Host range and variability of calcium binding by surface loops in the capsids of canine and feline parvoviruses

Simpson, A.A.; Chandrasekar, Veda; Hébert, Benoı̂t; Sullivan, Gail M.; Rossmann, Michael G.; Parrish, Colin R.

doi:10.1006/jmbi.2000.3868

Cited by 69 publications

(89 citation statements)

References 48 publications

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“…Viruses were prepared by transfection of plasmids into NLFK cells and passaged fewer than six times. Capsids were prepared by growing virus in NLFK cells and concentrated with polyethylene glycol precipitation or by centrifugation, and then full and empty capsids were separated in sucrose gradients and dialyzed against phosphate-buffered saline (PBS) or 20 mM Tris-HCl (pH 7.5) (1,36).…”

Section: Cells and Virusesmentioning

confidence: 99%

“…The 28-nm-diameter nonenveloped capsid is assembled from 60 copies of a combination of the overlapping capsid proteins VP1 and VP2 (46). The three sites on the capsid that can affect canine host range on the threefold spike are separated from each other by 25 to 30 Å , and all affect the folding or flexibility of loops within the capsid structure, suggesting roles in virus-receptor interactions or in capsid uncoating (1,18,36).CPV type 2 and FPV capsids bind the human or feline transferrin receptors (TfRs) and use those receptors to infect normally resistant Chinese hamster ovary (CHO) cells (25). …”

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confidence: 99%

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The Natural Host Range Shift and Subsequent Evolution of Canine Parvovirus Resulted from Virus-Specific Binding to the Canine Transferrin Receptor

Hueffer

Parker

Weichert

et al. 2003

J Virol

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220

238

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Canine parvovirus (CPV) is a host range variant of a feline virus that acquired the ability to infect dogs through changes in its capsid protein. Canine and feline viruses both use the feline transferrin receptor (TfR) to infect feline cells, and here we show that CPV infects canine cells through its ability to specifically bind the canine TfR. Receptor binding on host cells at 37°C only partially correlated with the host ranges of the viruses, and an intermediate virus strain (CPV type 2) bound to higher levels on cells than did either the feline panleukopenia virus or a later strain of CPV. During the process of adaptation to dogs the later variant strain of CPV gained the ability to more efficiently use the canine TfR for infection and also showed reduced binding to feline and canine cells compared to CPV type 2. Differences on the top and the side of the threefold spike of the capsid surface controlled specific TfR binding and the efficiency of binding to feline and canine cells, and these differences also determined the cell infection properties of the viruses.Canine parvovirus (CPV) emerged in 1978 as the cause of new enteric and myocardial diseases in dogs. The new virus spread globally in a pandemic of disease during 1978 and has since remained endemic in dogs throughout the world (27, 43). The 1978 strain of CPV (termed CPV type 2) was a new virus infecting dogs since there is no serological or other evidence for infection of dogs by a related virus prior to the mid-1970s (27). Phylogenetic analysis shows that all CPV isolates were descended from a single ancestor which emerged during the mid-1970s, which was closely related to the long-known feline panleukopenia virus (FPV) which infects cats, mink, and raccoons but not dogs or cultured dog cells (43). FPV and CPV isolates differ by as little as 0.5% in DNA sequence, and the characteristic properties of CPV type 2 are controlled by a small number of changes in the capsid surface. Two differences between FPV and CPV changed VP2 residues 93 from Lys to Asn and 323 from Asp to Asn, and those changes alone could introduce the canine host range, a CPV-specific antigenic epitope, and a difference in the pH dependence of hemagglutination into FPV (9, 14). Despite the close relationship to FPV, CPV type 2 isolates did not replicate in cats (42,44), and this host range was determined at least in part by VP2 residues 80, 564, and 568 which are in close proximity in the capsid structure (41). Other mutations in the same structural region of CPV type 2 were selected by passage in cat cells (VP2 residue 300 from Ala to Asp), and these reduced the infection of canine cells, as did closely adjacent changes in in vitro prepared mutants (VP2 residue 299 Gly to Glu) (18,26).Host range-controlling residues are located on a raised region of the capsid that surrounds the threefold axis (the threefold spike) (9, 46). VP2 residues 93 and 323 are found near the top of that structure, whereas residues 299 and 300, and changes controlling feline host range, are all on a ridge ...

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Section: Cells and Virusesmentioning

confidence: 99%

mentioning

confidence: 99%

The Natural Host Range Shift and Subsequent Evolution of Canine Parvovirus Resulted from Virus-Specific Binding to the Canine Transferrin Receptor

Hueffer

Parker

Weichert

et al. 2003

J Virol

Self Cite

220

238

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“…Crystal structures of host range and antigenic mutants of CPV, as well as of CPV and FPV under various pH and ionic conditions, have also been determined (26,36,53). The structures of AMDV strain G (AMDV-G), AAV2, AAV4, AAV5, B19-globoside receptor complex, CPV-Fab complex, and Junonia coenia densovirus (JcDNV) have been determined by cryoelectron microscopy and image reconstruction (13,18,34,39,44,64,65).…”

mentioning

confidence: 99%

Structural Determinants of Tissue Tropism and In Vivo Pathogenicity for the Parvovirus Minute Virus of Mice

Kontou

Govindasamy

Nam

et al. 2005

J Virol

194

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Two strains of the parvovirus minute virus of mice (MVM), the immunosuppressive (MVMi) and the prototype (MVMp) strains, display disparate in vitro tropism and in vivo pathogenicity. We report the crystal structures of MVMp virus-like particles (MVMp b ) and native wild-type (wt) empty capsids (MVMp e ), determined and refined to 3.25 and 3.75 Å resolution, respectively, and their comparison to the structure of MVMi, also refined to 3.5 Å resolution in this study. A comparison of the MVMp b and MVMp e capsids showed their structures to be the same, providing structural verification that some heterologously expressed parvovirus capsids are indistinguishable from wt capsids produced in host cells. The structures of MVMi and MVMp capsids were almost identical, but local surface conformational differences clustered from symmetry-related capsid proteins at three specific domains: (i) the icosahedral fivefold axis, (ii) the "shoulder" of the protrusion at the icosahedral threefold axis, and (iii) the area surrounding the depression at the icosahedral twofold axis. The latter two domains contain important determinants of MVM in vitro tropism (residues 317 and 321) and forward mutation residues (residues 399, 460, 553, and 558) conferring fibrotropism on MVMi. Furthermore, these structural differences between the MVM strains colocalize with tropism and pathogenicity determinants mapped for other autonomous parvovirus capsids, highlighting the importance of common parvovirus capsid regions in the control of virus-host interactions.

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“…In the case of FPV and CPV, related parvoviruses, attachment then entry by endocytosis can occur in many different kinds of non-permissive cells, indicating that their host range can be determined by events after cell entry. Amino acid residues 359 to 375 found in a flexible capsid protein loop were found to exhibit differential conformation when exposed to various concentrations of protons and Ca ++ (Simpson et al, 2000). It was found that this region was functionally associated with both hemagglutinating activity and host range determinants providing continuance of successful replication.…”

Section: Attachment Of Virus To the Cellmentioning

confidence: 99%

Clathrin-Associated Endocytosis as a Route of Entry into Cells for Parvoviruses

Johnson¹,

Dudleenamjil²

2012

Molecular Regulation of Endocytosis

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Host range and variability of calcium binding by surface loops in the capsids of canine and feline parvoviruses

Cited by 69 publications

References 48 publications

The Natural Host Range Shift and Subsequent Evolution of Canine Parvovirus Resulted from Virus-Specific Binding to the Canine Transferrin Receptor

The Natural Host Range Shift and Subsequent Evolution of Canine Parvovirus Resulted from Virus-Specific Binding to the Canine Transferrin Receptor

Structural Determinants of Tissue Tropism and In Vivo Pathogenicity for the Parvovirus Minute Virus of Mice

Clathrin-Associated Endocytosis as a Route of Entry into Cells for Parvoviruses

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