could be achieved by incubating the DR-crude. Binding to DR molecules of these peptides from nine donors was investigated by using the ELISA binding assay.

Identification of core B cell epitope in the synthetic peptide inducing cross-inhibiting antibodies to a surface protein antigen of Streptococcus mutans.

A surface protein antigen (PAc) of Streptococcus mutans, in particular, A-region of the molecule, has been considered as a possible target for the development of an effective anticaries vaccine. This region might be implicated in the induction of dental caries via interaction with salivary components. We have recently specified a unique peptide, TYEAALKQYEADL, as one of the minimum peptides that completely corresponds to the amino acid sequence of a part of the A-region.

Identification of human antigenic epitopes in an alanine-rich repeating region using sera from hu-PBL-SCID mice immunized with a surface protein antigen of Streptococcus mutans.

A 190-kDa surface protein antigen (PAc) of Streptococcus mutans is considered to play an important role in dental caries. To identify antigenic epitopes of the PAc in humans, we immunized severe combined immunodeficient (SCID) mice with recombinant PAc that was transplanted with human peripheral blood mononuclear cells (PBMC). The reactivities of the sera from the immunized hu-PBL-SCID mice to the recombinant PAc and 24 19-mer synthetic peptides covering the alanine-rich repeating region (A-region) presented in the PAc molecule were then examined.

Immunogenicity of peptides coupled with multiple T-cell epitopes of a surface protein antigen of Streptococcus mutans.

A surface protein antigen (PAc) of Streptococcus mutans, in particular the A-region of the molecule, has been noted as a possible target of effective dental caries vaccine. We have previously shown that two peptides of 19 amino acids (residues 361-379, NAKATYEAALKQYEADLAA, and residues 301-319, ANAANEADYQAKLTAYQTE), which correspond to parts of the A-region, contain both T- and B-cell epitopes for the induction of cross-reacting antibodies to the PAc. In this study, for development of an appropriate antigen as a peptide vaccine for use in prophylactic dentistry, we analysed in detail the localization of the T- and B-cell epitopes of PAc(361-379) peptide and the T-cell epitope of PAc(301-319) peptide in B10 congenic mice.

Interaction of lysozyme with a surface protein antigen of Streptococcus mutans.

The interaction of salivary lysozyme with the surface protein antigen (PAc) of Streptococcus mutans and the interaction of lysozyme with the pathogen were examined by ELISA using S. mutans MT8148 (PAc+) and the PAc-defective mutant EM-2 (PAc-). The lysozyme clearly bound to the S.

Identification of a repeated epitope recognized by human serum antibodies in a surface protein antigen of Streptococcus mutans.

This study determined the antigen determinants of a 190-kDa protein antigen of Streptococcus mutans that is involved in the initial attachment to the tooth surface. In 5 subjects, the reactivities of serum antibodies to 7 overlapping surface protein antigen fragments covering the entire antigen molecule and 19 sequential overlapping synthetic 19-mer peptides covering the entire A-region of the surface protein antigen were examined with enzyme-linked immunosorbent assay (ELISA). The study showed that the A-region of the antigen is strongly immunogenic in humans and contains several widely distributed epitopes.