Abstract:
:Protein modifications by intricate cellular machineries often redesign the structure and function of existing proteins to impact biological networks. Disulfide bond formation between cysteine (Cys) pairs is one of the most common modifications found in extracellularly-destined proteins, key to maintaining protein structure. Unpaired surface cysteines on secreted mammalian proteins are also frequently found disulfide-bonded with free Cys or glutathione (GSH) in circulation or culture, the mechanism for which remains unknown. Here we report that these so-called Cys-capping modifications take place outside mammalian cells, not in the endoplasmic reticulum (ER) where oxidoreductase-mediated protein disulfide formation occurs. Unpaired surface cysteines of extracellularly-arrived proteins such as antibodies are uncapped upon secretion before undergoing disulfide exchange with cystine or oxidized GSH in culture medium. This observation has led to a feasible way to selectively modify the nucleophilic thiol side-chain of cell-surface or extracellular proteins in live mammalian cells, by applying electrophiles with a chemical handle directly into culture medium. These findings provide potentially an effective approach for improving therapeutic conjugates and probing biological systems.
journal_name
J Biotechnoljournal_title
Journal of biotechnologyauthors
Zhong X,He T,Prashad AS,Wang W,Cohen J,Ferguson D,Tam AS,Sousa E,Lin L,Tchistiakova L,Gatto S,D'Antona A,Luan YT,Ma W,Zollner R,Zhou J,Arve B,Somers W,Kriz Rdoi
10.1016/j.jbiotec.2017.03.006subject
Has Abstractpub_date
2017-04-20 00:00:00pages
48-58eissn
0168-1656issn
1873-4863pii
S0168-1656(17)30104-9journal_volume
248pub_type
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