2026-06-14T03:29:38Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/69652025-06-09T13:50:43Zcom_20.500.12105_2052com_20.500.12105_2051col_20.500.12105_19609
Repisalud
author
Lopez-Huertas, Maria Rosa
author
Callejas, S.
author
Abia, David
author
Mateos, Elena
author
Dopazo, A.
author
Alcamí, José
author
Coiras, Mayte
funder
Plan Nacional sobre el Sida (España)
funder
Fundación para la Investigación y la Prevención del Sida en España
funder
Comunidad de Madrid (España)
funder
Instituto de Salud Carlos III
funder
Ministerio de Ciencia e Innovación (España)
2018-12-27T11:33:01Z
2018-12-27T11:33:01Z
2010-02-05
Nucleic Acids Res. 2010;38(10):3287-307
10.1093/nar/gkq037
1362-4962
0305-1048
Nucleic Acids Research
20139419
http://hdl.handle.net/20.500.12105/6965
The human immunodeficiency virus type 1 (HIV-1) regulator Tat is essential for viral replication because it achieves complete elongation of viral transcripts. Tat can be released to the extracellular space and taken up by adjacent cells, exerting profound cytoskeleton rearrangements that lead to apoptosis. In contrast, intracellular Tat has been described as protector from apoptosis. Tat gene is composed by two coding exons that yield a protein of 101 amino acids (aa). First exon (1-72aa) is sufficient for viral transcript elongation and second exon (73-101 aa) appears to contribute to non-transcriptional functions. We observed that Jurkat cells stably expressing intracellular Tat101 showed gene expression deregulation 4-fold higher than cells expressing Tat72. Functional experiments were performed to evaluate the effect of this deregulation. First, NF-kappaB-, NF-AT- and Sp1-dependent transcriptional activities were greatly enhanced in Jurkat-Tat101, whereas Tat72 induced milder but efficient activation. Second, cytoskeleton-related functions as cell morphology, proliferation, chemotaxis, polarization and actin polymerization were deeply altered in Jurkat-Tat101, but not in Jurkat-Tat72. Finally, expression of several cell surface receptors was dramatically impaired by intracellular Tat101 but not by Tat72. Consequently, these modifications were greatly dependent on Tat second exon and they could be related to the anergy observed in HIV-1-infected T cells.
eng
Modifications in host cell cytoskeleton structure and function mediated by intracellular HIV-1 Tat protein are greatly dependent on the second coding exon
research article
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URL
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File
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application/pdf
ModificationsInHostCell_2010.pdf
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https://repisalud.isciii.es/bitstreams/6f7d3b0c-3fff-4133-bb9a-abc4308bdf2b/download
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text/plain
ModificationsInHostCell_2010.pdf.txt