Analysis of the functional compatibility of SIV capsid sequences in the context of the FIV gag precursor
| Autor: | José L. Affranchino, Silvia A. González, César A. Ovejero |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
RNA viruses Serum Proteins animal diseases viruses lcsh:Medicine Pathology and Laboratory Medicine Biochemistry VIRAL ASSEMBLY law.invention Virions purl.org/becyt/ford/1 [https] Database and Informatics Methods Immunodeficiency Viruses law Chlorocebus aethiops Medicine and Health Sciences lcsh:Science Peptide sequence Multidisciplinary virus diseases Transfection Poxviruses Vaccinia Virus Recombinant Proteins Capsid SIV Medical Microbiology Viral Pathogens COS Cells Viruses Recombinant DNA Simian Immunodeficiency Virus GAG POLYPROTEIN Pathogens Sequence Analysis CIENCIAS NATURALES Y EXACTAS Research Article Bioinformatics Otras Ciencias Biológicas Gene Products gag Biology Immunodeficiency Virus Feline Viral Structure Research and Analysis Methods Microbiology Virus Ciencias Biológicas 03 medical and health sciences Sequence Motif Analysis Virology Retroviruses Extracellular Animals purl.org/becyt/ford/1.6 [https] Microbial Pathogens lcsh:R Lentivirus Organisms Biology and Life Sciences Proteins HIV Gag Polyprotein Fiv FIV 030104 developmental biology HIV-1 lcsh:Q Capsid Proteins DNA viruses Linker |
| Zdroj: | CONICET Digital (CONICET) Consejo Nacional de Investigaciones Científicas y Técnicas instacron:CONICET PLoS ONE PLoS ONE, Vol 12, Iss 5, p e0177297 (2017) |
| DOI: | 10.1371/journal.pone.0177297 |
| Popis: | The formation of immature lentiviral particles is dependent on the multimerization of the Gag polyprotein at the plasma membrane of the infected cells. One key player in the virus assembly process is the capsid (CA) domain of Gag, which establishes the protein-protein interactions that give rise to the hexagonal lattice of Gag molecules in the immature virion. To gain a better understanding of the functional equivalence between the CA proteins of simian and feline immunodeficiency viruses (SIV and FIV, respectively), we generated a series of chimeric FIV Gag proteins in which the CA-coding region was partially or totally replaced by its SIV counterpart. All the FIV Gag chimeras were found to be assembly-defective; however, all of them are able to interact with wild-type SIV Gag and be recruited into extracellular virus-like particles, regardless of the SIV CA sequences present in the chimeric FIV Gag. The results presented here markedly contrast with our previous findings showing that chimeric SIVs carrying FIV CA-derived sequences are assembly-competent. Overall, our data support the notion that although the SIV and FIV CA proteins share 51% amino acid sequence similarity and exhibit a similar organization, i.e., an N-terminal domain joined by a flexible linker to a C-terminal domain, their functional exchange between these different lentiviruses is strictly dependent on the context of the recipient Gag precursor. Fil: Ovejero, César Antonio. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales. Laboratorio de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Affranchino, Jose Luis. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales. Laboratorio de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Gonzalez, Silvia Adriana. Universidad de Belgrano. Facultad de Ciencias Exactas y Naturales. Laboratorio de Virología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina |
| Databáze: | OpenAIRE |
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