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Article

Disulfide bonds and membrane topology of the vaccinia virus A17L envelope protein.

Journal of virology - 1 Mar 2000

Betakova T, Moss B

Abstract excerpt

The envelope protein encoded by the vaccinia virus A17L open reading frame is essential for virion assembly. Our mutagenesis studies indicated that cysteines 101 and 121 form an intramolecular disulfide bond and that cysteine 178 forms an intermolecular disulfide linking two A17L molecules. This arrangement of disulfide bonds has important implications for the topology of the A17L protein and supports a...

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Identifiers

PMID: 10666276
DOI: 10.1128/jvi.74.5.2438-2442.2000
PMCID: PMC111727

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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