Mediation of human immunodeficiency virus type 1 binding by interaction of cell surface heparan sulfate proteoglycans with the V3 region of envelope gp120-gp41

Roderiquez, Gregory; Oravecz, Tamás; Yanagishita, Masaki; Bou-Habib, Dumith Chequer; Mostowski, Howard; Norcross, Michael A.

doi:10.1128/jvi.69.4.2233-2239.1995

Cited by 227 publications

(111 citation statements)

References 43 publications

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“…In addition, heparan sulphate binding on the human immunodeficiency virus type 1 (HIV-1) envelope also involves two regions, V3 and C4, of glycoprotein 120 (gp120). Soluble heparan sulphate inhibited binding of monoclonal antibodies that recognize the V3 and C4 domains of gp120 (Roderiquez et al, 1995). The V3 and C4 domains are positively charged regions of gp120 and may be juxtaposed in the native gp120 protein (Callahan et al, 1991) to form a single heparin binding site.…”

Section: Discussionmentioning

confidence: 99%

Proteoglycan receptor binding by Neisseria gonorrhoeae MS11 is determined by the HV‐1 region of OpaA

Grant

Bos

Belland

1999

Molecular Microbiology

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SummaryThe interaction of the OpaA protein of Neisseria gonorrhoeae MS11mk with heparan sulphate-containing proteoglycan receptors on Chang conjunctiva epithelial cells was examined using isolated receptor binding and cell adherence/internalization assays. OpaA deletion proteins, in which the four surface-exposed regions of the protein were deleted individually, and chimeric OpaA/B proteins, in which the surface-exposed regions of the OpaA and OpaB proteins were exchanged, were expressed in N. gonorrhoeae. The recombinant deletion proteins and the chimeric OpaA/B proteins were surface exposed in the outer membrane of N. gonorrhoeae.

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Section: Discussionmentioning

confidence: 99%

Proteoglycan receptor binding by Neisseria gonorrhoeae MS11 is determined by the HV‐1 region of OpaA

Grant

Bos

Belland

1999

Molecular Microbiology

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“…The interaction between the Dengue virus (a positive singlestranded RNA virus of the Flavivirus genus) envelope proteins could be antagonised by competing HP with a minimum chain length of a decasaccharide. This interaction could be Germi et al (2002), Barth et al (2003Barth et al ( , 2006 and Kalia et al (2009) Human immunodeficiency virus (HIV) AIDS HS Patel et al (1993) and Roderiquez et al (1995) Herpes simplex virus ( antagonised by a highly sulphated form of HS (derived from liver) while HS (derived from testis) with lower sulphation showed much lower potency (Chen et al, 1997). In a recent publication, CSE showed antiviral activity as an entry inhibitor, targeting envelope (E) protein located on the lipid bilayer envelope of the virus in all four serotypes of Dengue virus (Kato et al, 2010).…”

Section: (2) Virusesmentioning

confidence: 99%

Glycosaminoglycans in infectious disease

et al. 2013

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Glycosaminoglycans (GAGs) are complex carbohydrates that are ubiquitously present on the cell surface and in the extracellular matrix. Interactions between GAGs and pathogens represent the first line of contact between pathogen and host cell and are crucial to a pathogen's invasive potential. Their complexity and structural diversity allow GAGs to control a wide array of biological interactions influencing many physiological and pathological processes, including adhesion, cell-to-cell communication, biochemical cascades, and the immune response. In recent years, increasing evidence indicates an extraordinary role for GAGs in the pathogenesis of viruses, bacteria and parasites. Herein, we examine the interface between GAGs and different pathogens, and address the divergent biological functions of GAGs in infectious disease. We consider approaches to use this understanding to design novel therapeutic strategies addressing new challenges in the treatment of infectious diseases.

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“…A cross-section towards the middle of cells for each staining with the merge of the two colors in yellow are presented. [6,48,49], and on the other hand by the surfaceexpressed nucleolin [4,5]. Consequently, HIV attachment could be inhibited either by FGF-2 which uses heparan-sulfate proteoglycans as low affinity receptors [45], and by various specific ligands of nucleolin such as the HB-19 pseudopeptide, midkine, PTN, and lactoferrin [4,5,8,9,35].…”

Section: Mergementioning

confidence: 99%

Pleiotrophin inhibits HIV infection by binding the cell surface‐expressed nucleolin

Said

Courty²,

Svab

et al. 2005

The FEBS Journal

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The human immunodeficiency virus (HIV) infects target cells by the capacity of its envelope glycoproteins gp120-gp41 to attach cells and induce the fusion of virus to cell membranes, a process which leads to virus entry. The receptor complex essential for HIV entry consists of the CD4 molecule and at least one of the members of the chemokine receptor family: CCR5 or CXCR4 [1,2]. Contrary to the virus entry process, the attachment of HIV particles to cells can occur even independently of CD4. We have previously demonstrated that HIV attachment is inhibited by the pseudopeptide HB-19 that binds specifically the C-terminal tail of nucleolin, a cell-surface-expressed protein identified to be implicated in HIV attachment [3][4][5]. Consequently, we have suggested that HIV attachment is achieved by the coordination of at least two events implicating on the one hand heparan sulfate proteoglycans [6,7] and on the other hand the cell surfaceexpressed nucleolin [4]. In the search for natural ligands of nucleolin that exhibit a potential inhibitory activity against HIV infection, other than midkine [8] and lactoferrin [9], here we show that pleiotrophin The growth factor pleiotrophin (PTN) has been reported to bind heparan sulfate and nucleolin, two components of the cell surface implicated in the attachment of HIV-1 particles to cells. Here we show that PTN inhibits HIV-1 infection by its capacity to inhibit HIV-1 particle attachment to the surface of permissive cells. The b-sheet domains of PTN appear to be implicated in this inhibitory effect on the HIV infection, in particular the domain containing amino acids 60-110. PTN binding to the cell surface is mediated by high and low affinity binding sites. Other inhibitors of HIV attachment known to bind specifically surface expressed nucleolin, such as the pseudopeptide HB-19 and the cytokine midkine prevent the binding of PTN to its low affinity-binding site. Confocal immunofluorescence laser microscopy revealed that the cross-linking of surface-bound PTN with a specific antibody results in the clustering of cell surface-expressed nucleolin and the colocalization of both PTN and nucleolin signals. Following its binding to surface-nucleolin, PTN is internalized by a temperature sensitive mechanism, a process which is inhibited by HB-19 and is independent of heparan and chondroitin sulfate proteoglycans. Nevertheless, proteoglycans might play a role in the concentration of PTN on the cell surface for a more efficient interaction with nucleolin. Our results demonstrate for the first time that PTN inhibits HIV infection and suggest that the cell surfaceexpressed nucleolin is a low affinity receptor for PTN binding to cells and it is also implicated in PTN entry into cells by an active process.Abbreviations ALK, anaplastic lymphoma kinase; AZT, azidothymidine; CHO, Chinese hamster ovary; HARP, heparin affin regulatory peptide; HB-GAM, heparin-binding growth-associated molecule; HBNF, heparin-binding neurite-promoting factor; MK, midkine; PTN, pleiotrophin; RPTP, receptor-type t...

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Mediation of human immunodeficiency virus type 1 binding by interaction of cell surface heparan sulfate proteoglycans with the V3 region of envelope gp120-gp41

Cited by 227 publications

References 43 publications

Proteoglycan receptor binding by Neisseria gonorrhoeae MS11 is determined by the HV‐1 region of OpaA

Proteoglycan receptor binding by Neisseria gonorrhoeae MS11 is determined by the HV‐1 region of OpaA

Glycosaminoglycans in infectious disease

Pleiotrophin inhibits HIV infection by binding the cell surface‐expressed nucleolin

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