Neuraminidase (NA), which is expressed on the membrane surface of an influenza virus, plays a critical role in the growth of a virus exhibiting sialidase activity, and this activity is a target for therapeutic drugs. The authors have developed a novel substrate, BTP3-Neu5Ac, that is capable of fluorescence imaging of sialidase activity and have developed a method for detection of influenza virus by fluorescence imaging of sialidase activity. The method has been applied to the detection and isolation of a drug-resistant influenza virus. Water-soluble BTP3-Neu5Ac undergoes hydrolysis by sialidase resulting in the liberation of sialic acid and generation of free BTP3. BTP3 is deposited and enabling fluorescence imaging of sialidase activity. Fluorescence imaging of the sialidase activity of influenza virus NA enables convenient and rapid detection of viruses and infected cells. A drug-resistant influenza virus, which has become a problem in recent years, is a virus that has acquired by mutation resistance to a sialidase inhibitor and retains its activity even in the presence of a sialidase inhibitor. The authors have therefore developed a method for selective detection of a drug-resistant influenza virus. BTP3-Neu5Ac for detection and isolation of a drug-resistant influenza virus is expected to be widely used in the future as a useful tool in basic research, hygiene and clinical fields.

Glycosaminoglycans (GAGs), including chondroitin sulfate, dermatan sulfate, heparan sulfate, heparin, and hyaluronan, are important for various biological processes including construction of the extracellular matrix, tissue development, and cell signaling through interaction with extracellular matrix components, morphogens, and growth factors. GAGs are synthesized by various glycosyltransferases and sulfotransferases using donor substrates including uridine diphosphate (UDP)-sugars and 3′-phosphoadenosine 5′-phosphosulfate, respectively. GAGs as well as UDP and adenosine-3′, 5′-bisphosphate, which are reaction products, are mainly catabolized in lysosomes and the Golgi apparatus. Disturbances in the anabolism and catabolism of GAGs cause human genetic diseases such as connective tissue disorders and mucopolysaccharidoses, respectively. Furthermore, disturbances of catabolism of UDP and adenosine-3′, 5′-bisphosphate also cause Desbuquois dysplasia type 1 and chondrodysplasia with joint dislocations, respectively. Effective therapy for genetic disorders caused by defects in the biosynthesis of GAGs has not been established. This review provides an overview of the growing number of glycobiological studies on characterized genetic disorders caused by faults in the anabolism of GAGs.

Aberrant glycosylation, in abundance or type, influences the overall physiology of tissues and the functions of proteins. This review is focused on the role of glycosylation in the reproductive process in the female reproductive tract from a glycoprotein perspective. Many biological events are essential to allow for sperm-egg fertilisation in oviduct and subsequent blastocyst implantation in a receptive uterus during the window of implantation, including adhesion and proliferation. The process of blastocyst implantation is managed by a series of orchestrated events among several glycoproteins found on the surface of oviduct and uterine tissues. A change in the molecular surface of the oviduct and uterine tissues, such as the glycosylation of its membrane proteins, would affect the blastocyst journey through the female reproductive tract. In particular, the glycosylation presented by the mucins on the surface of the oviduct and uterus in diabetes, that is associated with reduced embryo implantation rates, is highlighted since these heavily glycosylated proteins have been shown to play an important role in blastocyst implantation. An understanding of the glycosylation changes to the surface of the oviduct and uterus has potential for the development of a test for uterine receptivity and may provide the next leap forward for the treatment of infertility.

In this review, we show novel methods for utilizing plant biomass, polysaccharides, and lignin. Firstly, the simultaneous enzymatic saccharification and comminution (SESC) of plant materials is described as an extraction method for polysaccharides and lignin that does not require toxic reagents or organic solvents. Secondly, we demonstrate the utilization of saccharides and lignin extracted by SESC, such as for sugar and ethanol synthesis, and as antioxidant, spin trap reagent, heatproof filler, shape memory polymer, and UV protection film. Thirdly, a possibility of SESC in relative to previous utilization technique of plant biomass was presented.

Neuraminidase (NA), which is expressed on the membrane surface of an influenza virus, plays a critical role in the growth of a virus exhibiting sialidase activity, and this activity is a target for therapeutic drugs. The authors have developed a novel substrate, BTP3-Neu5Ac, that is capable of fluorescence imaging of sialidase activity and have developed a method for detection of influenza virus by fluorescence imaging of sialidase activity. The method has been applied to the detection and isolation of a drug-resistant influenza virus. Water-soluble BTP3-Neu5Ac undergoes hydrolysis by sialidase resulting in the liberation of sialic acid and generation of free BTP3. BTP3 is deposited and enabling fluorescence imaging of sialidase activity. Fluorescence imaging of the sialidase activity of influenza virus NA enables convenient and rapid detection of viruses and infected cells. A drug-resistant influenza virus, which has become a problem in recent years, is a virus that has acquired by mutation resistance to a sialidase inhibitor and retains its activity even in the presence of a sialidase inhibitor. The authors have therefore developed a method for selective detection of a drug-resistant influenza virus. BTP3-Neu5Ac for detection and isolation of a drug-resistant influenza virus is expected to be widely used in the future as a useful tool in basic research, hygiene and clinical fields.

Glycosaminoglycans (GAGs), including chondroitin sulfate, dermatan sulfate, heparan sulfate, heparin, and hyaluronan, are important for various biological processes including construction of the extracellular matrix, tissue development, and cell signaling through interaction with extracellular matrix components, morphogens, and growth factors. GAGs are synthesized by various glycosyltransferases and sulfotransferases using donor substrates including uridine diphosphate (UDP)-sugars and 3′-phosphoadenosine 5′-phosphosulfate, respectively. GAGs as well as UDP and adenosine-3′, 5′-bisphosphate, which are reaction products, are mainly catabolized in lysosomes and the Golgi apparatus. Disturbances in the anabolism and catabolism of GAGs cause human genetic diseases such as connective tissue disorders and mucopolysaccharidoses, respectively. Furthermore, disturbances of catabolism of UDP and adenosine-3′, 5′-bisphosphate also cause Desbuquois dysplasia type 1 and chondrodysplasia with joint dislocations, respectively. Effective therapy for genetic disorders caused by defects in the biosynthesis of GAGs has not been established. This review provides an overview of the growing number of glycobiological studies on characterized genetic disorders caused by faults in the anabolism of GAGs.

In this review, we show novel methods for utilizing plant biomass, polysaccharides, and lignin. Firstly, the simultaneous enzymatic saccharification and comminution (SESC) of plant materials is described as an extraction method for polysaccharides and lignin that does not require toxic reagents or organic solvents. Secondly, we demonstrate the utilization of saccharides and lignin extracted by SESC, such as for sugar and ethanol synthesis, and as antioxidant, spin trap reagent, heatproof filler, shape memory polymer, and UV protection film. Thirdly, a possibility of SESC in relative to previous utilization technique of plant biomass was presented.