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. 1993 Mar;67(3):1676–1680. doi: 10.1128/jvi.67.3.1676-1680.1993

Disulfide bond formation in the human immunodeficiency virus type 1 Nef protein.

E Zazopoulos 1, W A Haseltine 1
PMCID: PMC237542  PMID: 8437238

Abstract

Substitution of alanine for cysteine residues of the human immunodeficiency virus type 1 LAI (BRU) and ELI Nef proteins was used to determine pairing of the cysteine residues present in each protein. The results show that under nonreducing conditions, alternative pairing of the cysteines occurs. The preferred pairing of cysteine residues of the LAI and ELI proteins differs. In the experimental system used, viruses carrying the ELI nef allele are found to express Nef proteins which accelerate virus replication. Mutation in critical cysteine residues of the protein reduce the rate of virus replication. In the same system, viruses harboring the LAI nef allele fail to replicate. These observations raise the possibility that differences in the observed biological activity of nef alleles may be attributed, at least in part, to differences in the secondary structure of the proteins.

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Selected References

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