The Novel Avian Leukosis Virus Subgroup K Shares Its Cellular Receptor with Subgroup A

ABSTRACTAvian leukosis virus subgroup K (ALV-K) is composed of newly emerging isolates, which, in sequence analyses, cluster separately from the well-characterized subgroups A, B, C, D, E, and J. However, it remains unclear whether ALV-K represents an independent ALV subgroup with regard to receptor usage, host range, and superinfection interference. In the present study, we examined the host range of the Chinese infectious isolate JS11C1, an ALV-K prototype, and we found substantial overlap of species that were either resistant or susceptible to ALV-A and JS11C1. Ectopic expression of the chickentvagene in mammalian cells conferred susceptibility to JS11C1, while genetic ablation of thetvagene rendered chicken DF-1 cells resistant to infection by JS11C1. Thus,tvaexpression is both sufficient and necessary for JS11C1 entry. Receptor sharing was also manifested in superinfection interference, with preinfection of cells with ALV-A, but not ALV-B or ALV-J, blocking subsequent JS11C1 infection. Finally, direct binding of JS11C1 and Tva was demonstrated by preincubation of the virus with soluble Tva, which substantially decreased viral infectivity in susceptible chicken cells. Collectively, these findings indicate that JS11C1 represents a new andbona fideALV subgroup that utilizes Tva for cell entry and binds to a site other than that for ALV-A.IMPORTANCEALV consists of several subgroups that are particularly characterized by their receptor usage, which subsequently dictates the host range and tropism of the virus. A few newly emerging and highly pathogenic Chinese ALV strains have recently been suggested to be an independent subgroup, ALV-K, based solely on their genomic sequences. Here, we performed a series of experiments with the ALV-K strain JS11C1, which showed its dependence on the Tva cell surface receptor. Due to the sharing of this receptor with ALV-A, both subgroups were able to interfere with superinfection. Because ALV-K could become an important pathogen and a significant threat to the poultry industry in Asia, the identification of a specific receptor could help in the breeding of resistant chicken lines with receptor variants with decreased susceptibility to the virus.

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Endocytic Delivery of Vancomycin Mediated by a Synthetic Cell Surface Receptor: Rescue of Bacterially Infected Mammalian Cells and Tissue Targeting In Vivo

Journal of the American Chemical Society ◽

10.1021/ja067674f ◽

2007 ◽

Vol 129 (2) ◽

pp. 268-269 ◽

Cited By ~ 30

Author(s):

Siwarutt Boonyarattanakalin ◽

Jianfang Hu ◽

Sheryl A. Dykstra-Rummel ◽

Avery August ◽

Blake R. Peterson

Keyword(s):

Cell Surface ◽

Mammalian Cells ◽

Cell Surface Receptor ◽

Synthetic Cell ◽

Tissue Targeting ◽

Surface Receptor

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Targeting Avian Leukosis Virus Subgroup A Vectors by Using a TVA-VEGF Bridge Protein

Journal of Virology ◽

10.1128/jvi.75.3.1571-1575.2001 ◽

2001 ◽

Vol 75 (3) ◽

pp. 1571-1575 ◽

Cited By ~ 16

Author(s):

Sophie Snitkovsky ◽

Thomas M. J. Niederman ◽

Richard C. Mulligan ◽

John A. T. Young

Keyword(s):

Growth Factor ◽

Retroviral Vectors ◽

Avian Leukosis Virus ◽

Cell Surface Receptor ◽

Egf Receptors ◽

Retroviral Infection ◽

Linker Peptide ◽

Amino Acid Form ◽

Surface Receptor ◽

Endothelial Growth Factor

ABSTRACT Previously, we have demonstrated that bridge proteins comprised of avian leukosis virus (ALV) receptors fused to epidermal growth factor (EGF) can be used to selectively target retroviral vectors with ALV envelope proteins to cells expressing EGF receptors. To determine whether another type of ligand incorporated into an ALV receptor-containing bridge protein can also function to target retroviral infection, the TVA-VEGF110 bridge protein was generated. TVA-VEGF110 consists of the extracellular domain of the TVA receptor for ALV subgroup A (ALV-A), fused via a proline-rich linker peptide to a 110-amino-acid form of vascular endothelial growth factor (VEGF). This bridge protein bound specifically to its cell surface receptor, VEGFR-2, and efficiently mediated the entry of an ALV-A vector into cells. These studies indicate that ALV receptor-ligand bridge proteins may be generally useful tools for retroviral targeting approaches.

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Neuropilin-1 and heparan sulfate proteoglycans cooperate in cellular uptake of nanoparticles functionalized by cationic cell-penetrating peptides

Science Advances ◽

10.1126/sciadv.1500821 ◽

2015 ◽

Vol 1 (10) ◽

pp. e1500821 ◽

Cited By ~ 36

Author(s):

Hong-Bo Pang ◽

Gary B. Braun ◽

Erkki Ruoslahti

Keyword(s):

Cell Surface ◽

Heparan Sulfate ◽

Vascular Permeability ◽

Mammalian Cells ◽

Cell Penetrating Peptides ◽

Proteolytic Processing ◽

Cell Surface Receptor ◽

Neuropilin 1 ◽

Cell Penetrating ◽

Surface Receptor

Cell-penetrating peptides (CPPs) have been widely used to deliver nanomaterials and other types of macromolecules into mammalian cells for therapeutic and diagnostic use. Cationic CPPs that bind to heparan sulfate (HS) proteoglycans on the cell surface induce potent endocytosis; however, the role of other surface receptors in this process is unclear. We describe the convergence of an HS-dependent pathway with the C-end rule (CendR) mechanism that enables peptide ligation with neuropilin-1 (NRP1), a cell surface receptor known to be involved in angiogenesis and vascular permeability. NRP1 binds peptides carrying a positive residue at the carboxyl terminus, a feature that is compatible with cationic CPPs, either intact or after proteolytic processing. We used CPP and CendR peptides, as well as HS- and NRP1-binding motifs from semaphorins, to explore the commonalities and differences of the HS and NRP1 pathways. We show that the CendR-NRP1 interaction determines the ability of CPPs to induce vascular permeability. We also show at the ultrastructural level, using a novel cell entry synchronization method, that both the HS and NRP1 pathways can initiate a macropinocytosis-like process and visualize these CPP-cargo complexes going through various endosomal compartments. Our results provide new insights into how CPPs exploit multiple surface receptor pathways for intracellular delivery.

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Specific Capture of Mammalian Cells by Cell Surface Receptor Binding to Ligand Immobilized on Gold Thin Films

Journal of Proteome Research ◽

10.1021/pr050467e ◽

2006 ◽

Vol 5 (7) ◽

pp. 1580-1585 ◽

Cited By ~ 32

Author(s):

Dora Peelen ◽

Voula Kodoyianni ◽

Jieun Lee ◽

Ting Zheng ◽

Michael R. Shortreed ◽

...

Keyword(s):

Thin Films ◽

Cell Surface ◽

Receptor Binding ◽

Mammalian Cells ◽

Cell Surface Receptor ◽

Surface Receptor ◽

Gold Thin Films

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Subcellular Redistribution of Pit-2 PiTransporter/Amphotropic Leukemia Virus (A-MuLV) Receptor in A-MuLV-Infected NIH 3T3 Fibroblasts: Involvement in Superinfection Interference

Journal of Virology ◽

10.1128/jvi.74.6.2847-2854.2000 ◽

2000 ◽

Vol 74 (6) ◽

pp. 2847-2854 ◽

Cited By ~ 25

Author(s):

Zsolt Jobbagy ◽

Susan Garfield ◽

Lisa Baptiste ◽

Maribeth V. Eiden ◽

Wayne B. Anderson

Keyword(s):

Plasma Membrane ◽

Mammalian Cells ◽

Leukemia Virus ◽

Cell Surface Receptor ◽

3T3 Cells ◽

Sodium Dependent ◽

Surface Receptor ◽

A Cell ◽

Nih 3T3 ◽

Nih 3T3 Cells

ABSTRACT Amphotropic murine leukemia virus (A-MuLV) utilizes the Pit-2 sodium-dependent phosphate transporter as a cell surface receptor to infect mammalian cells. Previous studies established that infection of cells with A-MuLV resulted in the specific down-modulation of phosphate uptake mediated by Pit-2 and in resistance to superinfection with A-MuLV. To study the mechanisms underlying these phenomena, we constructed plasmids capable of efficiently expressing ɛ epitope- and green fluorescent protein (GFP)-tagged human Pit-2 proteins in mammalian cells. Overexpression of ɛ-epitope-tagged Pit-2 transporters in NIH 3T3 cells resulted in a marked increase in sodium-dependent Pi uptake. This increase in Piuptake was specifically blocked by A-MuLV infection but not by infection with ecotropic MuLV (E-MuLV) (which utilizes a cationic amino acid transporter, not Pit-2, as a cell surface receptor). These data, together with the finding that the tagged Pit-2 transporters retained their A-MuLV receptor function, indicate that the insertion of epitope tags does not affect either retrovirus receptor or Pitransporter function. The overexpressed epitope-tagged transporters were detected in cell lysates, by Western blot analysis using both ɛ-epitope- and GFP-specific antibodies as well as with Pit-2 antiserum. Both the epitope- and GFP-tagged transporters showed almost exclusive plasma membrane localization when expressed in NIH 3T3 cells, as determined by laser scanning confocal microscopy. Importantly, when NIH 3T3 cells expressing these proteins were productively infected with A-MuLV, the tagged transporters and receptors were no longer detected in the plasma membrane but rather were localized to a punctate structure within the cytosolic compartment distinct from Golgi, endoplasmic reticulum, endosomes, lysosomes, and mitochondria. The intracellular Pit-2 pool colocalized with the virus in A-MuLV-infected cells. A similar redistribution of the tagged Pit-2 proteins was not observed following infection with E-MuLV, indicating that the redistribution of Pit-2 is not directly attributable to general effects associated with retroviral infection but rather is a specific consequence of A-MuLV–Pit-2 interactions.

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Cell surface receptor for ecotropic host-range mouse retroviruses: a cationic amino acid transporter

Positive-Strand RNA Viruses ◽

10.1007/978-3-7091-9326-6_47 ◽

1994 ◽

pp. 485-494

Author(s):

M. P. Kavanaugh ◽

H. Wang ◽

C. A. R. Boyd ◽

R. A. North ◽

D. Kabat

Keyword(s):

Amino Acid ◽

Cell Surface ◽

Host Range ◽

Amino Acid Transporter ◽

Cell Surface Receptor ◽

Cationic Amino Acid Transporter ◽

Cationic Amino Acid ◽

Surface Receptor ◽

Acid Transporter

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NCAM regulates cell motility

Journal of Cell Science ◽

10.1242/jcs.115.2.283 ◽

2002 ◽

Vol 115 (2) ◽

pp. 283-292 ◽

Cited By ~ 1

Author(s):

Søren Prag ◽

Eugene A. Lepekhin ◽

Kateryna Kolkova ◽

Rasmus Hartmann-Petersen ◽

Anna Kawa ◽

...

Keyword(s):

Heparan Sulfate ◽

Cell Motility ◽

Ectopic Expression ◽

Inhibitory Effect ◽

Heparan Sulfate Proteoglycan ◽

Cell Surface Receptor ◽

Sulfate Proteoglycan ◽

Cellular Motility ◽

Cellular Attachment ◽

Surface Receptor

Cell migration is required during development of the nervous system. The regulatory mechanisms for this process, however, are poorly elucidated. We show here that expression of or exposure to the neural cell adhesion molecule (NCAM) strongly affected the motile behaviour of glioma cells independently of homophilic NCAM interactions. Expression of the transmembrane 140 kDa isoform of NCAM (NCAM-140) caused a significant reduction in cellular motility, probably through interference with factors regulating cellular attachment, as NCAM-140-expressing cells exhibited a decreased attachment to a fibronectin substratum compared with NCAM-negative cells. Ectopic expression of the cytoplasmic part of NCAM-140 also inhibited cell motility, presumably via the non-receptor tyrosine kinase p59fyn with which NCAM-140 interacts. Furthermore, we showed that the extracellular part of NCAM acted as a paracrine inhibitor of NCAM-negative cell locomotion through a heterophilic interaction with a cell-surface receptor. As we showed that the two N-terminal immunoglobulin modules of NCAM, which are known to bind to heparin, were responsible for this inhibition, we presume that this receptor is a heparan sulfate proteoglycan. A model for the inhibitory effect of NCAM is proposed, which involves competition between NCAM and extracellular components for the binding to membrane-associated heparan sulfate proteoglycan.

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Faculty Opinions recommendation of Endocytic delivery of vancomycin mediated by a synthetic cell surface receptor: rescue of bacterially infected Mammalian cells and tissue targeting in vivo.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1103770.559890 ◽

2008 ◽

Author(s):

Daniel Flynn

Keyword(s):

Cell Surface ◽

Mammalian Cells ◽

Cell Surface Receptor ◽

Synthetic Cell ◽

Tissue Targeting ◽

Surface Receptor

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Endocytosis

Physiological Reviews ◽

10.1152/physrev.1997.77.3.759 ◽

1997 ◽

Vol 77 (3) ◽

pp. 759-803 ◽

Cited By ~ 1061

Author(s):

S. Mukherjee ◽

R. N. Ghosh ◽

F. R. Maxfield

Keyword(s):

Antigen Presentation ◽

Mammalian Cells ◽

Membrane Lipids ◽

Extracellular Fluid ◽

Cell Polarization ◽

Receptor Expression ◽

Cell Surface Receptor ◽

Coated Pits ◽

Surface Receptor ◽

Membrane Components

Mammalian cells take up extracellular material by a variety of different mechanisms that are collectively termed endocytosis. Endocytic mechanisms serve many important cellular functions including the uptake of extracellular nutrients, regulation of cell-surface receptor expression, maintenance of cell polarity, and antigen presentation. Endocytic pathways are also utilized by viruses, toxins, and symbiotic microorganisms to gain entry into cells. One of the best-characterized endocytic mechanisms is receptor-mediated endocytosis via clathrin-coated pits. This type of endocytosis constitutes the major emphasis of this review, with a brief discussion of other endocytic mechanisms and their comparison with the receptor-mediated pathway. This review describes and evaluates critically current understanding of the mechanisms of entry of plasma membrane components such as the receptor-ligand complexes and membrane lipids as well as the extracellular fluid into cells. The intracellular sorting and trafficking of these molecules upon internalization are also described. The roles of endocytosis in physiological and pathological processes are discussed. These include maintenance of cell polarization, antigen presentation, glucose transport, atherosclerosis, Alzheimer's disease, and the endocytosis of toxins and viruses.

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