The Poliovirus Receptor: Identification of Domains and Amino Acid Residues Critical for Virus Binding

Bernhardt, Günter; Harber, James; Zibert, Andree; deCrombrugghe, Marie; Wimmer, Eckard

doi:10.1006/viro.1994.1493

Cited by 70 publications

(64 citation statements)

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“…The interactions described above are consistent with mutational analyses of CD155 (19,20,(38)(39)(40)(41)(42)(43) (Fig. 4 and Table S14) in that all of the mutations that affect receptor binding are on or very close to the residues identified as being in the virus-receptor interface.…”

Section: Resultssupporting

confidence: 78%

“…In general, mutations (other than conservative changes) that are in the receptor footprint affect CD155 binding (magenta residues in Fig. 6A) and viral replication (19,20,(38)(39)(40)(41)(42)(43) (Table S14). Conversely, mutations that are not in the footprint do not have any effect (yellow residues in Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The CD155 amino-terminal domain, D1, which is responsible for viral recognition (19,20), is most closely related to the variable domains in antibodies (21). The fully deglycosylated CD155 can function as a receptor for PV, but is significantly more efficient in mediating PV infection compared with WT CD155 (13).…”

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confidence: 99%

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Crystal structure of CD155 and electron microscopic studies of its complexes with polioviruses

Zhang

Mueller

Morais

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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When poliovirus (PV) recognizes its receptor, CD155, the virus changes from a 160S to a 135S particle before releasing its genome into the cytoplasm. CD155 is a transmembrane protein with 3 Ig-like extracellular domains, D1-D3, where D1 is recognized by the virus. The crystal structure of D1D2 has been determined to 3.5-Å resolution and fitted into Ϸ8.5-Å resolution cryoelectron microscopy reconstructions of the virus-receptor complexes for the 3 PV serotypes. These structures show that, compared with human rhinoviruses, the virus-receptor interactions for PVs have a greater dependence on hydrophobic interactions, as might be required for a virus that can inhabit environments of different pH. The pocket factor was shown to remain in the virus during the first recognition stage. The present structures, when combined with earlier mutational investigations, show that in the subsequent entry stage the receptor moves further into the canyon when at a physiological temperature, thereby expelling the pocket factor and separating the viral subunits to form 135S particles. These results provide a detailed analysis of how a nonenveloped virus can enter its host cell.cell entry ͉ receptor ͉ virus

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Section: Resultssupporting

confidence: 78%

Section: Resultsmentioning

confidence: 99%

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Crystal structure of CD155 and electron microscopic studies of its complexes with polioviruses

Zhang

Mueller

Morais

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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“…Feline calicivirus (FCV), which is culturable, shares a number of biochemical properties, similar genomic organization and primary RNA sequences with noroviruses, and has been used as a virus surrogate to study the noroviruses (Slomka and Appleton 1998;Doultree et al 1999). Poliovirus (PV) is a member of the Picornaviridae family and is an enteric virus which infects the epithelial cells of the upper and lower intestinal tract of humans initially and infection may then progress to the central nervous system, and in severe cases can cause paralysis (Sicinski et al 1990;Bernhardt et al 1994;Ponnuraj et al 1998).…”

Section: Introductionmentioning

confidence: 99%

The effect of bovine lactoferrin and lactoferricin B on the ability of feline calicivirus (a norovirus surrogate) and poliovirus to infect cell cultures

et al. 2003

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Aims:To characterize the effect of bovine lactoferrin and lactoferricin B against feline calicivirus (FCV), a norovirus surrogate and poliovirus (PV), as models for enteric viruses. Methods and Results: Crandell-Reese feline kidney (CRFK) cells were used for the propagation of FCV and monkey embryo kidney (MEK) cells for PV. The assays included visual assessment of cell lines for cytopathic effects and determination of the percentage cell death using MTT [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium] dye reduction assay. Incubation of bovine lactoferrin with CRFK cells either prior to or together with FCV inoculation substantially reduced FCV infection. In contrast, the interference of lactoferrin with the infection of cells with PV was demonstrated only when lactoferrin was present with cell lines and virus for the entire assay period. Using indirect immunofluorescence, lactoferrin was detected on the surface of both CRFK and MEK cells, suggesting that the interference of viral infection may be attributed to lactoferrin binding to the surfaces of susceptible cells, thereby preventing the attachment of the virus particles. Lactoferricin B, a cationic antimicrobial peptide derived from the N-terminal domain of bovine lactoferrin, reduced FCV but not PV infection. Conclusion: Lactoferrin was shown to interfere with the infection of cells for both FCV and PV. However, lactoferricin B showed no interference of infection with PV and interference with infection for FCV required the presence of lactoferricin B together with the cell line and virus. Significance and Impact of the Study: An in vitro basis is provided for the effects of bovine lactoferrin and lactoferricin B in moderating food-borne infections of enteric viruses.

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“…Whether the low steady state level of the hPVR␦ message is due to less frequent splicing events or is the result of decreased hPVR␦ mRNA stability (2) remains to be determined. Unexpectedly, this is not reflected by the amount of the corresponding proteins observed in various cell lines (10). The reason for the unequal expression of the hPVR mRNAs, on the one hand, and the roughly similar abundance of the polypeptides, on the other hand, is not known.…”

Section: Discussionmentioning

confidence: 92%

The Promoters for Human and Monkey Poliovirus Receptors

Solecki

Schwarz

Wimmer

et al. 1997

Journal of Biological Chemistry

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The cellular receptors for poliovirus (PVR) are glycoproteins belonging to the immunoglobulin superfamily. Functional receptors for poliovirus are only expressed by primates; known rodent homologues lack the ability to bind virus due to amino acid differences. Human poliovirus infections are targeted to the gastrointestinal tract and, rarely, to motor neurons in the central nervous system. Available evidence suggests that poliovirus uses only one cellular receptor, implying that the tissue tropism of poliovirus is likely to be related to the expression of the human PVR (hPVR). However, low levels of expression of hPVR-specific mRNAs can be detected in many human tissues other than the apparent target cells. The nonpathogenic function of hPVR is unknown. For a study of the transcriptional control of hPVR expression, we have isolated and characterized the promoter of the hPVR gene. Deletion analysis defined an approximately 280 base pair minimal promoter fragment that: 1) lacks TATA-and CAAT-like elements, 2) is distinguished by a high GC content, and 3) promotes transcription at multiple start sites. The pattern of activity caused by transfection of serial 5 -and 3 -promoter deletions is almost identical in HEp2, HeLa, COS-1, and mouse L929 cells, indicating a similar transcriptional regulation of the hPVR promoter in these cell lines. However, on transfection of Raji cells, a Burkitt's lymphoma cell line harboring a transcriptionally inactive hPVR gene, all promoter reporter constructs tested exerted only residual activity. These results suggest that the cis-element(s) governing cell type-specific hPVR expression resides in the minimal promoter region. We also report the sequences of the promoters of two monkey homologues to hPVR (AGM␣1 and AGM␣2).

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The Poliovirus Receptor: Identification of Domains and Amino Acid Residues Critical for Virus Binding

Cited by 70 publications

References 0 publications

Crystal structure of CD155 and electron microscopic studies of its complexes with polioviruses

Crystal structure of CD155 and electron microscopic studies of its complexes with polioviruses

The effect of bovine lactoferrin and lactoferricin B on the ability of feline calicivirus (a norovirus surrogate) and poliovirus to infect cell cultures

The Promoters for Human and Monkey Poliovirus Receptors

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