pckA-deficientPorphyromonas gingivalisW83 shows reduction in hemagglutination activity and alteration in the distribution of gingipain activity

2018 ◽  
Vol 126 (5) ◽  
pp. 359-366 ◽  
Author(s):  
Leng Wu ◽  
Lei Zhao ◽  
Jun Wang ◽  
Chengcheng Liu ◽  
Yan Li ◽  
...  
1980 ◽  
Vol 30 (2) ◽  
pp. 506-512
Author(s):  
R Głosnicka ◽  
E Gruszkiewicz

Purification of the envelope antigen of Yersinia pestis EV with passive hemagglutination activity is described. The purification procedure consisted of pancreatin digestion, chromatography on human erythrocyte stroma set on Celite, and rechromatography on Sephadex G-200. Chemical, physical, and biological properties of this antigen were investigated. The results show the lipid-polysaccharide structure of the isolated antigen. The carbohydrate moiety of the galactolipid antigen consists of galactose and fucose. The lipid fraction contained phosphatidylethanolamine and phosphatidylserine. The preparation showed high specificity in the hemagglutination reaction and in Y. pestis phage receptor activity. In two-dimensional immunoelectrophoresis, the isolated pancreatic envelope digest antigen appeared as a single line. Two-dimensional immunoelectrophoresis was modified for tandem separation and was employed to electrophoretically identify the pancreatic envelope digest, trypsin envelope digest preparation, and F1 envelope antigen of Y. pestis. Related or identical antigens showed confluence of peaks with reactions of identity.


2019 ◽  
Vol 2019 ◽  
pp. 1-11
Author(s):  
Peng-peng Sun ◽  
Yuan-yuan Ren ◽  
Jie Zheng ◽  
Ai-jun Hu

Lectin from loach skin mucus plays an important role in pathogen defense. However, hardly can any paper relevant to the character of lectin from loach skin mucus be found in recent years. In this study, a kind of new lectin (LML), with a high hemagglutination activity of 166.23 × 103 HU/mg, was successfully isolated and purified from loach skin mucus. LML was a kind of glycoprotein with a molecular weight of 245 kDa. Also, the monosaccharide composition suggested that its carbohydrate chain was composed of rhamnose, arabinose, xylose, mannose, glucose, and galactose with a molar ratio of 2.02 : 11.66 : 2.06 : 1.00 : 14.09 : 6.00. Besides, LML depended on Ca2+ to induce hemagglutination and was strongly inhibited by D-lactose. The lectin exhibited powerful resistance to alkali and kept about 30% hemagglutination activity at pH 14.0, whereas its capacity of acid resistance was weak. The maximum hemagglutination activity of LML maintained at a temperature range from 20°C to 50°C. Moreover, the structure of LML was preliminarily studied, indicating it contained abundant glutamic acid, histidine, and serine, and its secondary structure contained α-helix (4.97%), β-sheet (27.55%), turns structure (49.78%), and unordered structure (17.70%).


2002 ◽  
Vol 76 (24) ◽  
pp. 12992-13000 ◽  
Author(s):  
Rika Komagome ◽  
Hirofumi Sawa ◽  
Takashi Suzuki ◽  
Yasuo Suzuki ◽  
Shinya Tanaka ◽  
...  

ABSTRACT JC virus (JCV) belongs to the polyomavirus family of double-stranded DNA viruses and in humans causes a demyelinating disease of the central nervous system, progressive multifocal leukoencephalopathy. Its hemagglutination activity and entry into host cells have been reported to depend on an N-linked glycoprotein containing sialic acid. In order to identify the receptors of JCV, we generated virus-like particles (VLP) consisting of major viral capsid protein VP1. We then developed an indirect VLP overlay assay to detect VLP binding to glycoproteins and a panel of glycolipids. We found that VLP bound to sialoglycoproteins, including α1-acid glycoprotein, fetuin, and transferrin receptor, and that this binding depended on α2-3-linked sialic acids and N-linked sugar chains. Neoglycoproteins were synthesized by using ovalbumin and conjugation with oligosaccharides containing the terminal α2-3- or α2-6-linked sialic acid or the branched α2-6-linked sialic acid. We show that the neoglycoprotein containing the terminal α2-6-linked sialic acid had the highest affinity for VLP, inhibited the hemagglutination activity of VLP and JCV, and inhibited the attachment of VLP to cells. We also demonstrate that VLP bound to specific glycolipids, such as lactosylceramide, and gangliosides, including GM3, GD2, GD3, GD1b, GT1b, and GQ1b, and that VLP bound weakly to GD1a but did not bind to GM1a, GM2, or galactocerebroside. Furthermore, the neoglycoprotein containing the terminal α2-6-linked sialic acid and the ganglioside GT1b inhibited JCV infection in the susceptible cell line IMR-32. These results suggest that the oligosaccharides of glycoproteins and glycolipids work as JCV receptors and may be feasible as anti-JCV agents.


2007 ◽  
Vol 72 (12) ◽  
pp. 1271-1274 ◽  
Author(s):  
Ivana Pajic ◽  
Zoran Vujcic ◽  
Miroslava Vujcic ◽  
Irena Novakovic ◽  
Dusan Sladic ◽  
...  

The quinone avarone, isolated from the marine sponge Dysidea avara, possesses the ability to chemically modify proteins. In this work, modification of lectin isolated from the coral Gerardia savaglia by avarone was examined. The techniques used for studying the modification were: SDS PAGE, isoelectric focusing and hemagglutination testing. The results of the SDS PAGE indicate dimerization of the protein. A shift of the pI toward lower value occurs upon modification. The change of the hemagglutination activity of the protein confirms that chemical modification of G. savaglia lectin by avarone changes its ability to interact with the membrane of erythrocytes.


2015 ◽  
Vol 2015 ◽  
pp. 1-6 ◽  
Author(s):  
Jefferson Muniz de Lima ◽  
Ronaldo Rodrigues Sarmento ◽  
Joelma Rodrigues de Souza ◽  
Fábio André Brayner ◽  
Ana Paula Sampaio Feitosa ◽  
...  

Chitosan is a polysaccharide composed of randomly distributed chains ofβ-(1-4) D-glucosamine and N-acetyl-D-glucosamine. This compound is obtained by partial or total deacetylation of chitin in acidic solution. The chitosan-based hemostatic agents have been gaining much attention in the management of bleeding. The aim of this study was to evaluate in vitro hemagglutination activity of chitosan nanoparticles using human erythrocytes. The preparation of nanoparticles was achieved by ionotropic gelification technique followed by neutralization with NaOH 1 mol/L−1. The hemagglutination activity was performed on a solution of 2% erythrocytes (pH 7.4 on PBS) collected from five healthy volunteers. The hemolysis determination was made by spectrophotometric analysis. Chitosan nanoparticle solutions without NaOH addition changed the reddish colour of the wells into brown, suggesting an oxidative reaction of hemoglobin and possible cell lysis. All neutralized solutions of chitosan nanoparticles presented positive haemagglutination, without any change in reaction color. Chitosan nanoparticles presented hemolytic activity ranging from 186.20 to 223.12%, while neutralized solutions ranged from 2.56 to 72.54%, comparing to distilled water. Results highlight the need for development of new routes of synthesis of chitosan nanoparticles within human physiologic pH.


2015 ◽  
Vol 30 (3) ◽  
pp. 228-234 ◽  
Author(s):  
So Fujiyoshi ◽  
Hiroaki Tateno ◽  
Tomoo Watsuji ◽  
Hideyuki Yamaguchi ◽  
Daisuke Fukushima ◽  
...  

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