ArticleProtein science : a publication of the Protein Society2010
Topology of the disulfide bonds in the antiviral lectin scytovirin.
Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Lectins and lectibodies: potential promising antiviral agents.Cellular & molecular biology letters · 2022Review
- Antiviral Cyanometabolites-A Review.Biomolecules · 2021Review
- Recent mass spectrometry-based techniques and considerations for disulfide bond characterization in proteins.Analytical and bioanalytical chemistry · 2018Review
- In silico analysis of the cyanobacterial lectin scytovirin: new insights into binding properties.Molecular biology reports · 2017Article
- Mass spectrometry-based methods for identifying oxidized proteins in disease: advances and challenges.Biomolecules · 2015Review
- Facilitating protein disulfide mapping by a combination of pepsin digestion, electron transfer higher energy dissociation (EThcD), and a dedicated search algorithm SlinkS.Molecular & cellular proteomics : MCP · 2014Article
- Antiviral lectins as potential HIV microbicides.Current opinion in virology · 2014Review
- Algal lectins as potential HIV microbicide candidates.Marine drugs · 2012Review
- HIV-1 enhancing effect of prostatic acid phosphatase peptides is reduced in human seminal plasma.PloS one · 2011Article
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9 authors.
Funding
Abstract
The antiviral lectin scytovirin (SVN) contains a total of five disulfide bonds in two structurally similar domains. Previous reports provided contradictory results on the disulfide pairing in each individual domain, and we have now re-examined the disulfide topology. N-terminal sequencing and mass spectrometry were used to analyze proteolytic fragments of native SVN obtained at acidic pH, yielding the assignment as Cys7-Cys55, Cys20-Cys32, Cys26-Cys38, Cys68-Cys80, and Cys74-Cys86. We also analyzed the N-terminal domain of SVN (SD1, residues 1-48) prepared by expression/oxidative folding of the recombinant protein and by chemical synthesis. The disulfide pairing in the chemically synthesized SD1 was forced into predetermined topologies: SD1A (Cys20-Cys26, Cys32-Cys38) or SD1B (Cys20-Cys32, Cys26-Cys38). The topology of native SVN was found to be in agreement with the SD1B and the one determined for the recombinant SD1 domain. Although the two synthetic forms of SD1 were distinct when subjected to chromatography, their antiviral properties were indistinguishable, having low nM activity against HIV. Tryptic fragments, the "cystine clusters" [Cys20-Cys32/Cys26-Cys38; SD1] and [Cys68-Cys80/Cys74-C-86; SD2], were found to undergo rapid disulfide interchange at pH 8. This interchange resulted in accumulation of artifactual fragments in alkaline pH digests that are structurally unrelated to the original topology, providing a rational explanation for the differences between the topology reported herein and the one reported earlier (Bokesh et al., Biochemistry 2003;42:2578-2584). Our observations emphasize the fact that proteins such as SVN, with disulfide bonds in close proximity, require considerable precautions when being fragmented for the purpose of disulfide assignment.
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