Avian homologs of the mammalian low-density lipoprotein receptor family bind minor receptor group human rhinovirus

Gruenberger, Martin; Wandl, Robert; Nimpf, Johannes; Hiesberger, Thomas; Schneider, Wolfgang J.; Kuechler, Ernst; Blaas, Dieter

doi:10.1128/jvi.69.11.7244-7247.1995

Cited by 30 publications

(10 citation statements)

References 24 publications

(15 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We have previously shown that detergent-solubilized OVR, the avian homologue of mammalian VLDLR, inhibits infection of HeLa cells by HRV2 (9). However, since this receptor is not involved in viral infection (rhinoviruses do not replicate in any species except humans and other primates), it was of interest whether soluble LDLR fragments would also inhibit infection.…”

Section: Soluble Ldlr Fragments Inhibit Minor Group Hrv Infectionmentioning

confidence: 99%

Recombinant soluble low density lipoprotein receptor fragment inhibits minor group rhinovirus infection in vitro

et al. 1998

View full text Add to dashboard Cite

A fragment of the low density lipoprotein receptor encompassing the seven ligand binding repeats was expressed in Sf9 insect cells as a fusion protein with a carboxyl-terminally linked hexa-his tag by using a baculovirus vector. Up to 10 mg/l of the fusion protein was secreted into the medium. The material was soluble in the absence of detergent and active in binding beta very low density lipoprotein and a member of the minor group of human rhinoviruses (HRV2) in ligand blots from sodium dodecyl sulfate-polyacrylamide gels run under nonreducing conditions. The receptor fragment specifically inhibits viral infection of HeLa cells by minor group HRVs in a concentration-dependent manner. Viral infectivity is neutralized by aggregation.

show abstract

Section: Soluble Ldlr Fragments Inhibit Minor Group Hrv Infectionmentioning

confidence: 99%

Recombinant soluble low density lipoprotein receptor fragment inhibits minor group rhinovirus infection in vitro

et al. 1998

View full text Add to dashboard Cite

show abstract

“…Soluble recombinant human VLDLR inhibits HRV infection. We have previously shown that the chicken ovarian VLDL receptor (OVR) binds HRV2 on ligand blots and inhibits HRV2 infection of HeLa cells in its detergent solubilized form (8). However, HRVs fail to replicate in birds; therefore, the function of OVR as a viral receptor is questionable.…”

Section: The Protein Shed From Hela Cells Is a Fragment Of Vldlrmentioning

confidence: 99%

Very-Low-Density Lipoprotein Receptor Fragment Shed from HeLa Cells Inhibits Human Rhinovirus Infection

Marlovits¹,

Abrahamsberg²,

Blaas³

1998

J Virol

View full text Add to dashboard Cite

The large family of human rhinoviruses, the main causative agents of the common cold, is divided into the major and the minor group based on receptor specificity. Major group viruses attach to intercellular adhesion molecule 1 (ICAM-1), a member of the immunoglobulin superfamily, whereas minor group viruses use low-density lipoprotein receptors (LDLR) for cell entry. During early attempts aimed at isolating the minor group receptor, we discovered that a protein with virus binding activity was released from HeLa cells upon incubation with buffer at 37°C (F. Hofer, B. Berger, M. Gruenberger, H. Machat, R. Dernick, U. Tessmer, E. Kuechler, and D. Blaas, J. Gen. Virol. 73:627–632, 1992). In light of the recent discovery of several new members of the LDLR family, we reinvestigated the nature of this protein and present evidence for its being derived from the human very-low density lipoprotein receptor (VLDLR). A soluble VLDLR fragment encompassing the eight complement type repeats and representing the N-terminal part of the receptor was then expressed in the baculovirus system; both the shed protein and the recombinant soluble VLDLR bind minor group viruses and inhibit viral infection of HeLa cells in a concentration-dependent manner.

show abstract

“…The various members of the large family Picornaviridae use a number of different membrane receptors to attach to and ultimately infect their target cells. These surface proteins belong to families as diverse as the immunoglobulin (Ig) superfamily (14,45,47), integrins (4,5), complement-inactivating proteins (24,49), lipoprotein receptors (17,20), and mucintype glycoproteins (23). For several representative picornaviruses, data have been presented which strongly suggest that the virions are internalized by their respective receptors into endosomes (50), where it was shown for foot-and-mouth disease virus and for the minor-group rhinovirus human rhinovirus type 2 (HRV2) that the low intravesicular pH triggers RNA release (3,39).…”

mentioning

confidence: 99%

Major and Minor Receptor Group Human Rhinoviruses Penetrate from Endosomes by Different Mechanisms

Schober

Kronenberger

Prchla

et al. 1998

J Virol

100

View full text Add to dashboard Cite

Intercellular adhesion molecule 1 and the low-density lipoprotein receptor are used for cell entry by major and minor receptor group human rhinoviruses (HRVs), respectively. Whereas minor-group viruses, exemplified by HRV2, transfer their genomic RNA to the cytoplasm through a pore in the endosomal membrane (E. Prchla, C. Plank, E. Wagner, D. Blaas, and R. Fuchs, J. Cell Biol. 131:111–123, 1995), the mechanism of in vivo uncoating of major-group HRVs has not been elucidated so far. Using free-flow electrophoresis, we performed a comparative analysis of cell entry by HRV2 and the major group rhinovirus HRV14. Here we demonstrate that this technique allows the separation of free viral particles from those associated with early endosomes, late endosomes, and plasma membranes. Upon free-flow electrophoretic separation of microsomes, HRV14 was recovered from endosomes under conditions which prevent uncoating, whereas the proportion of free viral particles increased with time under conditions which promote uncoating. The remaining virus eluted within numerous fractions corresponding to membraneous material, with no clear endosomal peaks being discernible. This suggests that uncoating of HRV14 results in lysis of the endosomal membrane and release of subviral 135S and 80S particles into the cytoplasm.

show abstract

Avian homologs of the mammalian low-density lipoprotein receptor family bind minor receptor group human rhinovirus

Abstract: Avian oocyte-specific very low density lipoprotein receptor specifically binds human rhinovirus of the minor receptor group on ligand blots and in solution. The solubilized receptor protects cells against infection in a dose-dependent manner.

Cited by 30 publications

References 24 publications

Recombinant soluble low density lipoprotein receptor fragment inhibits minor group rhinovirus infection in vitro

Recombinant soluble low density lipoprotein receptor fragment inhibits minor group rhinovirus infection in vitro

Very-Low-Density Lipoprotein Receptor Fragment Shed from HeLa Cells Inhibits Human Rhinovirus Infection

Major and Minor Receptor Group Human Rhinoviruses Penetrate from Endosomes by Different Mechanisms

Contact Info

Product

Resources

About