3rd Conference on Retroviruses and Opportunistic Infections


Washington, DC - January 28-February 1, 1996


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ANTI-APOPTOTIC PROTEIN BCL-2 SHARES STRUCTURAL HOMOLOGY WITH HIV-1 NEF.

Conf Retroviruses Opportunistic Infect 1996 Jan 28-Feb 1; 3rd:62 (abstract no. 49)

Ranganathan PN, Croce CM, Srinivasan A Thomas Jefferson University, Philadelphia, PA 19107


Comparison of Bcl-2 with nef protein of HIV-1 revealed common biochemical properties. While nef proteins from various HIV-1 isolates showed 70-80% amino acid identities, members of Bcl-2 family exhibited identities of only 26-44%. Based on the assumption that similar biochemical properties may reflect similarities at the primary structure level, a search for amino acid homologies between Bcl-2 and various nef proteins was performed. This led to the following observations: 39-44% similarity between nef and Bcl-2 that is comparable to values exhibited among certain Bcl-2 family members; presence of structurally and/or functionally important protein kinase C and caesin kinase II motifs, block of identical residues at the amino terminus, proline-rich segments/repeats and invariant residues common to both. Interestingly, four highly conserved nef-defining, consensus blocks shared high sequence homology with Bcl-2 and two of these blocks also sharedidentical predicted secondary structure with their Bcl-2 counterparts. These observations raise the possibility of one or more functions being common to Bcl-2 and nef.

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Copyright © 1996 - Foundation for Retrovirology and Human Health . Reproduction of this abstract (other than one copy for personal reference) must be cleared through the Foundation for Retrovirology and Human Health.