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Страница 1 от 81 полученные результаты
Relapsing fever Borrelia binds to neolacto glycans and mediates rosetting of human erythrocytes.
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A hallmark of acute relapsing fever borreliosis is severe bacteremia. Some Borrelia species, such as B. duttonii and B. crocidurae, associate with erythrocytes and induce aggregation recognized as erythrocyte rosetting. Erythrocyte rosettes contribute to disease severity by increased tissue
N-Glycans on the Rift Valley Fever Virus Envelope Glycoproteins Gn and Gc Redundantly Support Viral Infection via DC-SIGN.
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Rift Valley fever is a mosquito-transmitted, zoonotic disease that infects humans and ruminants. Dendritic cell specific intercellular adhesion molecule 3 (ICAM-3) grabbing non-integrin (DC-SIGN) acts as a receptor for members of the phlebovirus genus. The Rift Valley fever virus (RVFV)
Structural and functional characterization of the glycan antigens involved in immunobiology of Q fever.
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Coxiella burnetii is the causative agent of Q fever. The bacterium is extremely infectious and is classified as a category biological weapon. A lipopolysaccharide I (LPS I) belongs to the main components of the C. burnetii outer membrane and its structure-function relationship studies are of
Small molecule inhibitors of ER α-glucosidases are active against multiple hemorrhagic fever viruses.
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Host cellular endoplasmic reticulum α-glucosidases I and II are essential for the maturation of viral glycosylated envelope proteins that use the calnexin mediated folding pathway. Inhibition of these glycan processing enzymes leads to the misfolding and degradation of these viral glycoproteins and
Removal of a N-linked glycosylation site of classical swine fever virus strain Brescia Erns glycoprotein affects virulence in swine.
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E(rns) glycoprotein, along with E(1) and E(2), is one of the three envelope glycoproteins of classical swine fever virus (CSFV). E(rns) is a heavily glycosylated protein involved in several functions, including virus attachment and entry to target cells, production of neutralizing antibodies, and
N-linked glycosylation of Gn (but not Gc) is important for Crimean Congo hemorrhagic fever virus glycoprotein localization and transport.
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The mature Gn glycoprotein of Crimean Congo hemorrhagic fever (CCHF) virus contains two predicted glycosylation sites (557N and 755N). Of these, N-glycans are added only at 557N, as evidenced by abrogation of Gn-glycosylation by mutation of 557N but not 755N site. Mutational block of
Glycosylation of classical swine fever virus E(rns) is essential for binding double-stranded RNA and preventing interferon-beta induction.
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Host cells sense double-stranded RNA (dsRNA) produced during viral replication and initiate type I interferon (IFN-alpha/beta) production, leading to subsequent antiviral responses. Many viruses, including classical swine fever virus (CSFV), have developed strategies for counteracting the
The N-glycosylation of classical swine fever virus E2 glycoprotein extracellular domain expressed in the milk of goat.
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Classical swine fever virus (CSFV) outer surface E2 glycoprotein represents an important target to induce protective immunization during infection but the influence of N-glycosylation pattern in antigenicity is yet unclear. In the present work, the N-glycosylation of the E2-CSFV extracellular domain
Abnormal IgD and IgA1 O-glycosylation in hyperimmunoglobulinaemia D and periodic fever syndrome.
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In order to determine the glycosylation pattern for IgD, and to examine whether there are changes in the pattern of IgD and IgA1 O-glycosylation in patients with hyperimmunoglobulinaemia D and periodic fever syndrome (HIDS) during acute febrile attacks and during periods of quiescence, serum was
Characterization of the cellular receptors for the South American hemorrhagic fever viruses Junin, Guanarito, and Machupo.
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The New World arenaviruses Junin, Machupo, and Guanarito are the causative agents of hemorrhagic fevers (HF) with high mortality in humans. The cellular receptor for Old World arenaviruses and one subgroup of the New World arenaviruses (Clade C) have been identified as alpha-dystroglycan (alpha-DG).
Recent progress in glycomics and proteomics of the Q fever bacterium Coxiella burnetii.
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Coxiella burnetii is an intracellular, Gram-negative bacterium and causative agent of Q fever. In humans, the disease ranges mostly from a flu-like illness and self-recovering mild pneumonia to severe meningoencephalitis, myocarditis or endocarditis. Recent molecular and biochemical/immunological
Elevated serum level and altered glycosylation of alpha 1-acid glycoprotein in hyperimmunoglobulinemia D and periodic fever syndrome: evidence for persistent inflammation.
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Crossed affinoimmunoelectrophoresis using concanavalin A and Aleuria aurantia lectin as diantennary glycan- and fucose-specific affinocomponents, respectively, was applied to study changes in the concentration and glycosylation of the acute phase protein alpha 1-acid glycoprotein (AGP) in sera
Specific glycosylation of alpha(1)-acid glycoprotein characterises patients with familial Mediterranean fever and obligatory carriers of MEFV.
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BACKGROUND
Familial Mediterranean fever (FMF) is a periodic febrile disorder, characterised by fever and serositis. The acute phase response during attacks of FMF results from the release of cytokines, which in turn induce increased expression and changed glycosylation of acute phase proteins. A
Characterization of yellow fever virus proteins E and NS1 expressed in Vero and Spodoptera frugiperda cells.
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The cDNA encoding the E and NS1 proteins of the yellow fever virus (YFV) was expressed in Spodoptera frugiperda cells via the recombinant baculovirus Ac-E. NS1 as a gp100 precursor which was cleaved to generate the recombinant proteins E and NS1 similar in size, folding and antigenicity to the
Glycans with Antiviral Activity from Marine Organisms.
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There remains today a critical need for new antiviral agents, particularly in view of the alarming increase in drug resistance and associated issues. The marine environment has been a prolific contributor towards the identification of novel therapeutic agents in the recent few decades. Added to
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