A 60 kD heat-shock protein-like molecule interacts with the HIV transmembrane glycoprotein gp41

Speth, Cornelia; Prohászka, Zoltán; Mair, Mechthild; Stöckl, Gabriele; Zhu, Xiaoyan; Jöbstl, Barbara; Füst, George; Dierich, Manfred P.

doi:10.1016/s0161-5890(99)00082-6

Cited by 27 publications

(19 citation statements)

References 26 publications

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“…Previously, interaction of eukaryotic Hsp60 with staphylococcal fibronectin-binding protein had also been established in both human and bovine epithelial cell lines (11). Surface Hsp60 extracted from Raji B cells also interacted with the human immunodeficiency virus transmembrane glycoprotein gp41 (44).…”

Section: Discussionmentioning

confidence: 99%

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Heat Shock Protein 60 Acts as a Receptor for theListeriaAdhesion Protein in Caco-2 Cells

et al. 2004

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The 104-kDa Listeria adhesion protein (LAP) in Listeria monocytogenes is involved in binding to various mammalian cell lines. However, the receptor that interacts with LAP in eukaryotic cells is unknown. In this study, scanning immunoelectron microscopy qualitatively demonstrated greater binding capacity of wild-type (WT) L. monocytogenes strain (F4244) than a LAP-deficient mutant strain (KB208) to Caco-2 cells. The goal of this study was identification of the host cell receptor for LAP. Using a Western blot ligand overlay assay, we identified a protein of 58 kDa to be the putative receptor for LAP from Caco-2 cells. N-terminal sequencing and subsequent database search identified this protein as heat shock protein 60 (Hsp60). Modified immunoseparation with protein A-Sepharose beads bound to the LAP-specific monoclonal antibody H7 (MAb-H7) and a sequential incubation with LAP preparation and Caco-2 lysate confirmed the receptor to be the same 58-kDa protein. Western blot analysis with anti-Hsp60 MAb of whole-cell adhesion between Caco-2 and WT also revealed the receptor protein to be a 58-kDa protein, thus corroborating the identification of Hsp60 as a host cell receptor for LAP. Furthermore, the anti-Hsp60 antibody also caused approximately 74% reduction in binding of L. monocytogenes WT to Caco-2 cells, whereas a control antibody, C11E9, had no effect on binding. The adhesion mechanism of L. monocytogenes to eukaryotic cells is a complex process, and identification of Hsp60 as a receptor for LAP adds to the list of previously discovered ligand-receptor modules that are essential to achieve successful adhesion.

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Section: Discussionmentioning

confidence: 99%

“…Furthermore, systemic stress or Crohn's disease can also increase Hsp60 expression, respectively, in rat or human intestinal mucosa (30,37). Hsp60 has been identified as a ligand for fibronectin in Staphylococcus aureus (11) and the human immunodeficiency virus protein gp41 (44) in human cultured cell lines.…”

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confidence: 99%

Heat Shock Protein 60 Acts as a Receptor for theListeriaAdhesion Protein in Caco-2 Cells

et al. 2004

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“…Interestingly, it has been reported that HSP-60 interacts with gp41, a transmembrane protein anchoring the surface protein gp120 to the envelope of HIV-1. In addition, gp41 mediates fusion between the membranes of the virus, HIV-1, and the host cell, a step essential for viral entry (Speth et al, 1999). In the current study, HSP60 was found to be overexpressed upon treatment of NHA with Δ 9 -THC.…”

Section: Discussionmentioning

confidence: 99%

Genomic and proteomic analysis of the effects of cannabinoids on normal human astrocytes

et al. 2008

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Delta-9-tetrahydrocannabinol (Δ 9 -THC), the main psychoactive component of marijuana, is known to dysregulate various immune responses. Cannabinoid (CB)-1 and -2 receptors are expressed mainly on cells of the central nervous system (CNS) and the immune system. The CNS is the primary target of cannabinoids and astrocytes are known to play a role in various immune responses. Thus we undertook this investigation to determine the global molecular effects of cannabinoids on normal human astrocytes (NHA) using genomic and proteomic analyses. NHA were treated with Δ 9 -THC and assayed using gene microarrays and two-dimensional (2D) difference gel electrophoresis (DIGE) coupled with mass spectrometry (MS) to elucidate their genomic and proteomic profiles respectively. Our results show that the expression of more than 20 translated protein gene products from NHA was differentially dysregulated by treatment with Δ 9 -THC compared to untreated, control NHA.

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“…With regard to the interaction of stress proteins with viral polypeptides at the cell surface level, an hsp60-like protein located on the surface of freshly isolated human monocytes, as well as in established monocytic and T-cell lines, has been shown to interact with the human immunodeficiency virus gp41 protein, and it has been suggested that this interaction might facilitate the virus infection (52). Also, hsc70 has been described as an enhancement factor on the surface of murine fibroblasts and in a human T-cell line for the syncytium formation induced by human T-cell lymphotropic virus type 1 (13,49).…”

Section: Vol 76 2002 Notes 4097mentioning

confidence: 99%

Heat Shock Cognate Protein 70 Is Involved in Rotavirus Cell Entry

Guerrero

Bouyssounade

Zárate

et al. 2002

J Virol

152

128

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In this work, we have identified the heat shock cognate protein (hsc70) as a receptor candidate for rotaviruses. hsc70 was shown to be present on the surface of MA104 cells, and antibodies to this protein blocked rotavirus infectivity, while not affecting the infectivity of reovirus and poliovirus. Preincubation of the hsc70 protein with the viruses also inhibited their infectivity. Triple-layered particles (mature virions), but not double-layered particles, bound hsc70 in a solid-phase assay, and this interaction was blocked by monoclonal antibodies to the virus surface proteins VP4 and VP7. Rotaviruses were shown to interact with hsc70 at a postattachment step, since antibodies to hsc70 and the protein itself did not inhibit the virus attachment to cells. We propose that the functional rotavirus receptor is a complex of several cell surface molecules that include, among others, hsc70.

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A 60 kD heat-shock protein-like molecule interacts with the HIV transmembrane glycoprotein gp41

Cited by 27 publications

References 26 publications

Heat Shock Protein 60 Acts as a Receptor for theListeriaAdhesion Protein in Caco-2 Cells

Heat Shock Protein 60 Acts as a Receptor for theListeriaAdhesion Protein in Caco-2 Cells

Genomic and proteomic analysis of the effects of cannabinoids on normal human astrocytes

Heat Shock Cognate Protein 70 Is Involved in Rotavirus Cell Entry

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