Open Access
PLoS ONE, volume 12, issue 1, pages e0170349
Derivative of Extremophilic 50S Ribosomal Protein L35Ae as an Alternative Protein Scaffold
Lomonosova Anna V
1
,
Ulitin Andrei B
2
,
Kazakov Alexei S
1
,
Mirzabekov Tajib A
3
,
Permyakov Eugene A.
1
,
2
Antherix, Pushchino, Moscow region, Russia
|
3
Antherix, Pushchino, Moscow region, Russia,
|
Publication type: Journal Article
Publication date: 2017-01-19
PubMed ID:
28103321
Multidisciplinary
Abstract
Small antibody mimetics, or alternative binding proteins (ABPs), extend and complement antibody functionality with numerous applications in research, diagnostics and therapeutics. Given the superiority of ABPs, the last two decades have witnessed development of dozens of alternative protein scaffolds (APSs) for the design of ABPs. Proteins from extremophiles with their high structural stability are especially favorable for APS design. Here, a 10X mutant of the 50S ribosomal protein L35Ae from hyperthermophilic archaea Pyrococcus horikoshii has been probed as an APS. A phage display library of L35Ae 10X was generated by randomization of its three CDR-like loop regions (repertoire size of 2×108). Two L35Ae 10X variants specific to a model target, the hen egg-white lysozyme (HEL), were isolated from the resulting library using phage display. The affinity of these variants (L4 and L7) to HEL ranges from 0.10 μM to 1.6 μM, according to surface plasmon resonance data. While L4 has 1–2 orders of magnitude lower affinity to HEL homologue, bovine α-lactalbumin (BLA), L7 is equally specific to HEL and BLA. The reference L35Ae 10X is non-specific to both HEL and BLA. L4 and L7 are more resistant to denaturation by guanidine hydrochloride compared to the reference L35Ae 10X (mid-transition concentration is higher by 0.1–0.5 M). Chemical crosslinking experiments reveal an increased propensity of L4 and L7 to multimerization. Overall, the CDR-like loop regions of L35Ae 10X represent a proper interface for generation of functional ABPs. Hence, L35Ae is shown to extend the growing family of protein scaffolds dedicated to the design of novel binding proteins.
Citations by journals
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Chemistry Letters
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Chemistry Letters
1 publication, 100%
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1
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Citations by publishers
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The Chemical Society of Japan
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The Chemical Society of Japan
1 publication, 100%
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1
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Lomonosova A. V. et al. Derivative of Extremophilic 50S Ribosomal Protein L35Ae as an Alternative Protein Scaffold // PLoS ONE. 2017. Vol. 12. No. 1. p. e0170349.
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Lomonosova A. V., Ulitin A. B., Kazakov A. S., Mirzabekov T. A., Permyakov E., Permyakov S. Derivative of Extremophilic 50S Ribosomal Protein L35Ae as an Alternative Protein Scaffold // PLoS ONE. 2017. Vol. 12. No. 1. p. e0170349.
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TY - JOUR
DO - 10.1371/journal.pone.0170349
UR - https://doi.org/10.1371%2Fjournal.pone.0170349
TI - Derivative of Extremophilic 50S Ribosomal Protein L35Ae as an Alternative Protein Scaffold
T2 - PLoS ONE
AU - Lomonosova, Anna V
AU - Ulitin, Andrei B
AU - Kazakov, Alexei S
AU - Mirzabekov, Tajib A
AU - Permyakov, Eugene A.
AU - Permyakov, Sergei
PY - 2017
DA - 2017/01/19 00:00:00
PB - Public Library of Science (PLoS)
SP - e0170349
IS - 1
VL - 12
PMID - 28103321
SN - 1932-6203
ER -
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@article{2017_Lomonosova,
author = {Anna V Lomonosova and Andrei B Ulitin and Alexei S Kazakov and Tajib A Mirzabekov and Eugene A. Permyakov and Sergei Permyakov},
title = {Derivative of Extremophilic 50S Ribosomal Protein L35Ae as an Alternative Protein Scaffold},
journal = {PLoS ONE},
year = {2017},
volume = {12},
publisher = {Public Library of Science (PLoS)},
month = {jan},
url = {https://doi.org/10.1371%2Fjournal.pone.0170349},
number = {1},
pages = {e0170349},
doi = {10.1371/journal.pone.0170349}
}
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MLA
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Lomonosova, Anna V., et al. “Derivative of Extremophilic 50S Ribosomal Protein L35Ae as an Alternative Protein Scaffold.” PLoS ONE, vol. 12, no. 1, Jan. 2017, p. e0170349. https://doi.org/10.1371%2Fjournal.pone.0170349.
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