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Sweet potato is an important crop, and rich in protein and peptide which have great development potential. Sweet potato protein mainly includes dominant storage protein and small amount glycoprotein, different molecular weight sweet potato peptide can be obtained from protein by enzymatic or chemical hydrolysis. Sweet potato protein and peptide contain 18 types of amino acids that are essential for human body, and its diverse composition of amino acids provides unique nutritional value and its biological activity possess prominent role in the prevention and treatment of cancer, hypertension, obesity and other diseases. Sweet potato is usually used to produce starch, vermicellis and other foods, whereas, huge wastewater was produced during the production process, causing environmental pollution and wastage of protein resource. Therefore, the extraction and application of sweet potato protein from waste water is crucial. Currently, effective extraction and purification methods of sweet potato protein and peptide are commonly used, such as alkaline extraction and acid precipitation, enzymatic digestion, ultrafiltration and so on, but still need optimization and innovation to improve the extraction rate and purity to meet the needs of various fields. Future research can combine modern biotechnology and information technology to study the structure-function relationship, and explore more biological activities and application potentials of sweet potato protein and peptide. The current research status of sweet potato protein and peptide are reviewed in terms of structure composition, physicochemical properties, extraction, purification and biological activity in this paper. This review provides a reliable basis for the industrial production of sweet potato protein and peptide, and promotes the sustainable development of sweet potato protein and peptide. [ABSTRACT FROM AUTHOR]

Sweet potato is an important crop, and rich in protein and peptide which have great development potential. Sweet potato protein mainly includes dominant storage protein and small amount glycoprotein, different molecular weight sweet potato peptide can be obtained from protein by enzymatic or chemical hydrolysis. Sweet potato protein and peptide contain 18 types of amino acids that are essential for human body, and its diverse composition of amino acids provides unique nutritional value and its biological activity possess prominent role in the prevention and treatment of cancer, hypertension, obesity and other diseases. Sweet potato is usually used to produce starch, vermicellis and other foods, whereas, huge wastewater was produced during the production process, causing environmental pollution and wastage of protein resource. Therefore, the extraction and application of sweet potato protein from waste water is crucial. Currently, effective extraction and purification methods of sweet potato protein and peptide are commonly used, such as alkaline extraction and acid precipitation, enzymatic digestion, ultrafiltration and so on, but still need optimization and innovation to improve the extraction rate and purity to meet the needs of various fields. Future research can combine modern biotechnology and information technology to study the structure-function relationship, and explore more biological activities and application potentials of sweet potato protein and peptide. The current research status of sweet potato protein and peptide are reviewed in terms of structure composition, physicochemical properties, extraction, purification and biological activity in this paper. This review provides a reliable basis for the industrial production of sweet potato protein and peptide, and promotes the sustainable development of sweet potato protein and peptide.

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Objective: The study aimed to investigate the effects of Periplaneta americana glycoprotein (PAG) on the growth and metabolites of Lactobacillus plantarum and Bifidobacterium adolescentis. Methods: With inulin as a positive control, the probiotic bacteria were cultured in medium containing different concentrations of PAG (MRS medium with PAG concentrations of 0.5, 1.0, 2.0, and 4.0 mg/mL, respectively. TPY medium with PAG concentrations of 1.0, 2.0, 4.0, and 8.0 mg/mL, respectively) to determine the OD600 and pH, and the contents of lactic acid, short-chain fatty acid (SCFA, snamely acetic acid, propionic acid and butyric acid) in the bacterial solution. Results: The growth of Lactobacillus plantarum was greatest when the concentration of PAG reached 1.0 mg/mL, while Bifidobacterium adolescentis grew best with a PAG concentration of 2.0 mg/mL. The OD600 value, production of lactic acid and SCFAs of Lactobacillus plantarum solution at 1.0 mg/mL PAG were higher than those of inulin, while the pH value was significantly lower. In the bacterial solution of Bifidobacterium adolescentis with 2.0 mg/mL PAG, the values of OD600 and the production of propionic acid and butyric acid increased compared to the same concentration of inulin, the lactic acid production was better than that of inulin at 12 h, the acetic acid production was better than that of inulin at 24 h, and the pH value decreased, indicating that PAG and inulin had different effects on promoting Bifidobacterium adolescentis to produce lactic acid and SCFAs. Conclusion: The PAG could promote the proliferation and organic acid production of Lactobacillus plantarum and Bifidobacterium adolescentis, and the effect was better than that of inulin.

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Objective: This study was conducted to investigate the purification process aimed at obtaining a shiitake glycoprotein with lead eliminating effect, and to explore its preventive and therapeutic efficacy against lead acetate-induced lead toxicity in a rat model. Methods: The crude polysaccharide was extracted from shiitake mushrooms using a hot water extraction method, followed by further purification involving protein removal and chromatography techniques to obtain the bioactive glycoprotein. The molecular characteristics of the glycoprotein were determined through various analytical methods, including infrared spectroscopy analysis, monosaccharide composition analysis, N-terminal amino acid sequencing, and internal amino acid sequence analysis. To evaluate the bioactive potential of shiitake polysaccharide-peptide in addressing lead poisoning in rats, 63 male Sprague-Dawley rats were randomly distributed into nine groups, including a control group, a model group, a positive control group, and shiitake glycoprotein treatment groups at doses of 4, 8 and 160 mg/kg, as well as shiitake fruiting body treatment groups at doses of 4, 12 and 36 g/kg. Lead poisoning was induced in the rats via intraperitoneal injection of lead acetate. The rats were administered polysaccharide-peptide and shiitake fruiting body treatments for a duration of 30 days, with observations made regarding their physical condition. Parameters assessed included body weight, lead content in blood and various organs, as well as biochemical markers in serum. Results: The monosaccharide composition analysis showed that the purified shiitake glycoprotein (LEPP) was composed of glucose, mannose, galactose, glucuronic acid, xylose, fucose, ribose, galacturonic acid, arabinose and rhamnose. The amino acid sequence analysis showed that the N-terminal sequence was MPEQVVVADA, indicating that the shiitake glycoprotein had polysaccharide and protein components. The findings indicated that shiitake glycoprotein effectively promoted weight gain in rats afflicted with lead poisoning. It significantly reduced lead concentrations in both blood and liver, mitigated lead deposition within the liver, enhanced the activities of superoxide dismutase (SOD) and catalase (CAT) in the serum, lowered the levels of malondialdehyde (MDA) （P

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O-linked-N-acetylglucosamine (O-GlcNAc) glycosylation is an abundant and unique post- translational modification by adding N-acetylglucosamine to serine and threonine residues of nuclear and cytoplasmic proteins, which is closely related to various diseases such as cancer, neurodegeneration and diabetes. Identification of the O-GlcNAc modification sites is a prerequisite for exploring their potential regulatory mechanisms in related diseases, as well as a key to clinical diagnosis and targeted intervention. In this paper, we summarize the progresses of diseases associated with aberrant O-GlcNAc modification in recent years, as well as the methods for identifying the relevant modification sites, including antibodies, lectins, chemoenzymatic assays, hydrophilic interaction liquid chromatography, and unnatural carbohydrate metabolism labeling, etc. Furthermore, the strategies of "bump and hole theory" and "spatial activation" have been attracted much attentions recently to targeted label proteins in expected tissues. In addition, multifunctional enzymes theory of "one stone, many birds" and the methods of simultaneous analysis of multiple glycan structures in “one pot” will greatly promote the development of glycoproteomics identification. In conclusion, the development of more effective and specific enrichment approaches for O-GlcNAcylated proteins will be of great significance to elucidate the regulatory mechanism of aberrant glycosylation modifications in related diseases. [ABSTRACT FROM AUTHOR]

Copyright of Journal of South China Agricultural University is the property of Gai Kan Bian Wei Hui and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Objective To screen, identify and verify the immunoreactive epitopes on Hantaan virus glycoprotein C-terminal (HTNV Gc). Methods On the basis of predicting the major histocompatibility complex (MHC) gene in more than 98% of the global population, the affinity of 9-peptide and 15-peptide epitopes on HTNV Gc was systematically analyzed by bioinformatics cutting-edge algorithms such as Immune Epitope Database (IEDB) and Technical University of Denmark (DTU). Their immunogenicity was analyzed by using the Vaxijen tool, and the interspecies intraspecific conservation was analyzed with the Blastp tool. Bidirectional hierarchical clustering was employed to compare the cross-immunoreactivity of MHC-class Ⅰ and class Ⅱ restricted epitopes. Possible results of dominant epitopes docking with MHC were simulated by using molecular docking. Enzyme-linked immunospot (ELISpot) assay was performed to validate the results of computer analyses. Results After integrating the results of various bioinformatics algorithms, we obtained 8 9-peptide epitopes and 80 15-peptide epitopes with high affinity, intraspecific conservation and strong immunogenicity, including 8 human-mouse common dominant epitopes. Cluster analysis showed that H-2 genotype had certain similarity as HLA genotype. The results of molecular docking revealed that dominant epitopes had good docking with various MHC genotypes, which were consistent with the results of affinity analysis. The amount of IFN-γ secreted from the spleen cells was higher in the mice with dominant epitopes than those with non-dominant epitopes. Conclusion With the aids of various bioinformatics algorithms, we successfully screen out the dominant epitopes on HTNV Gc, and validate the cellular immunoreactivity of these epitopes through ELISpot assay.

Copyright of Journal of Food Safety & Quality is the property of Journal of Food Safety & Quality Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

In order to obtain high-quality Auricularia auricula glycoprotein and clarify its monosaccharide and amino acid composition, the process conditions of ultrasonic assisted alkaline extraction of Auricularia auricula glycoprotein were optimized by single factor experiment and response surface methodology, and the glycoprotein was separated and purified by AKTAgo purifier and DEAE GE Healthcare chromatographic column, and its monosaccharide and amino acid composition were analyzed by high performance liquid chromatography (HPLC). The optimum extraction conditions of Auricularia auricula glycoprotein were: ultrasonic time 90 min, material liquid ratio 1:90 g/L, ultrasonic power 200 W, pH8.4, extraction temperature 45 ℃, and the comprehensive score of glycoprotein extraction was 55.93. After separation and purification, the purity of the glycoprotein was 74.1% and the protein recovery rate was 37.5%. The monosaccharide composition of the glycoprotein was mainly glucose (9.95 mg/g) and mannose (5.24 mg/g), and the amino acids were mainly L-aspartic acid/L-asparagine (1.16 mg/g), L-phenylalanine (1.14 mg/g) and L-glutamic acid/L-glutamine (1.10 mg/g). Therefore, the ultrasonic alkali method can effectively improve the extraction efficiency of Auricularia auricula glycoprotein, and the Auricularia auricula glycoprotein contains acidic heteropolysaccharides and the necessary amino acids are complete, which provides a scientific reference for the in-depth research and application development of Auricularia auricula glycoprotein.

The coronavirus disease 2019 (COVID-19) pandemic caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has serious consequences on global public health and social development. The binding of receptor binding domain (RBD) of spike protein to angiotensin converting enzyme 2 (ACE2) on the surface of SARS-CoV-2 host cell initiates the infection progress. Spike and ACE2 are both glycoproteins, the impact of glycosylation on protein structures and protein-protein interactions remains largely elusive. Characterizing the structural and dynamics of protein-protein binding progress will improve mechanism understanding of viral infection and facilitate targeted drug design. Structural mass spectrometry (MS) method is widely used in protein structural studies, providing complementary information to conventional biophysical methods, such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy and cryo-electron microscopy (cryo-EM). Native mass spectrometry (native MS) is an emerging technology that enables the study of intact protein, noncovalent protein-protein, and protein-ligand complexes in their biological state, which can provide structural stability, binding stoichiometry, and spatial arrangement information. Here, native MS was used to examine the interaction between RBD and ACE2 as well as the impact of deglycosylation on the interaction stability of the RBD-ACE2 complex. The results revealed that both RBD and ACE2 are highly glycosylated, ACE2 presents as a dimer while RBD as a monomer, and they form a (RBD-ACE2)2 complex. The conditions of using PNGase F to remove the N-glycan were optimized. At least two O-glycans including NeuAc(2) and GalNAc(1)Gal(1)NeuAc(2) or GlcNAc(1)Gal(1)NeuAc(2) were observed for the N-glycan removed RBD. Furthermore, the stability of the complexes formed by glycosylated and deglycosylated RBD with ACE2 was compared, and the results showed that the removal of N-glycan significantly drops the interaction stability of the RBD-ACE2 complex. Therefore, we -recommend that glycosylation should not be removed for structural and functional studies. Additional glycosylation, structural and dynamics studies on Spike (including separated RBD) and ACE2 complexes would help us to understand the process of viral infection, advance drug design and vaccine developments. Nowadays, a comprehensive MS-based toolbox has been developed for the analysis of protein structure, function, and dynamics, including hydrogen-deuterium exchange MS (HDX-MS), native top-down (nTD) MS, cross-linking MS (XL-MS), and covalent labelling MS (CL-MS), etc. Through integrating structural MS methods, more detailed and comprehensive structural information about glycoproteins and their complexes will be uncovered.

Characterization of protein structures at multiple levels plays an essential role in study on protein functions. Structural analysis at the intact protein or intact complex level allows access of information on aspects including level of post-translational modification (PTM), distribution of variants and stoichiometry of binding. Glycosylation is the most common and complex type of PTM, and most natural and therapeutic proteins are glycoproteins. With the increasing level of glycosylation, the heterogeneity of glycoprotein systems increases, the difference in biochemical properties between glycans and polypeptide chains compromises the accuracy of characterization using conventional tools. Mass spectrometry (MS) measures the mass-to-charge ratios of ionized protein species regardless of such difference, while the native MS strategy allows preservation of non-covalent interactions and direct analysis of intact protein and their complexes. However, the accuracy and even feasibility of native MS measurement of intact glycoprotein species are frequently hindered by signal overlapping caused by the wide mass distribution of the heterogeneous proteoforms, and inconsistency of mass profiles between proteoform populations in different charge states due to their differing ionization responses. Although several approaches based on charge reduction were developed to solve these problems, their applicability is limited by the efficiency of charge resolution or availability of electron-based or proton-based gas-phase reaction modules in commercial models of mass spectrometers. In this work, a tandem MS-based approach was used to characterize the intact size variants of an IgA2 monoclonal antibody (mAb) that incorporated non-covalent subunits. This approach utilized both charge reduction effect and the mass balance rule of the dissociation reactions, and employed collision induced dissociation (CID) or higher energy collisional dissociation (HCD) as the fragmentation reaction. Through parallel measurement of this IgA2 system using limited charge reduction approaches for both ensemble and subpopulations of proteoforms, as well as this tandem MS-based approach and cross-validation, the accuracy provided by these approaches was evaluated. The results suggested that when fragments can be released with high specificity and a defined mass, the tandem-MS based approach can provide sufficient accuracy for both charge and mass determination of heterogeneously glycosylated protein complexes at the intact level. This approach may be used as a universal solution to characterization of a larger variety of heterogeneously glycosylated protein systems.

Glycosylation is one of the most common types of post-translational modifications (PTMs) of proteins, which affects protein properties including conformation, stability and solubility, and plays essential roles in functions including molecular recognition, signaling and immune defense. Characterizing the higher order structures and dynamics of glycoprotein complexes at the intact level is essential for studying the biological functions of glycoproteins. Particularly, accessing structural information such as glycosylation pattern, proteoform distribution, protein interaction, and dynamic conformational evolvement requires direct measurement of intact species. Native mass spectrometry (nMS) allows preservation of non-covalent inter-protein interactions and direct analysis of topology, stoichiometry and dynamic assembly/disassembly at the intact complex level, highly complementing the conventional biophysical techniques. The combination of nMS with travelling-wave ion mobility spectrometry (TWIMS) provides not only an additional orthogonal dimension of separation, but also geometric features of the analytes through collisional cross-section (CCS) determination, thereby facilitating the structural characterization. The macro- and micro-heterogeneity caused by glycosylation, as well as binding with small molecules, induce structural changes of glycoproteins and their complexes on a scale smaller than those resulting from unfolding or macromolecular association/dissociation. However, the benefits of nMS-IMS for characterization of small-scale structural changes or differences of glycoprotein complexes remain to be further demonstrated, in aspects including proteoform-specific structural analysis, distinguishing different binding states of glycoprotein complexes in complex with small molecules, and solution-parameter-induced conformational or stability changes. In this work, aiming at characterizing the stability and small-scale structural differences of glycoprotein complexes, two formats of avidin (tetrameric biotin-binding glycoprotein) that were expressed from different species and exhibit differing carbohydrate contents and proteoform patterns were used as model systems, and the benefits of implementing ion mobility analysis in nMS for structural analysis of both intact complexes and subunits released in the gas-phase were evaluated. It was demonstrated that IMS allows separation of subpopulations of proteoforms, which facilitates not only profiling of proteoform distribution for intact glycoproteins by MS, but also investigation of correlation between glycosylation and CCS. We also demonstrated the power of IMS in measuring the geometric features of the protein complexes in complex with small molecules, and characterizing the extent of conformational changes of glycoproteins under conditions including gas-phase dissociation, supercharging, charge-reduction, and charge-manipulated dissociation. These advantages enable the stability evaluation for glycoprotein complexes.

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The coronavirus disease 2019 (COVID-19) pandemic caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has serious consequences on global public health and social development. The binding of receptor binding domain (RBD) of spike protein to angiotensin converting enzyme 2 (ACE2) on the surface of SARS-CoV-2 host cell initiates the infection progress. Spike and ACE2 are both glycoproteins, the impact of glycosylation on protein structures and protein-protein interactions remains largely elusive. Characterizing the structural and dynamics of protein-protein binding progress will improve mechanism understanding of viral infection and facilitate targeted drug design. Structural mass spectrometry (MS) method is widely used in protein structural studies, providing complementary information to conventional biophysical methods, such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy and cryo-electron microscopy (cryo-EM). Native mass spectrometry (native MS) is an emerging technology that enables the study of intact protein, noncovalent protein-protein, and protein-ligand complexes in their biological state, which can provide structural stability, binding stoichiometry, and spatial arrangement information. Here, native MS was used to examine the interaction between RBD and ACE2 as well as the impact of deglycosylation on the interaction stability of the RBD-ACE2 complex. The results revealed that both RBD and ACE2 are highly glycosylated, ACE2 presents as a dimer while RBD as a monomer, and they form a (RBD-ACE2)2 complex. The conditions of using PNGase F to remove the N-glycan were optimized. At least two O-glycans including NeuAc(2) and GalNAc(1)Gal(1)NeuAc(2) or GlcNAc(1)Gal(1)NeuAc(2) were observed for the N-glycan removed RBD. Furthermore, the stability of the complexes formed by glycosylated and deglycosylated RBD with ACE2 was compared, and the results showed that the removal of N-glycan significantly drops the interaction stability of the RBD-ACE2 complex. Therefore, we -recommend that glycosylation should not be removed for structural and functional studies. Additional glycosylation, structural and dynamics studies on Spike (including separated RBD) and ACE2 complexes would help us to understand the process of viral infection, advance drug design and vaccine developments. Nowadays, a comprehensive MS-based toolbox has been developed for the analysis of protein structure, function, and dynamics, including hydrogen-deuterium exchange MS (HDX-MS), native top-down (nTD) MS, cross-linking MS (XL-MS), and covalent labelling MS (CL-MS), etc. Through integrating structural MS methods, more detailed and comprehensive structural information about glycoproteins and their complexes will be uncovered. [ABSTRACT FROM AUTHOR]

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A capillary column coated with 3-aminophenylboronic acid (APBA)-functionalized gold nanoparticles (AuNPs@APBA) was prepared via electrostatic self-assembly. The coated column exhibited anti-nonspecific adsorption of glycoproteins, enabling selective online enrichment during capillary electrophoresis (CE). First, gold nanoparticles (AuNPs) were synthesized using the sodium citrate reduction method. Then, APBA was self-assembled electrostatically on the surface of the AuNPs to obtain AuNPs@APBA. This nanomaterial was bonded to the inner wall of a capillary through ion adsorption to produce a AuNPs@APBA-coated capillary column. Glycoproteins were adsorbed via bond formation with boric acid groups under alkaline conditions (pH 8) to generate borate esters. Under acidic conditions (pH 3), the borate esters dissociated to release the glycoproteins, thereby achieving the selective online enrichment and separation of glycoproteins. The AuNPs and AuNPs@APBA were characterized using Fourier transform infrared spectroscopy, and their sizes and Zeta potentials were determined. In addition, the electroosmotic flow (EOF) of the AuNPs@APBA-coated capillary column was measured. The results showed that the surface of the AuNPs was successfully modified with APBA and that AuNPs@APBA was adsorbed on the inner wall of the capillary. The peak area of ovalbumin (OVA) on the AuNPs@APBA-coated column was 26.46 times higher than that on a bare column via conventional electrophoresis. In contrast, the peak area of bovine serum albumin (BSA) only increased by 8.47 times, indicating that the AuNPs@APBA coated column selectively enriched glycoproteins. Evaluation of the reproducibility and stability of this method revealed that the AuNPs@APBA coated capillary column could be used continually for 33-67 h. The relative standard deviations (RSDs) of the peak areas for intra-day ( n =5) and inter-day ( n =6) analyses were 2.2% and 3.0%, respectively. The developed method was successfully applied to enrich glycoproteins in a 1×10 6 -fold diluted egg white sample. Glycoproteins were not detected using conventional electrophoresis on the bare column, whereas the AuNPs@APBA-coated capillary column effectively enriched and separated glycoproteins, resulting in a peak area of 10469 mAU·ms. Furthermore, the entire enrichment and separation process was completed within 3 min. This new online enrichment and separation method for glycoproteins has the advantages of low sample consumption, simple operation, and high separation efficiency.

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Copyright of Food & Machinery is the property of Food & Machinery Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Objective To study the application of agglutinin chip to detect the changes in cell surface glycoprotein levels of suspended red blood cells stored in MAP during storage. Methods Partial samples were taken at 1,7,14,21,28, and 35 days after the red blood cells were stored in suspension, and red blood cell membrane proteins were extracted to prepare lectin chips. The fluorescence intensity changes of ACA, PNA, DSA, ECA, EEL, GSL-I-B4, HHL and NPL after binding to corresponding glycoproteins on the surface of red blood cells were detected. Results When suspended red blood cells were stored for 7 days, the fluorescence intensity of PNA and NPL combined with corresponding glycoproteins on the surface of red blood cells was lower than that of 1 day. When suspended red blood cells were stored for 14 days, the fluorescence intensity of ACA, DSA, ECA, GSL-I-B4 and HHL combined with corresponding glycoproteins on the surface of red blood cells was lower than that of 1 day. When suspended red blood cells were stored for 21 days, the fluorescence intensity of EEL combined with corresponding glycoproteins on the surface of red blood cells was lower than that of 1 day. Conclusion During the storage of suspended red blood cells stored with MAP, the glyco-protein level on the surface of the red blood cells will gradually decrease, and most of them will decrease significantly after 21 days of storage. During the preservation process, the level of certain immune-related glycoproteins on the surface of red blood cells is significantly reduced, which may affect its immune function. [ABSTRACT FROM AUTHOR]

BACKGROUND: At present, the research on glucosamine mostly focused on the treatment of knee osteoarthritis, but the research on the effect of glucosamine on cartilage metabolism-related genes in peripheral blood of patients with knee osteoarthritis is limited. OBJECTIVE: To observe the effect of glucosamine capsule on knee osteoarthritis and the expressions of cartilage metabolism-related genes. METHODS: Totally 90 knee osteoarthritis patients admitted to the Zhengzhou Central Hospital Affiliated to Zhengzhou University from March 2017 to February 2019 were selected, and 40 healthy subjects from the medical examination center in the same period were selected as healthy subjects. The cartilage oligomeric matrix protein (COMP), type II collagen fiber α1 gene (COL2A1), glycoprotein and specific tissue inhibitor (TIMP)-3 gene expression levels in peripheral blood mononuclear cells were detected and compared between healthy subjects and knee osteoarthritis patients before treatment. Knee osteoarthritis patients were divided into routine group and study group by random number table, and they were treated with diclofenac sodium sustained-release tablets, diclofenac sodium sustained-release tablets and glucosamine capsules, respectively. Both groups were treated for 12 weeks. The levels of gene expressions and Lequesne index in peripheral blood mononuclear cells of two groups were compared before and after treatment. During the treatment, the occurrence of adverse reactions was counted in the two groups. RESULTS AND CONCLUSION: (1) The relative expressions of COMP and TIMP-3 in peripheral blood mononuclear cells of knee osteoarthritis patients were higher than those of healthy subjects (P < 0.05), while the mRNA relative expressions of COL2A1 and glycoprotein were lower than those of healthy subjects (P < 0.05). (2) There were no significant difference in gene expression levels in peripheral blood mononuclear cells before treatment between study group and routine group (P > 0.05). The mRNA relative expressions of COMP and TIMP-3 in peripheral blood mononuclear cells of the two groups after treatment were lower than those before treatment, and those of the study group were lower than those of the routine group (P < 0.05). The mRNA relative expressions of COL2A1 and glycoprotein in peripheral blood mononuclear cells of the two groups after treatment were higher than those before treatment, and the mRNA relative expressions of COL2A1 and ACAN in the study group were higher than those in the routine group (P < 0.05). (3) There was no significant difference in Lequesne index between the study group and the routine group before treatment (P > 0.05). Lequesne index in both groups after treatment was lower than that before treatment, and that in the study group was lower than that in the routine group (P < 0.05). (4) There was no significant difference in the incidence of adverse reactions between the study group and the routine group (P > 0.05). (5) Results suggest that glucosamine capsule can effectively improve the clinical symptoms of patients with knee osteoarthritis. It is safe and reliable. It may promote the expression of COL2A1 and glycoprotein genes by inhibiting the expression of COMP and TIMP-3 genes. [ABSTRACT FROM AUTHOR]

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Cryptocaryon irritans Brown is an important pathogen related to sea-fish, the study on invasion mech blocker showed great significance. In this paper, c-type lectin LvCTL3 from shrimp Litopenaeus Vanname was cloned and expressed by genet ic engineering methods, and then the recombinant protein was used to agglutination test with Cryptocaryon irritans Broon including Protomont and Theront. The results show that both Protomont and Theront has good aggregation effect with recombinant protein r-LvCTL3, furthermore, the vitality of Theront was restrain obviously. The result mean that rich of glycoprotein molecules, which may be diverse, distribute on the surface of Protomont and Theront, resulted in aggregation effect with r-LvCTL3 . [ABSTRACT FROM AUTHOR]

Salmonella enteritidis (SE) has been recognized as an important zoonotic pathogen, and the prevention and control of salmonellosis has long been a conundrum. However, glycoconjugate vaccines seem to be a promising solution. Glycoproteins are conventionally synthesized by chemical cross-linking which features complex procedure and cost-intensiveness. Therefore, a stable biosynthesis method at lower cost is in urgent need. For the biosynthesis of SE O-antigen-based glycoproteins, we used CRISPR/Cas9 to develop the waaL -deleted SE strain ∆ waaL . The synthesis of lipopolysaccharide (LPS) was detected based on silver staining. Circular polymerase extension cloning (CPEC) was employed to construct the plasmids expressing glycosyltransferase PglL, recombinant Pseudomonas aeruginosa exotoxin A (rEPA), and cholera toxin B subunit (CTB). Meanwhile, PilE S45-K73 glycosylation motif was added to the N-terminal and C-terminal of rEPA and CTB, respectively. The recombinant plasmids were transformed into SE ∆ waaL . After induction, the synthesis of glycoprotein was verified by Western blotting and the synthesized glycoprotein was purified by Ni-NTA column. The results showed that waaL deletion blocked the LPS synthesis of SE, and that rEPA and CTB proteins were expressed in SE ∆ waaL . In addition, obvious glycosylation occurred to rEPA and CTB when PglL was expressed, and the glycosylated part was SE O antigen polysaccharide. In summary, after waaL deletion in SE, PglL can transfer its own O antigen polysaccharides (OPS) to the carrier proteins rEPA and CTB, resulting in OPS-rEPA and OPS-CTB glycoproteins. The result lays a basis for the biosynthesis of SE glycoprotein.

The application of boronic acid affinity chromatography to glycoprotein/glycopeptide enrichment is increasingly maturing. The enrichment selectivity, biocompatibility, and facile operation protocol are key aspects in efficient enrichment methods. In this work, a novel triazo-cyanide boronic acid functionalized material (TCNBA) was prepared using triazo-cyanide click chemistry. The TCNBA was proved to be successfully synthesized through infrared ray (IR) characterization. Subsequently, the glycopeptide/glycoprotein enrichment selectivity of the TCNBA was evaluated. Matrix-assisted laser desorption/ionization time-of-flight mass (MALDI-TOF MS) was employed for the glycopeptide enrichment selectivity evaluation. Taking the digestion of horseradish peroxidase (HRP) and immunoglobulin G (IgG) as samples, 13 and 11 glycopeptides could be characterized with improved signals after TCNBA enrichment, respectively. High abundance non-glycopeptides could be removed effectively from the eluting fraction. This result indicates the high glycopeptide enrichment selectivity of TCNBA. In addition, a mixture of HRP and bovine serum albumin (BSA) enzymatic solution (1:10, amount of substance ratio) was utilized as a sample, and five glycopeptide signals could be identified following enrichment. To evaluate the glycoprotein enrichment selectivity, sodium salt-polyacrylamide gel electrophoresis (SDS-PAGE) was adopted as an evaluation method. Mixtures of HRP, IgG, BSA, and ribonuclease B (RNaseB) proteins were employed as samples, and the results demonstrated that TCNBA had a high glycoprotein enrichment selectivity. The application of TCNBA to the analysis of a real biosample was also evaluated using human plasma. The results indicated the TCNBA could be utilized in large-scale glycoprotein analysis.

Two proteins of similar molecular weight (named as ASPR-C-1 and ASPR-C-2) from the crude drug of Angelica sinensis were purified and characterized by 80% ammonium sulfate precipitation, Sephadex G-50 gel filtration chromatography, and DEAE-Sepharose anion exchange chromatography. The molecular weight of ASPR-C-1 and ASPR-C-2 on SDS-PAGE was 17.33 kDa and 17.18 kDa, respectively. They were mainly monomeric in solution, but partially formed dimers and they were glycoproteins with glycosyl content of 2.6% and 8.2%, respectively. Both ASPR-C-1 and ASPR-C-2 were identified to be members of pathogenesis-related 10 family of proteins by matrix-assisted laser desorption ionization time-of-flight mass spectrometry and have ribonuclease activities with the specific activity of 73.60 U/mg and 146.76 U/mg, respectively. The optimum pH of the two isoforms was similar, at about 5.6, while their optimum temperatures were different. The optimum temperature of ASPR-C-1 was 50 ℃, and that of ASPR-C-2 was 60 ℃. Both isoforms presented highest thermal stability at 60 ℃. However, ASPR-C-2 was more thermotolerant than ASPR-C-1. The latter was rapidly inactivated and retained only about 20% residual activity while the former still maintained about 80% of its original activity at a higher treatment temperature (80 to 100 ℃). In addition, Fe²⁺ had an activating effect on the ribonuclease activities of two isoforms while Ca²⁺, Mg²⁺, Zn²⁺, Mn²⁺, Ag⁺, Cu²⁺, EDTA (Elhylene diamine tetraacetic acid), dithiothreitol and sodium dodecylsulphate showed different degrees of inhibition of the enzyme activities. Our findings provide a foundation for further research on the biological function of PR-10 protein from Angelica sinensis.

Objective: To analyze the genetic characterization of glycoprotein M(gM.),glycoprotein L(gL) of varicella zoster virus. Methods: According to the program of "Ministry of Science and Technology of China" , Based on the 12 suspected VZV patients monitored in Beijing (1 case), Shanghai (5 cases), Jilin (2 cases), Qinghai (1 case), Guangdong (2 case) and Sichuan (case) in 2007-2015. A total of 12 Vesicle fluid and throat swab samples were collected. Positive samples were identified by Agarose gel electrophoresis and two glycoprotein genes were amplified by polymerase chain reaction (PCR). Nucleotide sequences were determined and analyzed by PCR amplification of VZV positive specimens V-OKA-BK of the domestic varicella attenuated live vaccine and the Varilrix-1 of the imported attenuated live vaccine. Nucleotide sequences of VZV positive specimens, vaccine strains (V-OKA-BK, varilrix-1) and GenBank foreign wild strains (41 strains), parent strains (P-oka), vaccine strains (V-oka, Varilrix, Varivax) were compared using BioEdit and MEGA 5.0. Results: 12 specimens were VZV positive. Compared with the vaccine strains and the parent strains, the GM gene of 1 positive specimen had radical mutation at 86686 sites, which resulted in amino acid mutation, 5 positive specimens had base mutation at 87844 sites, and 30 strains of foreign wild strains had the same variation at 87 844 sites. 1 positive specimens of gL gene in 101245 sites had base mutation, and led to amino acid mutation, 6 positive specimens at 101624, 101625, 101626 sites had base of loss and the foreign wild strains in these 3 sites had the same variation. Compared with the vaccine strains, the nucleotide and amino acid homology of gM of 12 VZV positive specimens were 99.2%-100% and 98.2%-100%, respectively, and gL of those were 99.3%-100% and 98.6%-100%, respectively. Compared with 41 strains of foreign wild strains, homology of gM's nucleotides and amino acid were 99.3%-100% and 98.5%-100%, respectively; 99.1%-100% and 98.6%-100% for gL. The results of phylogenetic analysis showed that 7 VZV positive samples were on the same branch with 4 vaccine strains and p-oka strain. Based on gL, 12 VZV positive samples were on the same branch as the vaccine strains and p-oka strain. Conclusion: This study demonstrates that the genes of gM, gL are highly conserved and remain stable immunogen, which may be involved in the attenuation of VZV and need to be further researched.

Dendrobium huoshanense is a rare traditional Chinese medicinal herb, and the anti-tumor activity of its polysaccharides is a research hotspot in traditional Chinese medicine resources domain. This study aims to explore the material basis for the anti-tumor activity of polysaccharide. D. huoshanense was used as raw material in the experiment, and the different protein components were obtained through low salt solution extraction and ammonium sulfate fractional precipitation. Then glycoprotein components were determined by SDS-PAGE electrophoresis staining, and were further isolated and purified by DEAE ion column and Sephadex gel column. At the same time, MTT assay was used in detecting the cytotoxicity of different products on HepG2 cells in vitro. As a result, three kinds of glycoprotein components RG1, RG2, RG3 with relative molecular mass of 22.5, 19.8, 15.6 kDa were gained, and the IC₅₀ of three compounds on human liver cancer cell HepG2 was 534.23 mg•L⁻¹, meanwhile IC₅₀ of single glycoprotein component RG1, RG2 was 432.96, 413.91 mg•L⁻¹ respectively, and glycoprotein component RG3 had no cytotoxicity on HepG2 cells. All in all, the experiment results suggested that two kinds of glycoproteins components with relative molecular mass of 22.5, 19.8 kDa may be one of the material basis for anti-tumor activity of D. huoshanense polysaccharide, and they had a synergistic effect., Competing Interests: The authors of this article and the planning committee members and staff have no relevant financial relationships with commercial interests to disclose., (Copyright© by the Chinese Pharmaceutical Association.)