scholarly journals Identification of a nonconventional motif necessary for the nuclear import of the human parvovirus B19 major capsid protein (VP2)

Virology ◽  
2003 ◽  
Vol 306 (1) ◽  
pp. 25-32 ◽  
Author(s):  
Sylvie Pillet ◽  
Zeinab Annan ◽  
Serge Fichelson ◽  
F.rédéric Morinet
Keyword(s):  
Capsid Protein ◽  
Nuclear Import ◽  
Major Capsid Protein ◽  
Parvovirus B19 ◽  
Human Parvovirus B19

scholarly journals Visualization of the Externalized VP2 N Termini of Infectious Human Parvovirus B19

2008 ◽  
Vol 82 (15) ◽  
pp. 7306-7312 ◽  
Author(s):  
Bärbel Kaufmann ◽  
Paul R. Chipman ◽  
Victor A. Kostyuchenko ◽  
Susanne Modrow ◽  
Michael G. Rossmann
Keyword(s):  
Capsid Protein ◽  
Major Capsid Protein ◽  
Parvovirus B19 ◽  
Icosahedral Symmetry ◽  
Human Parvovirus B19 ◽  
Wild Type ◽  
Rich Region ◽  
Structural Differences ◽  
Capsid Protein Vp1 ◽  
Viral Surface

ABSTRACT The structures of infectious human parvovirus B19 and empty wild-type particles were determined by cryoelectron microscopy (cryoEM) to 7.5-Å and 11.3-Å resolution, respectively, assuming icosahedral symmetry. Both of these, DNA filled and empty, wild-type particles contain a few copies of the minor capsid protein VP1. Comparison of wild-type B19 with the crystal structure and cryoEM reconstruction of recombinant B19 particles consisting of only the major capsid protein VP2 showed structural differences in the vicinity of the icosahedral fivefold axes. Although the unique N-terminal region of VP1 could not be visualized in the icosahedrally averaged maps, the N terminus of VP2 was shown to be exposed on the viral surface adjacent to the fivefold β-cylinder. The conserved glycine-rich region is positioned between two neighboring, fivefold-symmetrically related VP subunits and not in the fivefold channel as observed for other parvoviruses.

scholarly journals Down-Regulation of Na+/K+ATPase Activity by Human Parvovirus B19 Capsid Protein VP1

2013 ◽  
Vol 31 (4-5) ◽  
pp. 638-648 ◽  
Author(s):  
Ahmad Almilaji ◽  
Kalina Szteyn ◽  
Evelyn Fein ◽  
Tatsiana Pakladok ◽  
Carlos Munoz ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Capsid Protein ◽  
Parvovirus B19 ◽  
Human Parvovirus B19 ◽  
Down Regulation ◽  
Capsid Protein Vp1

Down-Regulation of Inwardly Rectifying Kir2.1 K+ Channels by Human Parvovirus B19 Capsid Protein VP1

2014 ◽  
Vol 248 (2) ◽  
pp. 223-229 ◽  
Author(s):  
Musaab Ahmed ◽  
Bernat Elvira ◽  
Ahmad Almilaji ◽  
C.-Thomas Bock ◽  
Reinhard Kandolf ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Parvovirus B19 ◽  
Human Parvovirus B19 ◽  
Down Regulation ◽  
K Channels ◽  
Capsid Protein Vp1 ◽  
Inwardly Rectifying

scholarly journals The VP1u of Human Parvovirus B19: A Multifunctional Capsid Protein with Biotechnological Applications

Viruses ◽  
2020 ◽  
Vol 12 (12) ◽  
pp. 1463
Author(s):  
Carlos Ros ◽  
Jan Bieri ◽  
Remo Leisi
Keyword(s):  
Capsid Protein ◽  
Neutralizing Antibodies ◽  
Parvovirus B19 ◽  
Membrane Receptors ◽  
Endosomal Escape ◽  
Erythroid Cell ◽  
Human Parvovirus B19 ◽  
Unique Region ◽  
Differentiation Stage ◽  
Viral Protein 1

The viral protein 1 unique region (VP1u) of human parvovirus B19 (B19V) is a multifunctional capsid protein with essential roles in virus tropism, uptake, and subcellular trafficking. These functions reside on hidden protein domains, which become accessible upon interaction with cell membrane receptors. A receptor-binding domain (RBD) in VP1u is responsible for the specific targeting and uptake of the virus exclusively into cells of the erythroid lineage in the bone marrow. A phospholipase A2 domain promotes the endosomal escape of the incoming virus. The VP1u is also the immunodominant region of the capsid as it is the target of neutralizing antibodies. For all these reasons, the VP1u has raised great interest in antiviral research and vaccinology. Besides the essential functions in B19V infection, the remarkable erythroid specificity of the VP1u makes it a unique erythroid cell surface biomarker. Moreover, the demonstrated capacity of the VP1u to deliver diverse cargo specifically to cells around the proerythroblast differentiation stage, including erythroleukemic cells, offers novel therapeutic opportunities for erythroid-specific drug delivery. In this review, we focus on the multifunctional role of the VP1u in B19V infection and explore its potential in diagnostics and erythroid-specific therapeutics.

scholarly journals Unique region of the minor capsid protein of human parvovirus B19 is exposed on the virion surface.

1992 ◽  
Vol 89 (6) ◽  
pp. 2023-2029 ◽  
Author(s):  
S J Rosenfeld ◽  
K Yoshimoto ◽  
S Kajigaya ◽  
S Anderson ◽  
N S Young ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Parvovirus B19 ◽  
Human Parvovirus B19 ◽  
Unique Region ◽  
Minor Capsid Protein ◽  
Virion Surface

Down-regulation of K+ channels by human parvovirus B19 capsid protein VP1

2014 ◽  
Vol 450 (4) ◽  
pp. 1396-1401 ◽  
Author(s):  
Musaab Ahmed ◽  
Ahmad Almilaji ◽  
Carlos Munoz ◽  
Bernat Elvira ◽  
Ekaterina Shumilina ◽  
...  
Keyword(s):  
Capsid Protein ◽  
Parvovirus B19 ◽  
Human Parvovirus B19 ◽  
Down Regulation ◽  
K Channels ◽  
Capsid Protein Vp1

scholarly journals Nuclear Import Strategies of High Risk HPV16 L1 Major Capsid Protein

2002 ◽  
Vol 277 (26) ◽  
pp. 23958-23964 ◽  
Author(s):  
Lisa M. Nelson ◽  
Robert C. Rose ◽  
Junona Moroianu
Keyword(s):  
High Risk ◽  
Capsid Protein ◽  
Nuclear Import ◽  
Major Capsid Protein

scholarly journals Phospholipase A2 Activity-Dependent Stimulation of Ca2+ Entry by Human Parvovirus B19 Capsid Protein VP1

2006 ◽  
Vol 80 (22) ◽  
pp. 11370-11380 ◽  
Author(s):  
Adrian Lupescu ◽  
C.-Thomas Bock ◽  
Philipp A. Lang ◽  
Susanne Aberle ◽  
Heike Kaiser ◽  
...  
Keyword(s):  
Endothelial Dysfunction ◽  
Phospholipase A2 ◽  
Capsid Protein ◽  
Parvovirus B19 ◽  
Eukaryotic Expression ◽  
Expression Vectors ◽  
Human Parvovirus B19 ◽  
Pla2 Activity ◽  
Unique Region ◽  
The Impact

ABSTRACT Recent reports demonstrated an association of human parvovirus B19 with inflammatory cardiomyopathy (iCMP), which is accompanied by endothelial dysfunction. As intracellular Ca2+ activity is a key regulator of cell function and participates in mechanisms leading to endothelial dysfunction, the present experiments explored the effects of the B19 capsid proteins VP1 and VP2. A secreted phospholipase A2 (PLA2)-like activity has been located in the VP1 unique region of the B19 minor capsid protein. As PLA2 has recently been shown to activate the store-operated or capacitative Ca2+ channel ICRAC, we analyzed the impact of the viral PLA2 motif on Ca2+ entry. We cloned the VP1 and VP2 genes isolated from a patient suffering from fatal B19 iCMP into eukaryotic expression vectors. We also generated a B19 replication-competent plasmid to demonstrate PLA2 activity under the control of the complete B19 genome. After the transfection of human endothelial cells (HMEC-1), cytosolic Ca2+ activity was determined by utilizing Fura-2 fluorescence. VP1 and VP2 expression did not significantly modify basal cytosolic Ca2+ activity or the decline of cytosolic Ca2+ activity following the removal of extracellular Ca2+. However, expression of VP1 and of the full-length B19 clone, but not of VP2, significantly accelerated the increase of cytosolic Ca2+ activity following the readdition of extracellular Ca2+ in the presence of thapsigargin, indicating an activation of ICRAC. The effect of VP1 was mimicked by the PLA2 product lysophosphatidylcholine and abolished by an inactivating mutation of the PLA2-encoding region of the VP1 gene. Our observations point to the activation of Ca2+ entry by VP1 PLA2 activity, an effect likely participating in the pathophysiology of B19 infection.

Sign in / Sign up

Export Citation Format

Share Document