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Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
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Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus

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Modest truncation of the major capsid protein abrogates B19 parvovirus capsid formation

M Kawase1, M Momoeda, N S Young

  • 1Hematology Branch, National Heart, Lung, and Blood Institute, Bethesda, Maryland 20892, USA.

Journal of Virology
|October 1, 1995
PubMed

Insights

The major capsid protein (VP2) NH2-terminal region is crucial for B19 parvovirus assembly. Truncations beyond amino acid 30 disrupt capsid formation, impacting viral structure and immune response.

Area of Science:

  • Virology
  • Structural Biology
  • Immunology

Background:

  • The B19 parvovirus capsid structure is essential for its infectivity and immune response.
  • Specific regions of capsid proteins, including the minor capsid protein (VP1) unique region and the VP1-VP2 junction, are implicated in immune evasion.
  • The role of the NH2-terminal region of the major capsid protein (VP2) in B19 parvovirus capsid assembly remains incompletely understood.

Purpose of the Study:

  • To elucidate the role of the NH2-terminal region of the B19 parvovirus VP2 protein in capsid structure and assembly.
  • To determine the critical amino acid residues and structural elements within the VP2 NH2-terminus required for proper viral particle formation.

Main Methods:

  • Expression and analysis of progressively truncated VP2 gene variants.
  • Immunoblotting to detect and characterize VP2 protein fragments.
  • Electron microscopy to visualize capsid assembly and structure.
  • Density gradient centrifugation for purification of viral particles.

Main Results:

  • Deletion of the first 25 amino acids (aa) of VP2 did not impede capsid self-assembly.
  • Truncations affecting amino acids 26-30, including a single amino acid deletion at position 25, abolished VP2 self-assembly but allowed incorporation into existing capsids.
  • Further truncations beyond aa 30 prevented both self-assembly and co-assembly, indicating the loss of essential structural domains.
  • The critical region for assembly involves the beta A and beta B antiparallel strands.

Conclusions:

  • The NH2-terminal region of B19 parvovirus VP2, specifically beyond amino acid 30, is indispensable for proper capsid assembly.
  • The beta B strand appears to be a key structural component for viral core formation and assembly.
  • Understanding these structural requirements can inform strategies targeting B19 parvovirus infectivity and immune interactions.

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