The anti-HIV pentameric pseudopeptide HB-19 is preferentially taken up
            <i>in vivo</i>
            by lymphoid organs where it forms a complex with nucleolin

Krust, Bernard; Vienet, Raymond; Cardona, A; Rougeot, Catherine; Jacotot, Étienne; Callebaut, Christian; Guichard, Gilles; Briand, Jean‐Paul; Grognet, J. M.; Edelman, L

doi:10.1073/pnas.221467298

Cited by 16 publications

(19 citation statements)

References 18 publications

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“…This lack of interaction between the cationic HB-19A and the N-terminal part of nucleolin containing long stretches of acidic amino acid residues, and its specific binding to cells independent of expression of anionic proteoglycans, indicates that the binding of HB-19A with nucleolin is not simply a matter of charge. The specific nature of HB-19 interaction with nucleolin has also been demonstrated recently in vivo in rats (33). Indeed, HB-19 was shown to be preferentially taken up in vivo by lymphoid organs where it forms a stable complex with nucleolin.…”

Section: Figmentioning

confidence: 54%

“…The nucleolin-HB-19 complex then becomes internalized at 37°C but not at reduced temperatures (33). Indeed at 20°C, HB-19 remains attached to the cell surface without entering the cytoplasm.…”

Section: Several Componentsmentioning

confidence: 98%

“…Indeed, HB-19 was shown to be preferentially taken up in vivo by lymphoid organs where it forms a stable complex with nucleolin. Thus the molecular target of HB-19 in vivo is once again nucleolin (33).…”

Section: Figmentioning

confidence: 99%

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The Anti-HIV Pentameric Pseudopeptide HB-19 Binds the C-terminal End of Nucleolin and Prevents Anchorage of Virus Particles in the Plasma Membrane of Target Cells

Nisole¹,

Said²,

Mische³

et al. 2002

Journal of Biological Chemistry

101

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Section: Figmentioning

confidence: 54%

Section: Several Componentsmentioning

confidence: 98%

See 1 more Smart Citation

The Anti-HIV Pentameric Pseudopeptide HB-19 Binds the C-terminal End of Nucleolin and Prevents Anchorage of Virus Particles in the Plasma Membrane of Target Cells

Nisole¹,

Said²,

Mische³

et al. 2002

Journal of Biological Chemistry

101

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“…According to the investigation of Krust et al, cell surface-expressed NCL is predominantly found on the cell surface of lymphoid organs, including the liver, spleen, thymus, and bone marrow (66). A significant amount of NCL was also found on the cell surface of developing muscle and growing cells (43,67).…”

Section: Discussionmentioning

confidence: 99%

Cell Surface Nucleolin Facilitates Enterovirus 71 Binding and Infection

Wang

Huang

et al. 2015

J Virol

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Because the pathogenesis of enterovirus 71 (EV71) remains mostly ambiguous, identifying the factors that mediate viral binding and entry to host cells is indispensable to ultimately uncover the mechanisms that underlie virus infection and pathogenesis. Despite the identification of several receptors/attachment molecules for EV71, the binding, entry, and infection mechanisms of EV71 remain unclear. Herein, we employed glycoproteomic approaches to identify human nucleolin as a novel binding receptor for EV71. Glycoproteins purified by lectin chromatography from the membrane extraction of human cells were treated with sialidase, followed by immunoprecipitation with EV71 particles. Among the 16 proteins identified by tandem mass spectrometry analysis, cell surface nucleolin attracted our attention. We found that EV71 interacted directly with nucleolin via the VP1 capsid protein and that an antinucleolin antibody reduced the binding of EV71 to human cells. In addition, the knockdown of cell surface nucleolin decreased EV71 binding, infection, and production in human cells. Furthermore, the expression of human nucleolin on the cell surface of a mouse cell line increased EV71 binding and conferred EV71 infection and production in the cells. These results strongly indicate that human nucleolin can mediate EV71 binding to and infection of cells. Our findings also demonstrate that the use of glycoproteomic approaches is a reliable methodology to discover novel receptors for pathogens. IMPORTANCEOutbreaks of EV71 have been reported in Asia-Pacific countries and have caused thousands of deaths in young children during the last 2 decades. The discovery of new EV71-interacting molecules to understand the infection mechanism has become an emergent issue. Hence, this study uses glycoproteomic approaches to comprehensively investigate the EV71-interacting glycoproteins. Several EV71-interacting glycoproteins are identified, and the role of cell surface nucleolin in mediating the attachment and entry of EV71 is characterized and validated. Our findings not only indicate a novel target for uncovering the EV71 infection mechanism and anti-EV71 drug discovery but also provide a new strategy for virus receptor identification.

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“…The pentameric pseudopeptide HB-19 was found to inhibit HIV infection by binding to the nucleolin and to block the attachment of virus particles to cells. Hence HB-19 represents a potential anti-HIV drug [130,131]. Since nucleoin at the cell surface is also a binding site for a variety of ligands implicated in tumorigenesis and angiogenesis, its potential as an anticancer drug has also been evaluated [131].…”

Section: Peptidementioning

confidence: 99%