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

Autor:	Cynthia A. Pise-Masison, Dustin Edwards, Genoveffa Franchini, Robyn Washington Parks, Risaku Fukumoto, Luiz Carlos Junior Alcantara, Bernardo Galvão-Castro, Maria Fernanda de Castro-Amarante
Rok vydání:	2014
Předmět:	Lipoylation viruses Immunoblotting Molecular Sequence Data Immunology Mutation Missense Mutagenesis (molecular biology technique) Biology medicine.disease_cause Microbiology Palmitoylation hemic and lymphatic diseases Virology medicine Humans Immunoprecipitation Viral Regulatory and Accessory Proteins Amino Acid Sequence Cell adhesion DNA Primers Alanine Human T-lymphotropic virus 1 Mutation HEK 293 cells medicine.disease HTLV-I Infections Molecular biology Genome Replication and Regulation of Viral Gene Expression Protein Subunits Protein Transport Leukemia HEK293 Cells Mutagenesis Insect Science Dimerization Cysteine
Zdroj:	Journal of Virology. 88:2319-2322
ISSN:	1098-5514 0022-538X
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af74631311baa2b133c76bb9f3ec56af https://doi.org/10.1128/jvi.03444-13 Zobrazit plný text záznamu