Palmitoylation and p8-Mediated Human T-Cell Leukemia Virus Type 1 Transmission

Dustin Edwards, Risaku Fukumoto, Maria Fernanda de Castro-Amarante, Luiz Carlos Junior Alcantara, Bernardo Galvão-Castro, Robyn Washington Parks, Cynthia Pise-Masison, Genoveffa Franchini

2014publishedJournal of Virologyvolume 88, issue 4, pages 2319-232210.1128/jvi.03444-13doiopen accesslicense

Cited by 12 OpenAlex, read 2026-10-01

Mutating cysteine 39 stops HTLV-1 p8 and p12 from dimerizing and being palmitoylated, but p8 still reaches the cell surface and spreads the virus.

Abstract

The orf-I gene of human T-cell leukemia type 1 (HTLV-1) encodes p8 and p12 and has a conserved cysteine at position 39. p8 and p12 form disulfide-linked dimers, and only the monomeric forms of p8 and p12 are palmitoylated. Mutation of cysteine 39 to alanine (C39A) abrogated dimerization and palmitoylation of both proteins. However, the ability of p8 to localize to the cell surface and to increase cell adhesion and viral transmission was not affected by the C39A mutation.

Cited by 12

OpenAlex, read 2026-09-12. Newest first.

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  2. HTLV-1 p12 is cleaved to p8 by the signal peptidase complex and its inhibition impairs p8-dependent transmission, PLoS Pathogens, 2025
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  10. First report of HTLV-1 truncated p12 protein in Brazil, Virulence, 2016
  11. Molecular Mechanisms of HTLV-1 Cell-to-Cell Transmission, Viruses, 2016
  12. Co-dependence of HTLV-1 p12 and p8 Functions in Virus Persistence, PLoS Pathogens, 2014

Human and simian retroviruses