Abstract
The genome of the human immunodeficiency virus (HIV) contains several open reading frames (ORFs) not present in other viruses. The 'A' gene1, also known as Q2P'3, ORF-14 or sor5, partially overlaps the pol gene; its protein product has a relative molecular mass of 23,000 (Mr 23K) and is present in productively infected cells7–10. The function of this protein is unclear; mutant viruses deleted in 'A' replicate in and kill CD4+ lymphocyte lines8, but the high degree of conservation of the deduced amino-acid sequence in nine different HIV isolates (80%) and the presence of analogous genes in HIV-211 and other lentiviruses suggest that the gene function is an important one. Here we describe a mutant virus deficient in the 'A' gene which produces virion particles normally; however, the particles are & sm;1,000 times less infective than wild type. Transcomplementation experiments partially restore infectivity. The mutant virus spreads efficiently when virus-producing cells are co-cultivated with CD4+ lymphocytes, however, indicating that HIV can spread from cell to cell in a mechanism that does not require the 'A' gene product and probably does not require the production of infective virus particles.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Strebel, K., Daugherty, D., Clouse, K. et al. The HIV A (sor) gene product is essential for virus infectivity. Nature 328, 728–730 (1987). https://doi.org/10.1038/328728a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/328728a0
This article is cited by
-
Dimerization regulates both deaminase-dependent and deaminase-independent HIV-1 restriction by APOBEC3G
Nature Communications (2017)
-
Intrinsic host restrictions to HIV-1 and mechanisms of viral escape
Nature Immunology (2015)
-
HIV-1 Vif inhibits G to A hypermutations catalyzed by virus-encapsidated APOBEC3G to maintain HIV-1 infectivity
Retrovirology (2014)
-
Oligomerization transforms human APOBEC3G from an efficient enzyme to a slowly dissociating nucleic acid-binding protein
Nature Chemistry (2014)
-
Protein intrinsic disorder as a flexible armor and a weapon of HIV-1
Cellular and Molecular Life Sciences (2012)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.