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Gene Review

H3L  -  H3L

Monkeypox virus Zaire-96-I-16

 
 
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Disease relevance of H3L

  • In the present study, we have analyzed the sequences of H3L, A27L, and D8L gene-homologues of VACV in BPXV to elucidate its genetic relationship to VACV and other orthopoxviruses (OPVs) [1].
  • Effects of deletion or stringent repression of the H3L envelope gene on vaccinia virus replication [2].
  • IMV from the H3L(-) mutant virus are somewhat altered and less infectious than wild-type virions [3].
  • Mice inoculated intranasally with wild-type virus show high mortality and severe weight loss, whereas mice infected with H3L(-) mutant virus survive and recover faster, indicating that inactivation of the H3L gene attenuates virus virulence in vivo [3].
  • Together, these data show that H3L is a major target of the human anti-poxvirus antibody response and is likely to be a key contributor to protection against poxvirus infection and disease [4].
 

High impact information on H3L

  • Mice also make an immunodominant antibody response to H3L after vaccination with vaccinia virus, as determined by vaccinia virus protein microarray [4].
  • Finally, mutant viruses lacking the H3L, D8L, or A27L protein remained associated with lipid rafts, indicating that the initial attachment of vaccinia virions through glycosaminoglycans is not required for lipid raft formation [5].
  • The H3L protein, synthesized in a coupled in vitro transcription/translation system, was tightly anchored to membranes as determined by resistance to Na(2)CO(3) (pH 11) extraction and cytoplasmically oriented as shown by sensitivity to proteinase K digestion [6].
  • The phenotypes of the H3L deletion and repression mutants were identical to each other but differed from those produced by null mutations of genes encoding other vaccinia virus membrane components [2].
  • However, cells infected by the mutant virus form multinucleated syncytia after low pH treatment, suggesting that H3L protein is not required for cell fusion [3].
 

Chemical compound and disease context of H3L

  • In summary, these data indicate that H3L protein mediates vaccinia virus adsorption to cell surface heparan sulfate and is important for vaccinia virus infection in vitro and in vivo [3].
 

Biological context of H3L

  • Additionally, the A27L gene is also responsible for cell fusion during infection, while the H3L gene is required for synthesis of the highly immunogenic major envelope protein p35 [1].
  • Full-length nucleotide sequences of H3L, A27L, and D8L genes of three BPXV isolates were determined by PCR amplification, cloning, and sequencing [1].
  • The C-terminal membrane anchor protein encoded by the H3L open reading frame of vaccinia virus is located on the surfaces of intracellular mature virions [2].
  • The defect in vH3i replication could not be attributed to a role of the H3L protein in virus binding, internalization, or any event prior to late gene expression [2].
  • Virion morphogenesis is severely blocked and intermediate viral structures such as viral factories and crescents accumulate in cells infected with the H3L(-) mutant virus [3].
 

Anatomical context of H3L

  • Biochemical and microscopic studies demonstrated that the H3L protein was expressed late in infection, accumulated in the cytoplasmic viral factory regions, and associated primarily with amorphous material near immature virions and with intracellular virion membranes [6].
  • These data indicated that the H3L protein is a member of the C-terminal anchor family and supported a model in which it is synthesized on free ribosomes and inserts into the membranes of viral particles during their maturation [6].
 

Other interactions of H3L

  • This preceded a short ORF tentatively designated as F1L and predicted to be the beginning of a homologue of VAC H3L [7].
  • To develop diagnostic tests based on recombinant material, we cloned and sequenced a 3.7 kb viral DNA fragment of SPV that contained open reading frames homologous to the vaccinia virus J6R, H1L, H2R, H3L and H4L genes [8].

References

  1. Comparative sequence analysis of envelope protein genes of Indian buffalopox virus isolates. Singh, R.K., Hosamani, M., Balamurugan, V., Satheesh, C.C., Rasool, T.J., Yadav, M.P. Arch. Virol. (2006) [Pubmed]
  2. Effects of deletion or stringent repression of the H3L envelope gene on vaccinia virus replication. da Fonseca, F.G., Wolffe, E.J., Weisberg, A., Moss, B. J. Virol. (2000) [Pubmed]
  3. Vaccinia virus envelope H3L protein binds to cell surface heparan sulfate and is important for intracellular mature virion morphogenesis and virus infection in vitro and in vivo. Lin, C.L., Chung, C.S., Heine, H.G., Chang, W. J. Virol. (2000) [Pubmed]
  4. Vaccinia virus H3L envelope protein is a major target of neutralizing antibodies in humans and elicits protection against lethal challenge in mice. Davies, D.H., McCausland, M.M., Valdez, C., Huynh, D., Hernandez, J.E., Mu, Y., Hirst, S., Villarreal, L., Felgner, P.L., Crotty, S. J. Virol. (2005) [Pubmed]
  5. Vaccinia virus penetration requires cholesterol and results in specific viral envelope proteins associated with lipid rafts. Chung, C.S., Huang, C.Y., Chang, W. J. Virol. (2005) [Pubmed]
  6. Characterization of the vaccinia virus H3L envelope protein: topology and posttranslational membrane insertion via the C-terminal hydrophobic tail. da Fonseca, F.G., Wolffe, E.J., Weisberg, A., Moss, B. J. Virol. (2000) [Pubmed]
  7. Conservation of gene structure and arrangement between vaccinia virus and orf virus. Fleming, S.B., Blok, J., Fraser, K.M., Mercer, A.A., Robinson, A.J. Virology (1993) [Pubmed]
  8. A capripoxvirus detection PCR and antibody ELISA based on the major antigen P32, the homolog of the vaccinia virus H3L gene. Heine, H.G., Stevens, M.P., Foord, A.J., Boyle, D.B. J. Immunol. Methods (1999) [Pubmed]
 
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