BIOMAT Database Logo BIOMAT Database Logo

Unique region of the minor capsid protein of human parvovirus B19 is exposed on the virion surface. 1992

S J Rosenfeld, and K Yoshimoto, and S Kajigaya, and S Anderson, and N S Young, and A Field, and P Warrener, and G Bansal, and M S Collett
Cell Biology Section, National Heart, Lung and Blood Institute, Bethesda, Maryland 20817.

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.

UI MeSH Term Description Entries
D008854 Microscopy, Electron Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen. Electron Microscopy
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009838 Oligodeoxyribonucleotides A group of deoxyribonucleotides (up to 12) in which the phosphate residues of each deoxyribonucleotide act as bridges in forming diester linkages between the deoxyribose moieties. Oligodeoxynucleotide,Oligodeoxyribonucleotide,Oligodeoxynucleotides
D011233 Precipitin Tests Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate. Precipitin Test,Test, Precipitin,Tests, Precipitin
D002213 Capsid The outer protein protective shell of a virus, which protects the viral nucleic acid. Capsids are composed of repeating units (capsomers or capsomeres) of CAPSID PROTEINS which when assembled together form either an icosahedral or helical shape. Procapsid,Prohead,Capsids,Procapsids,Proheads
D002460 Cell Line Established cell cultures that have the potential to propagate indefinitely. Cell Lines,Line, Cell,Lines, Cell
D004797 Enzyme-Linked Immunosorbent Assay An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed. ELISA,Assay, Enzyme-Linked Immunosorbent,Assays, Enzyme-Linked Immunosorbent,Enzyme Linked Immunosorbent Assay,Enzyme-Linked Immunosorbent Assays,Immunosorbent Assay, Enzyme-Linked,Immunosorbent Assays, Enzyme-Linked
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D000914 Antibodies, Viral Immunoglobulins produced in response to VIRAL ANTIGENS. Viral Antibodies

Related Publications

S J Rosenfeld, and K Yoshimoto, and S Kajigaya, and S Anderson, and N S Young, and A Field, and P Warrener, and G Bansal, and M S Collett
Most of the VP1 unique region of B19 parvovirus is on the capsid surface.
August 1995, Virology,
S J Rosenfeld, and K Yoshimoto, and S Kajigaya, and S Anderson, and N S Young, and A Field, and P Warrener, and G Bansal, and M S Collett
Peptides derived from the unique region of B19 parvovirus minor capsid protein elicit neutralizing antibodies in rabbits.
January 1995, Virology,
S J Rosenfeld, and K Yoshimoto, and S Kajigaya, and S Anderson, and N S Young, and A Field, and P Warrener, and G Bansal, and M S Collett
The Effect of a Unique Region of Parvovirus B19 Capsid Protein VP1 on Endothelial Cells.
April 2021, Biomolecules,
S J Rosenfeld, and K Yoshimoto, and S Kajigaya, and S Anderson, and N S Young, and A Field, and P Warrener, and G Bansal, and M S Collett
Activation of synoviocytes by the secreted phospholipase A2 motif in the VP1-unique region of parvovirus B19 minor capsid protein.
February 2006, The Journal of infectious diseases,
S J Rosenfeld, and K Yoshimoto, and S Kajigaya, and S Anderson, and N S Young, and A Field, and P Warrener, and G Bansal, and M S Collett
Nuclear export of the nonenveloped parvovirus virion is directed by an unordered protein signal exposed on the capsid surface.
October 2004, Journal of virology,
S J Rosenfeld, and K Yoshimoto, and S Kajigaya, and S Anderson, and N S Young, and A Field, and P Warrener, and G Bansal, and M S Collett
Effects of human parvovirus B19 VP1 unique region protein on macrophage responses.
January 2009, Journal of biomedical science,
S J Rosenfeld, and K Yoshimoto, and S Kajigaya, and S Anderson, and N S Young, and A Field, and P Warrener, and G Bansal, and M S Collett
Formation of empty B19 parvovirus capsids by the truncated minor capsid protein.
July 1994, Journal of virology,
S J Rosenfeld, and K Yoshimoto, and S Kajigaya, and S Anderson, and N S Young, and A Field, and P Warrener, and G Bansal, and M S Collett
[Genetic diversity of human Parvovirus B19 VP1 unique region].
February 2003, Zhonghua er ke za zhi = Chinese journal of pediatrics,
S J Rosenfeld, and K Yoshimoto, and S Kajigaya, and S Anderson, and N S Young, and A Field, and P Warrener, and G Bansal, and M S Collett
B cell memory is directed toward conformational epitopes of parvovirus B19 capsid proteins and the unique region of VP1.
May 2004, The Journal of infectious diseases,
S J Rosenfeld, and K Yoshimoto, and S Kajigaya, and S Anderson, and N S Young, and A Field, and P Warrener, and G Bansal, and M S Collett
Modest truncation of the major capsid protein abrogates B19 parvovirus capsid formation.
October 1995, Journal of virology,
Copied contents to your clipboard!