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Gene Review

HPIV3gp1  -  nucleocapsid protein

Human parainfluenza virus 3

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Disease relevance of HPIV3gp1


High impact information on HPIV3gp1

  • Mapping of the domains in P (603 amino acids) involved in the association with NP revealed that NH2-terminal 40 and COOH-terminal 20 amino acids are important for such association [1].
  • Reconstitution with the soluble protein fraction was necessary for genome RNA replication and nucleocapsid assembly [2].
  • RNA editing was found to occur in both in vivo (HPIV3 infected cells) and in vitro (purified nucleocapsid complexes) synthesized mRNAs [4].
  • In spinal ganglion cells the internal, cytosolic viral proteins (the nucleocapsid, polymerase and matrix proteins) were confined to the perikarya, while the envelope glycoproteins (the haemagglutinin-neuraminidase and fusion proteins) also appeared in the axon-like processes [5].
  • The 3' non-coding regions of the nucleocapsid (NP) and M genes were completely conserved in contrast to the polymerase (L) gene in which 25% of the nucleotides were different [6].

Associations of HPIV3gp1 with chemical compounds

  • Deletion of NH2-terminal 40 and COOH-terminal 160 amino acids of NP reduced the CAT activity by more than 95% [1].

Analytical, diagnostic and therapeutic context of HPIV3gp1

  • Persistently infected cell cultures were established after low multiplicity infection with HPF3 in the presence of exogenous bacterial neuraminidase, and viral nucleocapsid RNA was analyzed for the presence of DI genomes at each passage after infection [7].


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