Glycan structures of the structural subunit (HtH1) of Haliotis tuberculata hemocyanin

Velkova, Lyudmila; Dolashka, Pavlina; Lieb, Bernhard; Dolashki, Aleksander; Voelter, Wolfgang; Beeumen, Jozef Van; Devreese, Bart

doi:10.1007/s10719-011-9337-2

Cited by 23 publications

(26 citation statements)

References 44 publications

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“…An ␣-galactoside was specifically recognized by MytiLec in FACT analysis, although the occurrence of these sugars in mussels is not yet clear. Certain Gal-containing oligosaccharides in glycoproteins have been recently found in some mollusks by mass spectrometric analysis (55)(56)(57). MytiLec was obtained together with the haptenic saccharide Gal and therefore bound to mussel tissues.…”

Section: Discussionmentioning

confidence: 99%

A Lectin from the Mussel Mytilus galloprovincialis Has a Highly Novel Primary Structure and Induces Glycan-mediated Cytotoxicity of Globotriaosylceramide-expressing Lymphoma Cells

Fujii

Dohmae

Takio

et al. 2012

Journal of Biological Chemistry

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Background: Studies on the diversity of carbohydrate-binding proteins (lectins) are important in glycobiology. Results: A lectin having a novel primary structure was isolated from a mussel and found to have a globotriose-dependent cytotoxicity on Burkitt lymphoma cells. Conclusion: A new primary structure quite distinct from known lectin is described. Significance: Discovery of similar lectin structures from vertebrates will lead to progress in medical sciences.

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Section: Discussionmentioning

confidence: 99%

A Lectin from the Mussel Mytilus galloprovincialis Has a Highly Novel Primary Structure and Induces Glycan-mediated Cytotoxicity of Globotriaosylceramide-expressing Lymphoma Cells

Fujii

Dohmae

Takio

et al. 2012

Journal of Biological Chemistry

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“…FLH is composed of a single type of subunit that forms homodidecamers (8). Another significant feature of the hemocyanin structure is the presence of carbohydrates, as heterogeneous N-and O-glycosylation ramifications, with mannose being the common and most abundant oligosaccharide (25)(26)(27)(28)(29)(30). Although the three hemocyanins present N-and O-linked oligosaccharides, there are differences in their arrangements.…”

mentioning

confidence: 99%

Hemocyanins Stimulate Innate Immunity by Inducing Different Temporal Patterns of Proinflammatory Cytokine Expression in Macrophages

Zhong

Arancibia

Born

et al. 2016

The Journal of Immunology

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Hemocyanins induce a potent Th1-dominant immune response with beneficial clinical outcomes when used as a carrier/adjuvant in vaccines and nonspecific immunostimulant in cancer. However, the mechanisms by which hemocyanins trigger innate immune responses, leading to beneficial adaptive immune responses, are unknown. This response is triggered by a proinflammatory signal from various components, of which macrophages are an essential part. To understand how these proteins influence macrophage response, we investigated the effects of mollusks hemocyanins with varying structural and immunological properties, including hemocyanins from Concholepas concholepas, Fissurella latimarginata, and Megathura crenulata (keyhole limpet hemocyanin), on cultures of peritoneal macrophages. Hemocyanins were phagocytosed and slowly processed. Analysis of this process showed differential gene expression along with protein levels of proinflammatory markers, including IL-1β, IL-6, IL-12p40, and TNF-α. An extended expression analysis of 84 cytokines during a 24-h period showed a robust proinflammatory response for F. latimarginata hemocyanin in comparison with keyhole limpet hemocyanin and C. concholepas hemocyanin, which was characterized by an increase in the transcript levels of M1 cytokines involved in leukocyte recruitment. These cytokine genes included chemokines (Cxcl1, Cxcl3, Cxcl5, Ccl2, and Ccl3), ILs (Il1b and Ifng), growth factors (Csf2 and Csf3), and TNF family members (Cd40lg). The protein levels of certain cytokines were increased. However, every hemocyanin maintains downregulated key M2 cytokine genes, including Il4 and Il5. Collectively, our data demonstrate that hemocyanins are able to trigger the release of proinflammatory factors with different patterns of cytokine expression, suggesting differential signaling pathways and transcriptional network mechanisms that lead to the activation of M1-polarized macrophages.

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“…It is known that hemocyanins are glycosylated (20,44,45), and some of the important features of hemocyanins in clinical applications such as immunogenicity and antigenicity are related to their high carbohydrate content and unusual glycans (46)(47)(48). Furthermore, Dolashka-Angelova et al (20) demonstrated that one functional unit (50 kDa; the building blocks of hemocyanin) of Rapana thomasiana hemocyanin that was natively devoid of glycans lacked antiviral activity against poliovirus type 1.…”

Section: Discussionmentioning

confidence: 99%

Abalone Hemocyanin Blocks the Entry of Herpes Simplex Virus 1 into Cells: a Potential New Antiviral Strategy

Zanjani

Miranda-Saksena

Valtchev

et al. 2016

Antimicrob Agents Chemother

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A marine-derived compound, abalone hemocyanin, from Haliotis rubra was shown to have a unique mechanism of antiviral activity against herpes simplex virus 1 (HSV-1) infections. In vitro assays demonstrated the dose-dependent and inhibitory effect of purified hemocyanin against HSV-1 infection in Vero cells with a 50% effective dose (ED 50 ) of 40 to 50 nM and no significant toxicity. In addition, hemocyanin specifically inhibited viral attachment and entry by binding selectively to the viral surface glycoproteins gD, gB, and gC, probably by mimicking their receptors. However, hemocyanin had no effect on postentry events and did not block infection by binding to cellular receptors for HSV. By the use of different mutants of gD and gB and a competitive heparin binding assay, both protein charge and conformation were shown to be the driving forces of the interaction between hemocyanin and viral glycoproteins. These findings also suggested that hemocyanin may have different motifs for binding to each of the viral glycoproteins B and D. The dimer subunit of hemocyanin with a 10-fold-smaller molecular mass exhibited similar binding to viral surface glycoproteins, showing that the observed inhibition did not require the entire multimer. Therefore, a small hemocyanin analogue could serve as a new antiviral candidate for HSV infections.T he predominant antiviral therapies for herpes simplex virus (HSV) infections are nucleoside analogue inhibitors, such as acyclovir, its prodrug valacyclovir, famciclovir (a prodrug of penciclovir), and the second line of drugs for resistant virus, foscarnet and cidofovir. These drugs are all inhibitors of viral DNA polymerase (1). The variety is limited despite the fact that HSV has more than 80 genes that are required for its functionality and, therefore, could potentially be targeted by multiple types of inhibitors (2). Thus, improving the efficacy of current HSV treatment relies on the discovery of new antiviral compounds targeting various functions of the virus, preferably earlier stages of the HSV viral life cycle such as viral attachment and entry. Viral attachment and entry are regulated by surface glycoproteins gC, gB, gD, and gH-gL (3, 4). Attachment is a two-step process involving the primary interaction of gC and/or gB with heparan sulfate proteoglycans (HSPG), followed by the secondary gD-mediated binding to its receptors, such as herpesvirus entry mediator (HVEM), nectin-1, or 3-O-sulfated heparan sulfate. This interaction triggers the activation of gH-gL and gB, which leads to the fusion of viral envelope and plasma membrane of the host cell either at the surface or in the endosomes (3, 4). Many steps in the entry process of HSV remain unclear; however, it is known that gD determines HSV tropism and that the conformational changes in gD upon binding to its receptors are critical in triggering an activation cascade (5, 6).Viral attachment or entry could be inhibited by mimicking cellular receptors that are involved in these events. For example, heparin interacts with HSPG bi...

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Glycan structures of the structural subunit (HtH1) of Haliotis tuberculata hemocyanin

Cited by 23 publications

References 44 publications

A Lectin from the Mussel Mytilus galloprovincialis Has a Highly Novel Primary Structure and Induces Glycan-mediated Cytotoxicity of Globotriaosylceramide-expressing Lymphoma Cells

A Lectin from the Mussel Mytilus galloprovincialis Has a Highly Novel Primary Structure and Induces Glycan-mediated Cytotoxicity of Globotriaosylceramide-expressing Lymphoma Cells

Hemocyanins Stimulate Innate Immunity by Inducing Different Temporal Patterns of Proinflammatory Cytokine Expression in Macrophages

Abalone Hemocyanin Blocks the Entry of Herpes Simplex Virus 1 into Cells: a Potential New Antiviral Strategy

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