Chaperoning a Pathogen

Important note: Information in this article was accurate in 1994. The state of the art may have changed since the publication date.

Chaperoning a Pathogen

Nature (11/24/94) Vol. 372, No. 6504, P. 319
Cullen, Brian R.; Heitman, Joseph

Studies conducted by Franke et al and Thali et al identify a human protein, cyclophilin A, that promotes the formation of infectious HIV-1 virions. Brian Cullen and Joseph Heitman, both of the Howard Hughes Medical Institute and Department of Genetics at Duke University Medical Center, question where the protein acts in the HIV-1 life cycle and how it exerts its effect. They suggest that cyclophilin A may play a role in virion morphogenesis, or that the protein may act during initial stages of the next viral replication cycle. One hypothesis about cyclophilin A is that it catalyses a "trans" to "cis" isomerization of a peptidyl-prolyl bond. Although the finding that an analogue of the immunosuppressive drug cyclosporin A--which inhibits proline isomerase activity--also blocks cyclophilin A incorporation and HIV-1 infectivity is inconsistent with the hypothesis, there are also data suggesting that cyclophilin A can act as a true protein-- independent of its action as a proline isomerase. Cullen and Heitman are pessimistic that cyclosporin A might be useful in the treatment of AIDS because the levels of the drug needed to prevent HIV-1 replication are also sufficient to block the enzymatic activity of the cyclophilins. In addition, because SIV--a similar infection found in simians--is not dependent on cyclophilin A for infectious virion production, HIV-1 may be able to mutate to a cyclosporin-A resistant form.

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