PDBsum entry 1k3v

Virus

PDB id

1k3v

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Contents

			Protein chain

					542 a.a. *

* Residue conservation analysis

PDB id:

1k3v

Links

Name:

Virus

Title:

Porcine parvovirus capsid

Structure:

Capsid protein vp2. Chain: a. Synonym: coat protein vp2. Engineered: yes

Source:

Porcine parvovirus. Organism_taxid: 10796. Gene: vp2. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.

Resolution:

3.50Å

R-factor:

0.286

R-free:

0.283

Authors:

A.A.Simpson,B.Hebert,G.M.Sullivan,C.R.Parrish,Z.Zadori,P.Tijssen, M.G.Rossmann

Key ref:

A.A.Simpson et al. (2002). The structure of porcine parvovirus: comparison with related viruses. J Mol Biol, 315, 1189-1198. PubMed id: 11827486 DOI: 10.1006/jmbi.2001.5319

Date:

04-Oct-01

Release date:

24-Oct-01

PROCHECK

	Headers

	References

Protein chain

P18546 (CAPSD_PAVPN) - Capsid protein VP1 from Porcine parvovirus (strain NADL-2)

Seq: Struc:

Seq: Struc:					729 a.a. 542 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

DOI no: 10.1006/jmbi.2001.5319	J Mol Biol 315:1189-1198 (2002)
PubMed id: 11827486

The structure of porcine parvovirus: comparison with related viruses.
A.A.Simpson, B.Hébert, G.M.Sullivan, C.R.Parrish, Z.Zádori, P.Tijssen, M.G.Rossmann.

ABSTRACT

The structure of baculovirus-expressed porcine parvovirus (PPV) capsids was solved using X-ray crystallography and was found to be similar to the related canine parvovirus (CPV) and minute virus of mice (MVM). The PPV capsid protein has 57 % and 49 % amino acid sequence identity with CPV and MVM, respectively, but the degree of conservation of surface-exposed residues is lower than average. Consequently, most of the structural differences are on the surface and are the probable cause of the known variability in antigenicity and host range. The NADL-2 and Kresse strains of PPV have distinct tissue tropisms and pathogenicity, which are mediated by one or more of the amino acid residues 381, 386, and 436. These residues are on or near the surface of the virus capsid, where they are likely to be associated with virus-cell interactions.

Selected figure(s)



	Figure 3. Figure 3. Surface view of residues (yellow) that control tissue tropism. Residue 436 is near the 3-fold spike and residues 378 and 383 are near the edge of the 2-fold dimple, with 383 being nearer the surface. (a) van der Waals surface representation of these residues with the rest of the capsid shown as a C^a backbone trace. (b) Suface representation of all atoms in the capsid, with one subunit shown in orange.		Figure 5. Figure 5. Conservation of surface features of PPV relative to FPV and MVM. (a) PPV compared to FPV; (b) PPV compared to MVM, with red being the most conserved and blue being the most variable. Left stereo figures show surface views and right mono figures show central cross-sections. Symmetry axes are shown in white.

Figures were selected by an automated process.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20484503

M.Boisvert, S.Fernandes, and P.Tijssen (2010).
Multiple pathways involved in porcine parvovirus cellular entry and trafficking toward the nucleus.

J Virol, 84, 7782-7792.

19634175

C.L.Heldt, P.V.Gurgel, L.A.Jaykus, and R.G.Carbonell (2009).
Influence of peptide ligand surface density and ethylene oxide spacer arm on the capture of porcine parvovirus.

Biotechnol Prog, 25, 1411-1418.

19437101

Z.Y.Wei, X.B.Wang, X.D.Ning, Y.B.Wang, H.Y.Zhang, D.F.Wang, H.Y.Chen, and B.A.Cui (2009).
Nitric oxide inhibits the replication cycle of porcine parvovirus in vitro.

Arch Virol, 154, 999.

18508892

B.Kaufmann, P.R.Chipman, V.A.Kostyuchenko, S.Modrow, and M.G.Rossmann (2008).
Visualization of the externalized VP2 N termini of infectious human parvovirus B19.

J Virol, 82, 7306-7312.

18491385

M.Carrillo-Tripp, C.L.Brooks, and V.S.Reddy (2008).
A novel method to map and compare protein-protein interactions in spherical viral capsids.

Proteins, 73, 644-655.

18367523

N.DiPrimio, A.Asokan, L.Govindasamy, M.Agbandje-McKenna, and R.J.Samulski (2008).
Surface loop dynamics in adeno-associated virus capsid assembly.

J Virol, 82, 5178-5189.

17626084

B.Kaufmann, A.López-Bueno, M.G.Mateu, P.R.Chipman, C.D.Nelson, C.R.Parrish, J.M.Almendral, and M.G.Rossmann (2007).
Minute virus of mice, a parvovirus, in complex with the Fab fragment of a neutralizing monoclonal antibody.

J Virol, 81, 9851-9858.

17393085

L.Cheng, S.Chen, Z.H.Zhou, and J.Zhang (2007).
Structure comparisons of Aedes albopictus densovirus with other parvoviruses.

Sci China C Life Sci, 50, 70-74.

16415031

A.López-Bueno, M.P.Rubio, N.Bryant, R.McKenna, M.Agbandje-McKenna, and J.M.Almendral (2006).
Host-selected amino acid changes at the sialic acid binding pocket of the parvovirus capsid modulate cell binding affinity and determine virulence.

J Virol, 80, 1563-1573.

17156442

L.Gilbert, J.Toivola, O.Välilehto, T.Saloniemi, C.Cunningham, D.White, A.R.Mäkelä, E.Korhonen, M.Vuento, and C.Oker-Blom (2006).
Truncated forms of viral VP2 proteins fused to EGFP assemble into fluorescent parvovirus-like particles.

J Nanobiotechnology, 4, 13.

15795290

E.Padron, V.Bowman, N.Kaludov, L.Govindasamy, H.Levy, P.Nick, R.McKenna, N.Muzyczka, J.A.Chiorini, T.S.Baker, and M.Agbandje-McKenna (2005).
Structure of adeno-associated virus type 4.

J Virol, 79, 5047-5058.

16103145

M.Kontou, L.Govindasamy, H.J.Nam, N.Bryant, A.L.Llamas-Saiz, C.Foces-Foces, E.Hernando, M.P.Rubio, R.McKenna, J.M.Almendral, and M.Agbandje-McKenna (2005).
Structural determinants of tissue tropism and in vivo pathogenicity for the parvovirus minute virus of mice.

J Virol, 79, 10931-10943.

PDB codes:

1z14 1z1c

14660623

A.Carreira, M.Menéndez, J.Reguera, J.M.Almendral, and M.G.Mateu (2004).
In vitro disassembly of a parvovirus capsid and effect on capsid stability of heterologous peptide insertions in surface loops.

J Biol Chem, 279, 6517-6525.

15289612

B.Kaufmann, A.A.Simpson, and M.G.Rossmann (2004).
The structure of human parvovirus B19.

Proc Natl Acad Sci U S A, 101, 11628-11633.

PDB code:

1s58

14981262

J.Reguera, A.Carreira, L.Riolobos, J.M.Almendral, and M.G.Mateu (2004).
Role of interfacial amino acid residues in assembly, stability, and conformation of a spherical virus capsid.

Proc Natl Acad Sci U S A, 101, 2724-2729.

14726513

S.Canaan, Z.Zádori, F.Ghomashchi, J.Bollinger, M.Sadilek, M.E.Moreau, P.Tijssen, and M.H.Gelb (2004).
Interfacial enzymology of parvovirus phospholipases A2.

J Biol Chem, 279, 14502-14508.

12552020

B.Hauck, and W.Xiao (2003).
Characterization of tissue tropism determinants of adeno-associated virus type 1.

J Virol, 77, 2768-2774.

12941411

K.Hueffer, and C.R.Parrish (2003).
Parvovirus host range, cell tropism and evolution.

Curr Opin Microbiol, 6, 392-398.

14581558

L.Govindasamy, K.Hueffer, C.R.Parrish, and M.Agbandje-McKenna (2003).
Structures of host range-controlling regions of the capsids of canine and feline parvoviruses and mutants.

J Virol, 77, 12211-12221.

PDB codes:

1p5w 1p5y

12970420

P.Tijssen, Y.Li, M.El-Far, J.Szelei, M.Letarte, and Z.Zádori (2003).
Organization and expression strategy of the ambisense genome of densonucleosis virus of Galleria mellonella.

J Virol, 77, 10357-10365.

12414944

H.G.Zhang, J.Xie, I.Dmitriev, E.Kashentseva, D.T.Curiel, H.C.Hsu, and J.D.Mountz (2002).
Addition of six-His-tagged peptide to the C terminus of adeno-associated virus VP3 does not affect viral tropism or production.

J Virol, 76, 12023-12031.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.