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Amendment history:
  • Correction (December 1992)

Research Article Free access | 10.1172/JCI115812

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

S J Rosenfeld, K Yoshimoto, S Kajigaya, S Anderson, N S Young, A Field, P Warrener, G Bansal, and M S Collett

Cell Biology Section, National Heart, Lung and Blood Institute, Bethesda, Maryland 20817.

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Cell Biology Section, National Heart, Lung and Blood Institute, Bethesda, Maryland 20817.

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Cell Biology Section, National Heart, Lung and Blood Institute, Bethesda, Maryland 20817.

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Cell Biology Section, National Heart, Lung and Blood Institute, Bethesda, Maryland 20817.

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Cell Biology Section, National Heart, Lung and Blood Institute, Bethesda, Maryland 20817.

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Cell Biology Section, National Heart, Lung and Blood Institute, Bethesda, Maryland 20817.

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Cell Biology Section, National Heart, Lung and Blood Institute, Bethesda, Maryland 20817.

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Cell Biology Section, National Heart, Lung and Blood Institute, Bethesda, Maryland 20817.

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Cell Biology Section, National Heart, Lung and Blood Institute, Bethesda, Maryland 20817.

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Published June 1, 1992 - More info

Published in Volume 89, Issue 6 on June 1, 1992
J Clin Invest. 1992;89(6):2023–2029. https://doi.org/10.1172/JCI115812.
© 1992 The American Society for Clinical Investigation
Published June 1, 1992 - Version history
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Abstract

Capsids of the B19 parvovirus are composed of major (VP2; 58 kD) and minor (VP1; 83 kD) structural proteins. These proteins are identical except for a unique 226 amino acid region at the amino terminus of VP1. Previous immunization studies with recombinant empty capsids have demonstrated that the presence of VP1 was required to elicit virus-neutralizing antibody activity. However, to date, neutralizing epitopes have been identified only on VP2. Crystallographic studies of a related parvovirus (canine parvovirus) suggested the unique amino-terminal portion of VP1 assumed an internal position within the viral capsid. To determine the position of VP1 in both empty capsids and virions, we expressed a fusion protein containing the unique region of VP1. Antisera raised to this protein recognized recombinant empty capsids containing VP1 and VP2, but not those containing VP2 alone, in an enzyme-linked immunosorbent assay. The antisera immunoprecipitated both recombinant empty capsids and human plasma-derived virions, and agglutinated the latter as shown by immune electron microscopy. The sera contained potent neutralizing activity for virus infectivity in vitro. These data indicate that a portion of the amino terminus of VP1 is located on the virion surface, and that this region contains intrinsic neutralizing determinants. The external location of the VP1-specific tail may provide a site for engineered heterologous epitope presentation in novel recombinant vaccines.

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