Human cyclophilin has a significantly higher affinity for HIV-1 recombinant p55 than p24

Article Abstract:

Cyclophilin appears to participate in the reproduction of HIV. Cyclophilin is a enzyme in human cells. It is believed to cut the p24 viral peptide by removing p17. Researchers measured the ability of cyclophilin to bind to various viral proteins. The enzyme became more strongly bound to the p24 protein when it contained the p17 amino acid sequence than it did to the p24 protein alone. This confirms that the enzyme binds to the p17-p24 amino acid sequence and then removes the p17 sequence. This step occurs when the virus reproduces.

Cyclophilin

---

HIV Tat protein requirements for transactivation and repression of transcription are separable

Article Abstract:

The Tat protein may have important and distinct effects on HIV replication and the immune response. Researchers found that the Tat protein, generated by the virus which causes HIV infection, promotes viral genetic transcription and, thus, virus replication. Another region of the protein may repress genetic transcription of the major histocompatibility complex, which may impair the ability of white blood cells to attack HIV infected cells.

Health aspects, HIV infection, HIV infections, Major histocompatibility complex

---

Similar abstracts:

• Abstracts: Stimulation of the CD2 receptor pathway induces apoptosis in human T lymphotropic virus type I-infected cell lines
• Abstracts: All for one, and one for all: Health visitors should stick to working with individuals if they really want to improve public health
• Abstracts: Philip Morris cigarettes recall, May 1995-March 1996. Ingestion of cigarettes and cigarette butts by children - Rhode Island, January 1994-July 1996
• Abstracts: Tobacco company rebuts its workers' affidavits. Bad deal: big tobacco wants to dodge FDA oversight, and do it on the cheap
• Abstracts: Mechanism of anti-HIV activity of negatively charged albumins: biomolecular interaction with the HIV-1 envelope protein gp120

This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.